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 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019)

Biology PREAMBLE
Singapore-Cambridge General Certificate of Education This preamble sets out the approach, objectives, directions and philosophy of the H2 B_iology syllabus,

Advanced Level Higher 2 (2019) In Singapore, Biology education from Primary to A-Level has been Organised as a continuum in the following
manner:
(Syllabus 9744)
(a) from Primary 3 to Primary 6, students learn about how life works at the systems level

(b) from Lower Secondary Science to 0-Level Biology, students learn about how life works at the
physiological level

CONTENTS (c) at A-Level, students~e about how llfe works at the cellular and molecular levels while understanding
the implications of th a e macro level.
Page
PREAMBLE 2 The Biology syllabus~\'i loped as a seamless continuum from 0-Level to A-Level, without the need for
topics to be revism~evel. The 0-Level syllabus is foundational and thus should provide the necessary
INTROOUCTION 3 background for;t._'<tldy t A-Level. Students who intend to offer H2 Biology will therefore be assumed to have
knowledge~~ standing of 0-Level Biology, either as a single subject or as part of a balanced science
AIMS 3 course.

PRACTICES OF SCIENCE 4 important fields of biology have emerged through recent advancements in life sciences. Vast
:nowledge have been generated, as evident from the sprouting of scientific journals catering to
CURRICULUM FRAMEWORK 6 as of research. As such, this syllabus refines and updates the content knowledge of the previous
ASSESSMENT OBJECTIVES (9648) so that students can keep_ up to date with knowledge that is relev_ant for their participation in
7
hnology-driven economy.
SCHEME OF ASSESSMENT 9
ADDITIONAL INFORMATION 10
STRUCTURE OF SYLLABUS 11
PRACTICAL ASSESSMENT 21
MATHEMATICAL REQUIREMENTS 24
TEXTBOOKS AND REFERENCES
GLOSSARY OF TERMS
-- ◊

C'
\:fl) Slngaporo Examinations and Assessmont Board '1 f~~~R~!
® MOE & UCLES 2017
1 2
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 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019)
INTRODUCTION
Candidates will be assumed to have knowledge and understanding of Qwlevel Biology, as a single subject or
as part of a balanced science course.
The syllabus has been arranged in the form of Core and Extension content to be studied by all candidates.
The syllabus places emphasis on the applications of biology and the impact of recent developments on the
needs of contemporary society.
Experimental work is an important component and should underpin the teaching and learning of biology.
The value of learning H2 Biology ultimately hinges on the development of a scientific mind and disposition
while addressing the broader questions of what life is and how life is sustained. The Science Curriculum
Framework developed by the Ministry of Education elaborates on the development of the scientific mind and
disposition. Through the study of the H2 Biology course, students will be prepared for life science.-related
courses at university and. consequently, careers that are related to this field,
AIMS
The syllabus aims to;
1. provide students with an experience that develops their interest in biology and builds the knowledge,
skills and attitudes necessary for further studies in related fields
2. enable students to become scientifically literate citizens who are weH--prepared for the challenges of the
21st century
3. develop in students the understanding, skills, ethics and attitudes relevant to the Practices of Science,
including the following:
3.1 understanding the nature of scientific knowledge
3.2 demonstrating science inquiry skills
3.3 relating science and society
4. address the broader questions of what life is and how life is sustained, including:
4.1 understanding life at the cellular and molecular levels, and making connections to how th
micro--systems interact at the physiological and organismal levels
4.2 recognising the evolving nature of biological knowledge
4.3 stimulating interest in and demonstrating care for the local and global environm
3 4
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9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019)
PRACTICES OF SCIENCE
Science as a discipline is more than the acquisition of a body of knowledge (e.g. scientific facts, concepts,
laws and theories); it is a way of knowing and doing. II includes an understanding of the nature of scientific
knowledge and how this knowledge is generated, established and communicated. Scientists rely on a set of
established procedures and practices associated with scientific inquiry to gather evidence and test their
ideas on how the natural world works. However, there is no single method and the real process of science is
often complex and iterative, following many different paths. While science is powerful, generating knowledge
that forms the basis for many technological feats and innovations, it has limitations.
The Practices of Science are explicitly articulated in the syllabus to allow teachers to embed them as
learning objectives in their lessons. Students' understanding of the nature and limitations of science and
scientific inquiry are developed effectively when the practices are taught in the context of relevant science
content. Attitudes relevant t i e ·ence
s such as inquisitiveness, concern for accuracy and precision, objectivity,
integrity and perseverance u e emphasised in the teaching of these practices where appropriate. For
example, students leamin.tU$.c1l
c ce should be introduced to the use of technology as an aid in practical work
or as a tool for the inte~n of experimental and theoretical results.
1.
,d that science is an evidence-based, modeJ..building enterprise concerned with the
rld
Understand that the use of both logic and creativity is required in the generation of scientific
knowledge
Recognise that scientific knowledge is generated from consensus within the community of
scientists through a process of critical debate and peer review
1.4 Understand that scientific knowledge is reliable and durable, yet subject to revision in the light of
new evidence
2. Demonstrating Science Inquiry Skills
2.1 Identify scientific problems, observe phenomena and pose scientific questions/hypotheses
2.2 Plan and conduct investigations by selecting the appropriate experimental procedures, apparatus
and materials, with due regard for accuracy, precision and safety
2.3 Obtain, organise and represent data in an appropriate manner
2.4 Analyse and interpret data
2.5 Construct explanations based on evidence and justify these explanations through sound reasoning
and logical argument
2.6 Use appropriate models1 to explain concepts, solve problems and make predictions
2.7 Make decisions based on evaluation of evidence, processes, claims and conclusions
2.8 Communicate scientific findings and information using appropriate language and terminology
1
A model is a representation of an Idea. an object, a process or a system that ls used to describe and explain
phenomena that cannot be experienced directly. Models elcist in different forms, from the concrete, such as physical
scale models. to the abstract, such as diagrams or mathematical expressions. The use of models involves the
understanding that an models contain approximations and assumptions limiting their validity and predictive power.
 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019) 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019)

3. Relating Science and Society

CURRICULUM FRAMEWORK
3.1 Recognise that the application of scientific knowledge to problem solving could be influenced by
other considerations such as economic, social, environmental and ethical factors
The rapid progress in the field cK life sciences poses a challenge for Biology education, especiaUy in terms of
3.2 Demonstrate an understanding of the benefits and risks associated wilh the application of science designing a framework that integrates fundamental knowledge, skills and attitudes. With this in mind, this
to society syllabus has adopted a framework that will chart a new direction for Biology education. An overview of this
framework is depicted in Fig. 1: H2 Biology Curriculum Framework.
3.3 Use scientific principles and reasoning to understand, analyse and evaluate real~wor!d systems, as
well as to generate solutions for problem solving

Practices of Science
Nat.ure of Scientific l<nowlC?dgc I Sdcmcc Inquiry Skills I Scii;ncC! and_Socie:tY_'I

·I: !~:Tut;N:'.:~~J~~;~;~:~ :/'.[IE

r-•TheStructureof l 'ill
Nucleic Adds &
Gene Expression Adaptation
ffl
• Biomolecules • Organisation of Environment & • Evolution &
ofUfe & Genomes organisms Biodiversity,
CeUular ~ Control of Gl:!ne • Communication Species &
Transport Expression &. Equilibrium Speciation
• Proteins • DNA Mutations in Organisms
• Stem Cells • The Cell Cyc:! e
• Inheritance

Extension Topics: {A) Infectious Diseases;

(B) Impact of Climate Change on Animals and Plants

Fig. 1: H2 Biology Curriculum Framework

◊ The Practices of Science are common to the natural sciences of Physics, Chemistry and Biology. These
practices highlight 1he ways of thinking and doing that are inherent in the scientific approach, with the aim of
equipping students with 1he understanding, skills, and attitudes shared by the scientific disciplines, including
an appropriate approach to ethical issues.

The content in this H2 Biology syllabus is organised around four Core Ideas of Biology and two Extension
Topics. The Leaming Experiences1 refer to a range of learning opportunities selected by teachers to link the
biology con1ent of the Core Ideas and Extension Topics with the Practices of Science, to enhance students'
learning of the concepts. Rather than being mandatory, teachers are encouraged to incorporate Leaming
Experiences that match the interests and abilities of their students and provide opportunities to illustrate and
exemplify the Practices of Science, where appropriate. Real~world contexts can help illustrate the biology
concepts and their applications. Experimental activities and ICT tools can also be used to build students'
understanding.

The two Extension Topics are based on important emerging biological issues impacting both the local and
global contexts. They require students to demonstrate assimilation of the Core Ideas and extend their
knowledge and understanding to real--world challenges. Furthermore, Extension Topics will equip students
with the necessary knowledge and process skills to make informed decisions about scientific issues. In line
with this, the two Extension Topics chosen are (A) Infectious Diseases and (B} Impact of Climate Change on
Animals and Plants. Both Extension Topics take up about 10% of the total H2 Biology curriculum.

Students are expected to study all four Core Ideas and both Extension Topics.

1
Leaming Experiences can be found in the Teaching and Leaming Syllabus.

5 6
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 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019) 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019)

C Experimental skills and investigations

ASSESSMENT OBJECTIVES
Candidates should be able to:
The Assessment ObjectWSs listed below reflect those parts of the Aims and Practices of Science that will be
assessed. 1. follow a detailed sequence of instructions or apply standard techniques

2. devise and plan investigations which may include constructing and/or testing a hypothesis and select
A Knowledge with understanding
techniques, apparatus and materials
Candidates should be able to demonstrate knowledge with understanding in relation to:
3. use techniques, apparatus and materials safely and effectively
1. scientific phenomena, facts, laws, definitions, concepts and theories
4. make and record observations, measurements and estimates
2. scientific vocabulary, terminology and conventions (including symbols, ·quantities and units)
5. interpret and evaluate observations and e.xperimental data
3. scientific instruments and apparatus, including techniques of operation 1and aspects of safety
6. evaluate methods and v u e s , and suggest possible improvements.
4. scientific quantities and their determination

5. scientific and technological applications with their social, economic and environmental implications.

The syllabus content defines the factual materials that candidates need to recall and explain. Questions
testing the objectives above will often begin with one of the following words: define, state, name, describe,
·G
~
o'
explain or outline (see the Glossary of Tenns).

8 Handli_ng, applying and evaluating information

Candidates should be able (in words or by using symbolic, graphical and numerical forms of presentation) to:

1. locate, select, organise, interpret and present information from a variety of sources

2. handle information, distinguishing the relevant from the extraneous

3. manipulate numerical and other data and translate information from one form to another

4. present reasoned explanations for phenomena, patterns, trends and relationships

5. make comparisons that may include the identfficalion of similarities and differences

6. analyse and evaluate information to identify patterns, report trends, draw inferences, report conclusions
and construct arguments
◊
7. justify decisions, make predictions and propose hypotheses

8. apply knowledge, including principles, to novel situations

9. use skills, knowledge and understanding from different areas of Biology to solve proble1

10. organise and present information, ideas and arguments clearly and coherently,
language.

These Assessment Objectives above cannot be precisely specified in the syllab

questions testing such skills are often based on information which is unfamiliarf<,1~
answering such questions, candidates are required to use principles and concept&,that are within the
syllabus and apply them in a logical, reasoned or deductive manner to a novel situation. Questions testing
these objectives may begin with one of the following words: discuss, predict, suggest. ca/cu/ate or detennine
(see the Glossary of Terms).

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 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019) 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019)

SCHEME OF ASSESSMENT Weighting of Assessment Objectives

~, a1 ""W:iox, ~'Zl87~~w.~ •'/%IIJ.~ji~@\\"c1i.it•.'lr,~ji;0P,7-,\,ffl~Ar

All candidates are required to enter for Papers 1, 2, 3 and 4. m1 lm!!.ij~J1§.~.M t~~~.!~Mi,,,ggiaag,ii;i,,,,.,,,,w
A I Knowledge with understanding 32 Papers 1, 2, 3
n~'.®tl~~
~~1~l1 ~.~~,,,f~
~¥5tifll
fo B I Handling, applying and evaluating 48
Papers 1, 2, 3
Multiple Choice 15 30 information

2 Structured Questions 2h 30 100

C I Experimental skills and investigations 20 Paper4

3 Long Structured and Free-response Questions 2h 35 75

4 !Practical 2 h 30min 20 55

Paper 1 (1 h, 30 marks) "

'draw extensively on concepts from the physical sciences. It is desirable therefore
This paper will consist of 30 compulsory multiple choice questions. All questions will be of the direct choice :urse, students should have knowledge of the following topics, sufficient to aid
type with 4 options. ,gical systems. No questions will be set directly on them except where relevant to the
ing Outcome.
Paper2 (2h, 100 marks)
This paper will consist of a variable number of structured questions, all compulsory, including data-based or agnetic spectrum
comprehension-type questions. These include questions which require candidates to integrate knowledge Iges {potential energy, activation energy, chemical bond energy)
and understanding from different areas of the syllabus. 1les, atoms, ions, electrons
,cids, bases, pH, buffers
Paper 3 (2 h, 75 marks) Isotopes, including radioactive isotopes
This paper will consist of a variable number of long structured questions, all compulsory, including
Oxidation and reduction
data-based or comprehension-type questions and one free-response question of 25 marks. These include
Hydrolysis, condensation
questions that assess the higher-<>rder skills of analysing, making conclusions and evaluating information
and require candidates lo integrate knowledge and understanding from different areas of the syllabus.
Nomenclature
Section A (50 marks) will comprise two or more compulsory long structured questions. There will be one or
Candidates will be expected to be familiar with the nomenclature used in the syllabus. The proposals in
more stimulus materials which may be taken or adapted from a source such as a scientific journal or book
"Signs, Symbols and Systematics" (The Association for Science Education Companion to 16-19 Science,
which may not necessarily relate directly to the content of the syllabus. Questions may require candidates to
2000) and the recommendations on terms, units and symbols in •Biological Nomenclature" (2009) published
explain terms used in the passage, analyse data, justify decisions, perform calculations and draw
by the Institute of Biology, in conjunction with the ASE, will generalty be adopted although the traditional
conclusions based on information in the stimulus material.
names sulfate, sulfite, nitrate, nitrite, sulfurous acid and nitrous acid will be used in question papers. Sulfur
(and all compounds of sulfur) will be spelt with f (not with ph) in question papers. However, candidates can
Section B (25 marks) will comprise two free-response questions, from which candidates will choose one,
use either spelllng in their answers.
The quality of scientific argumentation and written communication will be given a percentage of the m
available. • Disallowed Subject Combinations
Paper 4 (2 h 30 min. 55 marks)
Candidates may not simultaneously offer Biology at H1 and H2 Levels.
This paper will assess appropriate aspects of objectives C1 to CS in the following skill areas:
Units and Significant Figures
Planning {P}
.,lf \'\
re&..'
• Manipulation, measurement and observation (MMO) Candidates should be aware that misuse of units and/or significant figures, e.g. failure to quote units where
• Presentation of data and observations (PDO) necessary, the inclusion of units in quantities defined as ratios or quoting answers to an inappropriate
• Analysrs, conclusions and evaluation (ACE) number of significant figures, is liable to be penalised.
The assessment of skill area P wrll have a weighting of 5%, and the skill areas~, PDQ and ACE will
have a weighting of 15%. Candidates will require access to apparatus, as stated m the Confidential
Instructions. For some questions, candidates may be allocated a specific time for access to the apparatus.
Paper 4 may also include data handling/interpretation questions that do not require apparatus, in order to
lest the skill areas of PDQ and ACE.

Candidates are NOT allowed to refer to notebooks, textbooks or any other information in the Practical
Examination.

9 10
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 9744 BIOLOGY GCEADVANCED LEVEL H2 SYLLABUS (2019} 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019)

STRUCTURE OF SYLLABUS ,. CORE IDEAS

The Cell and Biomolecules of Life

The syllabus is divided into two parts: Core Ideas and Extension Topics, to be studied by all candidates.
Content
I. Core Ideas. There are 4 Core Ideas:
The cell theory
1. The Cell and Biomolecules of Life
Outline functions of membrane systems and organelles in cells
2. Genetics and Inheritance The structure of a typical bacterial cell
3. Energy and Equilibrium The structures of biomolecules and their functions
The structural components of viruses
4. Biological Evolution.
The fluid mosaic model of membrane structure
II. Extension Topics. There are 2 Extension Topics:
Stem cells
A. Infectious Diseases

B. Impact of Climate Change on Animals and Plants.

II theory with the understanding that cells are the smallest unit of life, all cells come from
cells, and living organisms are composed of cells

,ret and recognise drawings, photomicrographs and electronmicrographs of the following

membrane systems and organelles: rough and smooth endoplasmic reticulum, Golgi body,
mitochondria, ribosomes, lysosomes, chloroplasts, cell surface membrane. nuclear envelope,.
centrioles, nucleus and nucleolus (for practicitl assessment, candidates may be required to operate a
light microscope, mount slides and use a graticule)

(c) outline the functions of the membrane systems and organelles listed in (b)

{d) describe the structure of a typical bacterial cell (small and unicellular, peptidoglycan cell wall, circular
DNA, 70S ribosomes and lack of membrane-bound organelles)

(e) describe the structural components of viruses, Including enveloped viruses 'and bacteriophages, and
interpret drawings and photographs of them
¢
(Q discuss how viruses challenge the cell theory and concepts of what is considered living

{g) describe the structure and properties of the following monomers:

et-glucose and j3-glucose (in carbohydrates)
il. glycerol and fatty acids (in lipids)
m. amino acids (in proteins) (knowledge of chemical formulae of specific R-groups of different amino
acids is not required)

(h) describe the formation and breakage of the following bonds:

glycosidic bond
ii. ester bond
m. peptide bond

11 12

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 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019) 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019)

(i) describe the structures and properties of the following biomolecules and explain how lhese are related 2 Genetics and Inheritance
to their roles in living organisms:
Content
starch (including amylase and amylopectin)
ii. cellulose DNA- structure and function
iii, glycogen Central Dogma - DNA to RNA, RNA to protein
iv. triglyceride The structure of eukaryotic chromatin
v. phospholipid The genetics of viruses

G) explain the fluid mosaic model and the roles of the constituent biomolecules (including phospholipids, The genetics of bacteria
proteins, glycolipids, glycoproteins and cholestero0 in cell membranes Genome organisation at the DNA level
""""' ,n
(k) outline the functions of membranes at the surface of cells and membranes within the cell

(1) explain how and why different substances move across membranes through simple diffusion, osmosis,
facilitated diffusion, active transport, endocytosis and exocytosis

(m) explain primary structure, secondary structure, tertiary structure and quaternary structure of proteins,
and describe the types of bonds that hold the molecule in shape (hydrogen, ionic and disulfide bonds, ing of chromosome number and variation
and hydrophobic interactions) •f meiosis on chromosome number and variation
(n) explain the effects of temperature and pH on protein structure
(o) describe the molecular structure of the following proteins and explain how the structure of each protein The passage of information from parents to offspring
relates to the function it plays: Genotypes and phenotypes
haemoglobln (transport) Dihybrid crosses
ii. collagen (structural) Linkage and crossing-over
iii. G•protein linked receptor (signalling)
Interaction between loci
(knowledge of details of the number of amino acids and types of secondary structures present is not
The effect of genotype and environment on the phenotype
required)
(p) explain the mode of action of enzymes in terms of an active site, enzyme-substrate complex, lowering Learning Outcomes
of activation energy and enzyme specificity using the lock.and-key and induceMit hypotheses
Candidates should be able to:
(q) investigate and explain the effects of temperature, pH, enzyme concentration and substrate
concentration of an enzyme-catalysed reaction by measuring rates of formation of products (e. (a) describe the structure and rotes of DNA and RNA (tRNA, rRNA and mRNA) (knowledge of
◊
measuring gas produced using catalase) or rate of disappearance of substrate {e.g. using a mitochondrial DNA is not required)
starch and iodine)
(b) describe the process of DNA replication and how the end replication problem arises
(,) describe the structure of competitive and non•competitive inhibitors with reference to
ofthe inhibitor (c) describe how the information on DNA is used to synthesise polypeptides in prokaryotes and
eukaryotes (description of the processes of transcription, formation of mRNA from pre-mRNA and
(s)
rate of enzyme activity i..'
explain the effects of competitive and non•competitive inhibitors (including all~~ibitors) on the
(d)
translation Is required)

(!) describe the unique features of zygotic stem cells, embryonic stem cetl:Pa~~d stem cells,
correctly using the terms totipotency (zygotic stem cells which have th£;ilii(ity to differentiate into any
cell type to form whole organisms and so are also pluripotent and multi~ni), pluripotency
(embryonic stem cells which have the ability to differentiate into almost any cell type to fonn any organ
and so are not totipotent but are multipotent) and multipotency (blood stem cells which have the ability
to differentiate into a limited range of cell types and so are not pfuripotent or totipotent)
describe the structure and organisation of viral, prokaryotic and eukaryotic genomes (including
DNNRNA, single--/double-stranded, number of nucleotides, packing of DNA, linearity/circularity and
presence/absence of intrans)
(e) describe how the genomes of viruses are inherited through outlining the reproductive cycles of:
bacteriophages that reproduce via a lytic cycle only, including T4 phage

(u) explain the normal functions of stem cells in a Jiving organism, including embryonic stem cells and ii. bacteriophages that reproduce via lytic and lysogenic cycles, including lambda phage
blood stem cells iii. enveloped viruses, including influenza
(v) discuss the ethical implications of the application of stem cells in research and medical appfications iv. retroviruses, including HIV
and how human induced pluripotent stem cells (iPSCs) overcome some of these issues (procedural
detaITs of how iPSCs are formed are not required). (~ describe how variation in viral genomes arises, including antigenic shift and antigenic drift

Use the knowledge gained in this section tn new situations or to solve related problems.

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 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019) 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019)

(g) outline the mechanism of asexual reproduction by binary fission in a typical prokaryote and describe (u) explain the terms: locus, allele, dominant, ~cessive, codominant, incomplete dominance,
how transformation, transduction and conjugation (including the roJe:of F plasmids but not Hfr) give homozygous, heterozygous, phenotype, genotype and llnkage
rise to variation in prokaryotic genomes
(v} explain how genes are inherited from one generation to the next via the germ cells or gametes
(h) describe the structure and function of non-coding DNA in eukaryotes (i.e. portions that do not encode
protein or RNA. including intrans, ce'ntromeres, telomeres, promoters, enhancers and silencers) (w) explain how genotype is Jinked to phenotype
(knowledge of transposons, satellite DNA, pseudo-genes and duplication of segments is not required)
(x) use genetic diagrams to solve problems in dihybrid crosses, including those involving codominance,
(i) explain how gene expression in prokaryotes can be regulated, through the concept of simple operons incomplete dominance. multiple alleles. sex linkage, autosomal linkage and epistasis
(including lac and trp operons), including the role of regulatory genes, and distinguish between
inducible and repressible systems (knowledge of attenuation of the trp operon is not required) (y) use genelic diagrams to solve problems involving test crosses
(i) e.xplain how differential {Le. spatfal and temporal) gene expression ill eukaryotes can be regulated at (z) explain the meaning of the terms linkage and crossing-over and explain the effect of linkage and
different levels: crossing-.over on the phenotypic ratios from dihybrid crosses
chromatin level (histone modification and DNA methylation) (aa) ·een loci (epistasis) and predict phenotypic ratios in problems involving
ii. transcriptional level (control elements, such as promoters, silencers and enhancers, and expected ratio for various types of epistasis is not required; focus of this
proteins, such as transcription factors and repressors) lving)
iii. post-transcriptional level (processing of pre-mRNA in terms of splicing, polyadenylation and 5' (bb) ,nment may affect the phenotype {including how diet affects the differentiation of
capping) ·
how temperature affects fur colour of Himalayan rabbits)
iv. translational level (half-life of RNA and initiation of translation)
difference between genetic variation that is continuous {many, additive genes control a
v. post-translational level (biochemical modification and protein degradation) "istic) and genetic variation that is discontinuous (one or a few genes control a characteristic)
{k) describe the principles and procedures of these molecular techniques: ( ; ~ ~ ~ e chi-squared test to test the significance of differences between observed and expected
i. polymerase chain reaction (including its advantages and limitations) ~uresults.
ii. gel electrophoresis '),. Isa the knowledge gained in this section in new situations or to solve related problems.
iii. Southern blotting and nucleic acid hybridisation
Energy and Equilibrium
(I) explain what is meant by the terms gene mutation and chromosom81 aberration. For gene mutation,
knowledge of how substitution, addition and deletion could change the amino acid sequence (including Content
frameshift) is required. For chromosomal aberration. knowledge of numerical aberration {including
aneupJoidy, as in the case of trisomy 21, i.e. Down syndrome) and structural aberration (including The need for energy in living organisms
translocation, duplication, inversion and deletion) is required
Photosynthesis as an energy-trapping process
(m) explain how gene mutations can result in diseases (including sickle cell anaemia)
Respiration as an energy~releasing process
{n) describe the events that occur during the mitotic cell cycle and lhe main stages of mitosis (inclu, Aerobic respiration
◊
the behaviour of chromosomes, nuclear envelope, eel! membrane ahd centrioles)
Anaerobic respiration
(o) e:xplain the significance of the mitotic cell cycle (including growth, repair and asexual reproJ An overview of cell signaUing and communication
the need to regulate it tightly (knowledge that dysregulation of checkpoints of cell divisi1 signal reception and the initiation of transduction
uncontrolled cell division and cancer is required, but detail of the mechanism is no signal 1ransduclion pathways
cellular responses to signals
(p) identify the causative factors, including genetic, chemical carcinogens, ionising
immunity, which may increase the chances of cancerous growth Learning Outcomes
(q) explain how the loss of function mutation of tumour suppressor genes, i: Candidates should be able to:
function mutation of pro to-oncogenes, including ras, results in uncoOtro
(a) identify components of chloroplasls and mitochondria in drawings, photomicrographs and
(,) describe the development of cancer as a mulli•step process that includes accumulation of mutations. e\ectronmicrographs
angiogenesis and metastasis
(b) explain the absorption and action spectra of photosynthetic pigments
(s) describe the events that occur during the meiotic cell cycle and the i'nain stages of meiosis (including
the behaviour of chromosomes, nuclear envelope, cell membrane and centrioles) (names of the main (c) with reference to the chloroplast structure, describe and explain how light energy is harnessed and
stages are expected, but not the sub-divisions of prophase) converted into chemical energy during the light-dependent reactions of photosynthesis

(t) explain the significance of the meiotic cell cycle (including how meiosis and random fertilisation can (d) outline the three phases,of the CaMn cycle in C3 plants: {i) CO2 fixation, (ii) PGA reduction and
lead to variation) (iii) ribulose bisphosphate {RuBP) regeneration, indicating the roles of rubisco, ATP and reduced
NADP in these processes that ultimately allow synthesis of sugars

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 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019) 9744 BIOLOGY GCEADVANCED LEVEL H2 SYLLABUS (2019)

(e) discuss limiting factors in photosynthesis and cariy out investigations on the effect of limiting factors 4 Biological Evolution
such as temperature, light intensity and carbon dioxide concentration on the rate of photosynthesis
Content
(f) outline the process of glycolysis, highlighting the location, raw materials used and products formed
(knowledge of details of the intermediate compounds and isomerisation is not required} The concept of the species
The neo--Darwinian revolution
(g) ouUine the processes of the link reaction and Krebs cycle, highlighting the location, raw materials used
and products formed (in terms of dehydrogenation and decarboxylation) Variation, natural selection and evolution

(h) outline the process of oxidative phosphorylation including the role of oxygen and the electron transport Evidence of evolution
chain in aerobic respiration (names of complexes in the ETC are not required) Classification
(i) explain the production of a small yield of ATP from respiration trl anaerobic conditions in yeast and in Learning Outcomes
mammalian muscle tissue

OJ explain the significance of the formation of ethanol in yeast and lactate in mammals in the
regeneration of NAO {a) explain why ~fan (as a result of mutation, meiosis and sexual reproduction) is important in natural
selectionr ~
(k) investigate the effect of factors such as substrate concentration, type of substrate and temperature on
the rate of respiration {b) ~'Yexamples, how environmental factors act as forces of natural selection

0) outline chemiosmosis in photosynthesis and respiration (names of complexes in the ETC are not the role of natural selection in evolution
required)
lain why the population is the smallest unit that can evolve
(m) outline the main stages of cell signalling:
explain how genetic variation (including recessive alleles) may be preserved in a natural population
ligand-receptor Interaction
define biological evolution as descent with modification and explain the link between micro-evolution
ii. signal transduction {phosphorylation cascade and signal amplification)
and macro-evolution
m. cellular response (change in gene expression)
(g) explain how evidence based on homologies identified in biochemical data (molecular homologies) and
(knowledge of inlracel!ular receptors is not required)
the fossil record (anatomical homologies), together with biogeography, supports Darwin's theory of
evolution
(n) explain the roles and nature of second messengers (including cyclic AMP)
(h) explain the various concepts of the species (biological, ecological, morphological, genetic and
(o) explain the role of kinases and phosphatases in signal amplification
phylogenetic concepts)
{P) outline how insulin and glucagon regulate the concentration of blood glucose through the respective
(i) define biological classification as the organisation of species according to shared characteristics and
tyrosine kinase receptor and G-protein linked receptor. (The outline should be limited to descriL'
describe how evolutionary relationship is established
how the ligand induces a conformational change in a membrane-Oound receptor to trigger d 1

signalling pathways that elicit physiological changes in blood glucose concentration. Details
0) explain how new species are formed with respect to geographical isolation (allopatric speciation) and
different second messengers and specific kinases activated in the pathway are not required.
behavioural or physiological isolation within the same geographical location (sympatric speciation)
Use the knowledge gained in this section in new situations or to solve related problems.
(k) define phylogeny as the organisation of species to show their evolutionaiy relationships

{I) explain the importance of the use of genome sequences in reconstructing phylogenetic relationships
and state the advantages of molecular methods, including multiple sequence alignment (nucleotide
and amino acid), fn classifying organisms.

Use the knowledge gained in this section in new situations or to solve related problems.

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 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019) 9744 BIOLOGY GCEADVANCED LEVELH2 SYLLABUS (2019)

II, EXTENSION TOPICS B Impact of Climate Change on Animals and Plants

A Infectious Diseases Content
Content Human activities that contribute to climate change
The immune system- adaptive and innate Effects of climate change on the environment, plants and animals
Genetic recombination Impact on biodiversity, biomedicines and the global food supply
Mode of viral and bacterial infections Viral dengue disease in humans and how global warming affects its spread
Vaccination and modes of action of antibiotics Leaming Outcomes
Learning Outcomes Candidates should be able to:
Candidates should be able to: (a) man activities over the last few centuries that have contributed to climate
ea¼mission of greenhouse gases (limited to CO2 and methane) including
(a) describe the specific (adaptive) and non-specific (innate) immune systems including active and iriked to increasing energy usage, clearing of forests and food choices
passive, natural and acquired immunity of meat)
(b) outline the roles of B lymphocytes, T lymphocytes, antigen-presenting cells and memory cells in (b) ,f climate change as a result of greenhouse gas emissions including the melting of
specific primary and secondary immune responses rislng sea levels, stress on fresh water supplies, heat waves, heavy rains, death of
migration of fishes and insects, and release of greenhouse gases in frozen organic matter
(c) explain the relationship of the molecular structure of antibodies to their functions, using lgG as an
example how climate change affects plant distribution (vertical and latitude) and plant adaptations,
u-ding morphology and physiology
(d) explain how genetic recombination during development results in millions of different antibody
molecules (including somatic recombination, hyper-mutation and cl6ss switching) discuss the consequences to the global food supply of increased environmental stress resulting from
climate change, including the effects on plants and animals of increased temperature and more
(e) discuss how vaccination can control disease (including the eradication of small pox), limited to extreme weather conditions
vaccination stimulates immunity without causing the disease and vaccination of a high enough
proportion of the population can break the disease transmission cycle (e) explain how temperature changes impact insects, including increased temperature leading to
increased metabolism and the narrow temperature tolerance of insects
(f} discuss the benefits and risks of vaccination
(f) outline the life-cycle of Aedes aegypti as an example of a typical mosquito vector
(g) explain how viruses; including influenza and HIV, cause diseases in· humans through the disruption of
host tissue and functions (including HIV and T helper cells, influenza and epithelial cells of the (g) outline the development of viral dengue disease in humans, including host-pathogen interactions,
respiratory tract) human susceptibility to the virus, pathogen virulence, transmission and drug resistance
(h) explain the mode of transmission and infection of bacterial pathogens, using Myaobacterium (h) explain how global wanning affects the spread of mosquito-borne infectious diseases, including
tuberr:ulosis as an example malaria and dengue, beyond the tropics
$

(i) describe the modes of action of antibiotics, including penicillin, on bacteria, (i) discuss the effects of increased environmental stress (lncluding increased temperatures and more
extreme weather conditions) as a result of global climate change, on habitats, organisms, food chains
Use the knowledge gained in this section in new situations or to solve related problems. and niche occupation

(j) discuss how climate change affects the rich biodiversity of the tropics including the potential loss of
this rich reservoir for biomedicines and genetic diversity for food.

Use the knowledge gained in this section in new situations or to solve related problems.

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 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019) 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019)

PRACTICAL ASSESSMENT
Scientific subjects are, by their nature, experimental. It is therefore important that, wherever possible, the
candidates carry out appropriate practical work to support the learning of this subject and to develop the
expected practical skills.
Paper 4 Practical
This paper is designed to assess candidates' competence in those practical skills which can realistically be
assessed within the context of a formal practical assessment
Candidates wm be assessed in the following skill areas:
{a) Planning (P)
Candidates should be able to:
• define the question/problem using appropriate knowledge and understanding
give a clear, logical account of the experimental procedure to be followed
describe how the data should be used in order to reach a conclusion
assess the risks of the experiment and describe precautions that should be taken to keep risks to a
minimum.
Wrthin the Scheme of Assessment, Paper 4 is weighted to 20% of the Higher 2 assessment. It is therefore
recommended that the schemes of work include learning opportunities that apportion a commensurate
amount of time for the development and acquisition of practical skills. The guidance for practical work, which
is published separately, will provide examples of practical activities.
Candidates are NOT allowed to refer to notebooks, textbooks or any other information 1n the Practical
examination.
Apparatus List
This list given below has been drawn up in order to give guidance to Centres concerning the apparatus that
is expected to be generally available for examination purposes. The list is not intended to be exhaustive and
practical examinations may require additional apparatus and materials that will be specified in the
Confidential Instructions, e.g. enzymes, indicators, plastic straws, etc. Furthermore, general laboratory
glassware and items l h =commonly
t regarded as standard equipment in a Biology laboratory (e.g.
Bunsen burners, tripods uze, thermostatic waler-baths, safety goggles, disposable gloves, paper
towels, etc.) are not in - e ·n this list
1e rate of allocation is ·per candidate".
1- and low-power objective lens and fitted eyepiece graticule (2 candidates to 1)
(2 candidates to 1)
ides and coverslips

(b) Manipulation, measurement and observation (MMO)

Candidates should be able to: mm

demonstrate a high level of manipulative skills in all aspects of practical activity ; (e.g. 1 cni3, 5cm3, 10cm3)
make and record accurate observations with good details and measurements to an appropriate Droppers or Pasteur pipettes
degree of precision Measuring cylinders
make appropriate decisions about measurements or obseNations Beakers
recognise anomalous observations and/or measurements (where appropriate) with reasons Petri dishes
indicated. Test.tubes (some ofwhich should be heat-resistant)
Test-tube rack and holder
(c) Presentation of data and observations (PDO) Boiling tubes
Bomng tube rack
Candidates should be able to: Small containers
present all information in an appropriate form Glass rod
Corks or rubber bungs to fit test-tubes and boiling tubes
manipulate measurements effectively in order to identify trends/patterns
Knife or scalpel
present all quantitative dala to an appropriate number of decimal places/significant figures. ' -' - 0
Forceps
Cork borer(2 candidates to 1)
(d) Analysis, conclusions and evaluation {ACE)
Capillary tubes
Vaseline/petroleum jelly (or similar)
Candidates should be able to:
Specimen tubes
• analyse and interpret data or observations appropriately in relation to the task Visking tubing
draw conclusion(s) from the interpretation of experimental data or observationrafrd,linderlying Silicone tubing
principles ~ "-..J TheRTiometer: -10°C to +110°C
make predictions based on their data and conclusions ~' Stopwatch
identify significant sources of errors, limitations of measurements an~F..\!:ll"rimental procedures White tile
used, and explain how they affect the final result{s) fu · Filter paper and funnel
state and explain how signfficant errors/limitations may be overcome !edtlced, as appropriate, Mortar and pestle (2 candidates to 1)
including how experimental procedures may be improved. Spatulas
Glass marker pen
One or more of the questions may incorporate some assessment of ski!! P, set in the context of the syllabus Cotton wool
content, requiring candidates to apply and integrate knowledge and understanding from different sections of Black paper
the syllabus. These questions may also require the treatment of given experimental data to draw a relevant Aluminium foil
conclusion and analyse the proposed plan. Balance to 0.01 g (to be made accessible to candidates)
Retort stand and clamp
The assessment of skills MMO, PDQ and ACE will also be set mainly in the context of the syflabus content Bench lamp
and will require access to apparatus, as stated in the Confidential Instructions. For some questions, Distilled or deionised water
candidates may be allocated a specific time for access to the apparatus. The assessment of PDQ and ACE Microfuge tubes and rack
may also include questions on data-analysis which do nOt require practical equipment and apparatus. Micropipettes (e.g. 20 µI, 1000 µI, etc.}(2 candidates to 1) and disposable tips
Inoculating loops

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 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019) 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019)

Agarose gel electrophoresis cell (including tank, lid, cables, gel tray, comb)':and power supply (to be made
accessible to candidates) MATHEMATICAL REQUIREMENTS
TAE!TBE buffer
Agarose powder
Questions set in the examination may involve the basic processes of mathematics for the calculation and use
Nutrient medium of decimals, means, ratios and percentages.
The apparatus and material requirements for Paper 4 will vary year on year. Centres will be notified in Candidates may be required to {i} construct graphs or present data in other suitable graphical forms, and
advance of the details of the apparatus and materials required for each practical examination. (ii) calculate rates of processes.

Candidates should be aware of the problems of drawing conclusions from limited data and should appreciate
Reagents
levels of significance, standard deviation and probability, and the use oft- and chi-squared tests.
This list given below has been drawn up in order to give guidance to Centres concerning the standard Notes on the Use of Statistics in Biology
reagents thal are expected to. be generally avaHable for examination purposes. The list is not intended to be
exhaustive and Centres will be notified in advance of the full list of all the reagents required for each practical
apply a Mest and a chi•squared test Mests are of value in much of Biology,
examination.
ijhe evaluation of the results of breeding experiments and ecological
dealt with fully in many books on statistics for Biology.
iodine in potassium iodide solution
Benedict"s solution
to remember the following equations or what the symbols stand for. They are
biuret reagent
the equations to calculate standard deviations, to test for significant differences
sucrose (use AR for non-reducing sugar test) smaJI unpaired samples and to perform a chi-squared test on suitable data from
glucose
Candidates will be given access to the equations, the meaning of the symbols, a t-table
starch ·ed table.
potassium hydroxide
sodium chloride
dilute hydrochloric acid
hydrogencarbonate indicator (bicarbonate indicator)
sodium hydrogencarbonate (sodium bicarbonate)
,. j~(x-X}'
n-1
limewater
Universal Indicator paper and chart
litmus paper
I= lx1-X2I v=n1 +n 2 -2
methylene blue
OCPIP (2,6-dichlorophenolindophenol)
'(' ']
I~~
-+-
~ ~

.e test z'= L{o-E)'

E
v=c-1

◊ Key to symbols

s* = standard deviation L"" 'sum of X= mean

n = sample size (number of observations) :x = observation
v = degrees of freedom O = observed 'value'
E = expected 'value' c = number of classes

"Candidates should note that on some calculators the symbol O' may appear instead of the symbols.

Candidates are not expected to be familiar with the term standard error. nor to appreciate the difference
x2
between s,,(a,,) and s,...1 (0'11-1). tests will only be expected on one row of data. Candidates should have a
brief understanding of what is meant by the term normal distribution and appreciate levels of significance.
(Tables will be provided.) Questions involving the use ofa f-test or x2test may be set on Papers 1, 2 and 3.
Questions involving an understanding of the use of the tests may be set on Paper 4 but detailed computation
will not be required.

Calculators

Any calculator used must be on the Singapore Examinations and Assessment Board list of approved
calculators.

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 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019)
TEXTBOOKS AND REFERENCES
Alberts, B, Bray, D, Hopkin, K, Johnson, AD, Lewis, J, Raff, M, Roberts, Kand Walter, P (2013) Essentiaf
Ceff Biology (Fourth Edition) (Garland Science) ISBN 0853696470
Alberts, B, Johnson, A, Lewis, J, Morgan, 0, Raff, M, Roberts, Kand Walter, P (2014) Molecular Biology of
the Cell (Sixth Edition) (Garland Science) ISBN 0815344643
Jones, M, Fosbery, R, Gregory, J and Taylor, D (2014) Cambridge International AS and A Level Biology
Coursebook with CD-ROM (Fourth Edition) (Cambridge University Press) ISBN 9781107636828
Krebs, J E, Kilpatrick, S T and Goldstein, E S (2013) Lewin's Genes XI (Eleventh Revised Edilion) {Jones
and Bartlett) ISBN 1449659853
Lodish, H, Berk, A, Kaiser, CA. Krieger, M, Brelscher, A. Ploegh, H, Amon, A and Scott, MP (2012)
Molecular Ceff Biology (Seventh Edition) {W H Freeman and Co) ISBN 142923413X
Plopper, G, Sikorski, E and Sharp, D (2014) Lewin's Cells (Revised Third Edition) (Jones and Bartlett)
ISBN 1284029395
Pomerville, J C (2013) Fundamentals of Microbiology (Tenlh Edition) (Jones and Bartlett) ISBN 1284039684
Raven, PH, Johnson, GB, Mason, KA, Losos, J and Singer, S (2013) Biology {Tenth Edition) (McGraw-Hill)
ISBN 007338307
Reece, J B, Taylor, MR, Simon, E J and Dickey, J L (2013) Campbell Biology: Concepts and Connections
(Seventh Edition) (Pearson) JSBN 1292026359
Reece, J B, Urry, LA, Cain, M L, Wasserman, SA, Minorsky, P V and Jackson, R B (2011) Campbell
Biology (Ninth Edition) (Pearson Higher Education) ISBN 0321739752
Russell, P J, Hertz, P and McMillan, B (2013) Biology: The Dynamic Science (International Edition of Third
Revised Edition) {Brooks/Cole) ISBN 1133592058
Evolution
Dobzhansky, T (March 1973) Nothing in Biology Makes Sense Except in the Light of Evolution, Ameri1
Biology Teachervol. 35 (3)
Climate Change q 10. Discuss requires candidates to give a critical account of the points involved in the topic.
ISBN 9780691160832
0
,;s;
Alley, RB {2000) The Two-mile Time Machine (First Edition) (Princeton Science Library)
·
CJV
Bickford, D, Howard, SD, Ng, DJ J and Sheridan, J A (2010} Impacts of climate ~ n the amphibians
and reptiles of Southeast Asia. Biodiveraily and Conservation.
Sheridan, J A and Bickford, D P (2011) Shrinking body size as an ecological response to climate change.
Nature Climate Change 1:401406
25
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9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLLABUS (2019)
GLOSSARY OF TERMS
It is hoped that the glossary {which is relevant only to science subjects) will prove helpful to candidates as a
guide: it is neither exhaustive nor definitive. The glossary has been deliberately kept brief not only with
respect to the number of terms included but also lo the descriptions of their meanings. Candidates should
appreciate that the meaning of a term must depend in part on its context.
1. Analyse is a context-specific term involving the identification of the constituent parts of a complex
situation or result, an assessment of their individual implications and a consideration of how these relate
to one another and to scientific knowledge and understanding. Analysis may require further processing
of mathematical data to reveal underlying trends and patterns.
2. umerical answer is required. In general, working should be shown, especially
are involved.
3. to group things based on common characteristics.
4. as an open-ended [nstruction, inviting candidates to recall or infer points of
the context of the question, taking account of the number of marks available.
5. ·equires candidates to provide both the similarities and differences between things or
ruce is used in a simnar way as predict except that some supporting statement is required,
.g. reference to a law/principle, or the necessafY reasoning is to be included in the answer.
Define (the lerrn(s) ...) is intended literally. Only a formal statement or equivalent paraphrase is required.
8. Describe requires candidates to state in words (using diagrams where appropriate) the main points of
the topic. It is often used with reference either to particular phenomena or to particular experiments. In
the fonner instance, the term usually implies that the answer should include reference to (visual)
observations associated with the phenomena.
In other contexts, describe and give an account of should be interpreted more generally, i.e. the
candidate has greater discretion about the nature and the organisation of the material to be included in
the answer. Describe and explain may be coupled in a similar way to state and explain.
9, Detennine often implies that the quantity concerned cannot be measured directly but is obtained by
• calculation, substituting measured or known values of other quantities into a standard formula,
e.g. relative molecular mass.
11. Draw is often used in the context of drawing biological specimens. This is an instruction to make a
freehand diagram to show the structures observed, as accurately as possible with respect to shape and
proportion. Lines delimiting distinct regions should be continuous.
In other contexts, this will require an accurate representation of the required subject according to the
applicable conventions and criteria. E.g. Draw the structure of a molecule of glucose.
12. Estimate implies a reasoned order of magnitude statement or calculation of the quantity concerned,
making such simplifying assumptions as may be necessary about points of principle and about the
values of quantities not otheiwise included in the question.
13. EvallJate is a context-specific term requiring a critical use of information to make a judgement or
determination of a particular value or quality (e.g. accuracy). Evaluation of the validity of an
experimental procedure, a set of results or a conclusion involves an assessment of the extent to which
the procedures, results or conclusions are likely to obtain or represent a 'I rue' outcome. This will require
consideration of the advantages and disadvantages, strengths and weaknesses, and limitations of the
underlying approach, as well as other relevant criteria as applicable, and their relative importance.
14. Explain may imply reasoning or some reference to theory, depending on the context.
26
 9744 BIOLOGY GCE ADVANCED LEVEL H2 SYLlABUS {2019)

15. Find is a general term that may variously be interpreted as calculate, measure, determine, etc.

16. Justify requires candidates to give reasoning in support of an answer {for example, a decision,
conclusion, explanation or claim), based on a consideration of available evidence, including
experimental data, together with relevant scientific knowledge and understanding.

17. Label requires candidates to use an appropriate label {and labelling tine, where necessary) to accurately
show the position of a structure, region or point within a diagram or graph, according to the
requirements of the assessment.

18. Ust requires a number of points, generally each of one word, with no elaboration. Where a given
number of points is specified, this should not be exceeded.

19. Measure implies that the quantity concerned can be directly obtained from a suitable measuring
instrument, e.g. length, using a rule, or angle, using a protractor.

20. Outline implies brevity, i.e. restricting the answer to giving essentials.

21. Predict implies that the candidate is not expected to produce the required answer by recall but by
making a logical connection between other pieces of infonnation. Such .information may be wholly given
in the question or may depend on answers extracted in an early part of_the question.

22. Recognise is often used to identify facts, characteristics or concepts that are critical (relevant/
appropriate) to the understanding of a situation, event, process or phenomenon.

23. Sketch, when applied to graph work, implies that the shape and/or position of the curve need only be
qualitatively correct, but candidates should be aware that, depending on the context, some quantitative
aspects may be looked for, e.g. passing through the origin, having an intercept, asymptote or
discontinuity at a particular value.
In diagrams, sketch implies that a simple, freehand drawing is acceptable; nevertheless, care should be
taken over proportions and the clear exposition of important details.

24. State implies a concise answer with little or no supporting argument, e.g. a numerical answer that can
be obtained 'by inspection'.

25. Suggest is used in two main contexts, i.e. either to imp!ythat there is no unique answer (e.g. in
chemistry, two or more substances may satisfy the given conditions describing an 'unknown'), or to
imply that candidates are expected to apply their general knowledge to,a 'novel' situation, one that may
be formally 'not in the syllabus'.
◊
26, What is meant by (the term(s) .•. ) normally implies that a definillon should be given, together with so
relevant comment on the significance or context of the tem,(s) concerned, especially where two of/
terms are included in the question. The amount of supplementary comment intended should ~~
;ntecp,eteo ;n the Ught of the ;nd;cated mark value. ,;y'
0

27

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 CONTENTS

PAGE

1, INTRODUCTION 1

1.1 BACKGROUND 1

1.2 PURPOSE AND VALUE OF BIOLOGY 3

BIOLOGY SYLLABUS 1.3 AIMS~~ 4

1.4 PRAe FSOENCE 4

Pre-University 1~
,:;;,LOGY CURRICULUM FRAMEWORK 7

2. ~ T 8
Higher 2 ~ CoRE IOEA 1: THE CELLA ND BIOMOLECULES OF LIFE 8

Syllabus 9744 X'2} 2.2 CORE IDEA 2: GENETICS ANO INHERITANCE 15

2.3 CoRE IDEA 3: ENERGY AND EO.UILIBR!UM 25

2.4 CORE IDEA 4: BIOLOGICAL EVOLUTION 29

Implementation starting with 2.5 EXTENSIONTOPICA: INFECTIOUS DISEASES 33
2016 Pre-University One Cohort
2.6 ExTENS10N TOPIC 8; IMPACT OF QIMATE CHANGE ON ANIMALS AND PLANTS 35

3. PEDAGOGY 38

4. ASSESSMENT 39

·-
•
4.1

4,2
ASSESSMENT OBJECTIVES

SCHEME OF AsSESSMENT
39

41

s. TEXTBOOKS ANO REFERENCES 43

w
~
© 2016 Curriculum Planning and Development Division.
This publication is not for sale. Permission is granted to reproduce this
publication in its entirety for personal or non-commercial educational use
only. All other rights reserved.

·-
Ministry of Education

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1. INTRODUCTION that they can better apply these concepts to solve problems in novel situations and
contexts.
1.1 BACKGROUND
• Understand that science as a discipline is more than the acquisition of a body of
knowledge
Design of the A-Level science curriculum
The Practices of Science emphasises that science as a discipline is more than the
acquisition of a body of knowledge (e.g. scientific facts, concepts, Jaws, and theories); it is
The Higher 2 (H2) science subjects are the central pieces of the science curriculum at the A-
also a way of knowing and doing. The Practices of Science. includes an understanding of
Level, and were reviewed with the intention to shape how science is taught and lea mt at the
the nature of scientific knowledge and how such knowledge is gt;nerated, established and
pre-university level. The curriculum aims to lay a strong foundation of knowledge, skills and
communicated. Please refer to Section 1.4 for more details.
attitudes in order to prepare our students well for university, work and life in the future.
fate real-world cont, in the teaching and learning of H2
The curriculum design took into consideration MOE's key initiatives of Student-Centric,
Values-Driven Education (SVE), the development of 21st Century Competencies {21CC) in our
students find the teaching and learning of science more meaningful
students, changes to other equivalent qualifications, feedback and observations from local
when set in appropriate contexts. The use of real-world contexts also
universities, findings from science education research and feedback from schools and
teachers. entic platforms to bring out classroom discourse and deliberations on the
nomic, moral and ethical dimensions of science based on sound scientific
Purpose of HZ science curriculum

A strong background in science prepares students to take on careers in science and :trengthen the teaching of science through the use of a wider range of pedagogies
The use ·of inquiry-based pedagogical approaches, which include the skilful use of
engineering-related sectors as well as opens up in-roads to many.opportunities even in fields
not traditionally associated with the hard sciences. Beyond career considerations, science Information and Communication Technology (ICT), will engage students in critical
education should also contribute to the development of a scientifically literate citizenry. thinking, reasoning and argument. In addition, through practical and hands•on activities,
Therefore, the purpose of the H2 science curriculum should encompass the following aims: students will learn and assimilate key concepts and skills better. Students enjoy practical
work and regard it as a constructive learning activity. Science education should also aim
to develop students as independent and self-directed learners with the habit of inquiry
• For all students: As future citizens in an increasingly technologically-driven world and as
and constant pursuit of knowledge.
future leaders of the country, they should be equipped to make informed decisions based
on sound sdentific knowledge and principles about current and emerging issues which
are important to one's self, society and the world at large (for example, in appreciating
the energy constraints faced by Singapore, or understanding the mechanisms involved '
epidemics); •
• For students who intend to pursue science further: As practitioners and innova~he
learner of science should possess a deeper grasp of scientific knowledge aad~~ell-
versed in scientific practices, at the level of rigour befitting the A-level ce~Vn.

Key changes to HZ science curriculum

• Use of core ideas to frame the teaching and learning of science

Core ideas represent the enduring understanding that emerges from learning each
science subject. These ideas cut across traditional content boundaries, providing a
broader way of thinking about phenomena in the natural world. This is to shift the
students' learning mentality from a compartmentalised view of scientific knowledge to a
more coherent and integrated understanding of science. The use of core ideas in science
to frame the curriculum can help to build deep conceptual understanding in students so
1
Bennett, J., Lubben, F. & Hogarth, S. (2007). Bringing science to life: A synthesis of the research evidence on
the effects of context-based and STS approaches to science teaching. Sci. Ed., 91{3), 347-370.

1 2

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1.2 PURPOSE AND VALUE OF BIOLOGY
In Singapore, biology education from the primary to the A-Level has been organised as a
continuum in the following manner:
(a) From Primary 3 to 6, students learn about how life works at the systems level;
(b) From Lower Secondary science to 0-Level Biology, students learn about how life works
at the physlological level; and
{c) At the A-Level, students learn about how life works at the cellular and molecular level
while understanding the implications on macro levels.
The Biology syllabus is developed as a seamless continuum from the 0-Level to the A-Level,
without the need for topics to be revisited at the A-Level. The 0-level syllabus is foundational
and thus should provide the necessary background for study at the A-Level. Students who
intend to offer H2 Biology will therefore be assumed to have knowledge and understanding
of 0-Level Biology, either as a single subject or as part of a balanced science course.
Many new and important fields of biology have emerged through recent advancements in life
sciences. Vast amounts of knowledge have been generated as evident from the sprouting of
scientific journals catt;!:ring to niche areas of research. As such, this syllabus refines and
updates the content knowledge of the previous syllabus (9648) so that students can keep
themselves up to date with knowledge that is relevant for their participation in a technology-
driven economy.
The value of learning HZ Biology ultimately hinges on the development of a scientific mind
and disposition while addressing the broader questions of what life is and how life is sustained.
The Science Currfculum Framework developed by MOE elaborates on the development of the
scientific mind and disposition. Through the study of the HZ Biology course, students should
be prepared for life science-related courses at university and, consequently, careers that ate
related to this field.
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1.3 AIMS
The aims of a course based on this syllabus should be to:
1. provide students with an experience that develops their interest in biology and builds
the knowledge, skills and attitudes necessary for further studies in related fields;
2. enable students to become scientifically literate citizens who are well-prepared for the
challenges of the 21st century;
3. e understanding, skills, ethics and attitudes relevant to the
:e,. including the following:
ding the nature of scientific knowledge
,nstrating science inquiry skills
;ting science and society
dress the broader questions of what life is and how life is sustained, including:
-.1. understanding life at the cellular and molecular levels, and making connections to
how these micro-systems interact at the physiological and organismal levels
4.2. recognising the evolving nature of biological knowledge
4.3. stimulating interest in and demonstrating care for the local and global
environment.
1.4 PRACTICES OF SCIENCE
Science as a discipline Is more than the acquisftion of a body of knowledge (e.g. scientific facts,
concepts, laws, and theories); it Is a way of knowing and doing. ft includes an understanding of
the nature of scientific knowledge and how this knowledge is generated, established and
communicated. Scientists rely on a set of established procedures and practices associated with
0 scientific inquiry to gather evidence and test their ideas on how the natural world works.
However, there is no single method and the real process of science is often complex and iterative,
following many different paths. While science is powerful, generating knowledge that forms the
basis for many technological feats and innovations, it has limitations.
Teaching students the nature of science helps them to develop an accurate understanding of
what science is and how it Is practised and applied in society. Students should be encouraged
to consider relevant ethical issues, how scientific knowledge is developed, and the strengths
and limitations of science. Teaching the nature of science also enhances the students'
understanding of science content, increases their interest in science and helps show its human
side. Science teaching should emphasise how we know as well as what we know.
Understanding the nature of scientific knowledge, demonstrating science inquiry skills and
relating science and society are the three components that form our Practices of Science.
Students' understanding of the nature and limitations of science and scientific inquiry are
developed effectively when the practices are taught in the context of relevant science
content. Attitudes relevant to science such as inquisitiveness, concern for accuracy and
precision, objectivity, integrity and perseverance are emphasised.
The curriculum provides opportunities for students to reflect how the Practices of Science
contribute to the accumulation of scientific knowledge. Students are encouraged to think about
the 'whys' when planning and conducting investigations, developing mode!s 2 or engaging in
scientific arguments. Through such reflection, they can come to understand the importance of
each practice and develop a nuanced appreciation of the nature of science.
Developing 21st Century Competencies Through the learning of Science
To prepare our students for the future, a Framework for 21st Century Competencies (21CC)
and Student Outcomes was developed by MOE (see Figure 1.1). This 21cc framework is meant
to equip students with the key competencies and mindsets to be successful in the 21st
century.

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◊ Figure 1.1. Framework for 21st Century Competencies and Student Outcomes

The features and intent of the Practices of Science are consistent with the emphasis on
developing 21CC in our students.

The development of 21CC is not separate from the learning of science. The features of
scientific inquiry, such as the processes of scientific investigation, reasoning, modelling and
problem solving support a student's development of 21cc. The nature and limitations of
science and scientific inquiry are developed effectively when scientific practices are learnt in
the context of relevant science content. Deep disciplinary learning in science develops 21cc
and promotes the process of learning for transfer to other areas of life.

~ A model is a representation of an idea, an object, a process or a system that is used to describe and explain ·
phenomena that cannot be.experienced directly. Models exist in different forms from the c.onc.rete, such as
physlcal scale models, to abstract representations, suc.h as diagrams or mathematic.al expressions. The use
of models involves the understanding that all models contain approximations and assumptions Hmiting their
validity and predictive power.

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1.5 H2 BIOLOGY CURRICULUM FRAMEWORK 2. CONTENT
The rapid progress In the field of life sciences poses a challenge for biology education,
2,1 CORE IOEA 1: THE CELL AND BIOMOLECULES OF LIFE
especially in terms of designing a framework that integrates fundamental knowledge, skills
and attitudes. Figure 1.2 below provides an overview of this framework.
Core Idea 1-The Cell and Biomolecules of Life- entails the study of cells, which are the basic
units of life .

Students can frame their learning using the following questions:

• Why Is a cell th~asic unit of life and how does it promote continuity of life?
• How is th~b t crucial in understanding life?
How are r ures of biomolecules related to their functions?
• How qg en· regulate the movement of substances into and out of themselves, and
implications of such movements?
• Wha""tiare the differences between cells of prokaryotes and eukaryotes, between cells
•Natural
its and animals, and between cells of unicellular and multicellular organisms?
Nudefc Acids & s91ettlon &
Gene Expression Adaptation what ways do viruses not fit the cell model?
• Organisation of Environment & • Evolution &
Genomes Organiws 8lodlversity, b-cellular structures provide the means to drive cellular processes
• Control of Gene • Communication Species&
Expression & Equilibrium Specfation
In Organisms Knowing how cellular structures facilitate specific cellular processes is fundamental to
• ONA Mutations
• The Cell cycle explaining how life 'works'. The cell theory states that the cell is the smallest and most basic
• Inheritance unit of life and that cells grow from existing cells. Understanding the role of cellular organelles
(such as the nudeus, ribosome, chloroplast and mitochondrion) and cellular structures {for
Extension Topics: {A) Infectious Diseases; example, the cytoskeleton) will help in understanding the concept of how structure relates to
{B} Impact of Climate Ch~nge on Animals and Plants function.

Figure 1.2. Overview of the H2 Biology Curriculum Framework
The content in this H2 Biology syllabus is organised around four core ideas of Biolo,
• reticulum, are absent. Prokaryotic ribosomes are different from eukaryotic ribosomes. Some
each core idea, pertinent and open-ended guiding questions are listed to help stude
the concepts and promote inquiry, while narratives allow links between con
within and between core ideas- to be made.
Besides the core ideas, this H2 Biology syllabus features two extension to ."hrese are based
on important emerging biological issues impacting both the local an contexts. They
require students to demonstrate assimilation of the core ideas an d their knowledge
and understanding to real~world challenges. Furthermore, exte n topics will equip
students with the necessary knowledge and process skills to make informed decisions about
scientific issues. In line with this, the two extension topics chosen are (A) Infectious Diseases,
and (B) Impact of Climate Change on Animals and Plants. Both extension topics take up about
10 percent of the total H2 Biology curriculum and are presented through the use of guiding
questions, narratives, assessable learning outcomes and suggested learning experiences.
Students are expected to study all four core ideas and both extension topics.
There are significant differences between cells of prokaryotes and eukaryotes. Using bacteria
as a model, the nucleoid is not enclosed by any membrane. Plasmids may be present as extra~
chromosomal DNA. Membrane-bound organelles, such as mitochondria and endoplasmic
bacterial cells have cell walls that comprise peptidoglycan rather than cellulose. Within the
eukarya domain, the cell model of plants Is also different from that of animals. Unlike
unicellular organisms which merely undergo cellular diviSion, cells of multicellular organisms
undergo division and differentiation to allow them to carry out their specific functions.
Biomolecules make up cells and cells regulate many cellular processes, including the
movement of substances into and out of themselves, through membranes
The different classes of biomolecules (sugars, lipids, proteins and nucleic acids) function as
molecular building blocks for macromolecules to be assembled. Nucleic adds, which include
ONA and RNA, are made from monomers known as nucleotides. Phospholipids, cholesterol,
carbohydrates and proteins are important components In biological membranes.
Cells need to regulate the movement of substances into and out of themselves. Substances
such as water., oxygen, glucose and minerals are important in the synthesis of new molecules
and important cellular processes. According to the fluid mosaic model, cell membranes are

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selectively permeable due to the nature of the phospholipids and prqteins from which they It is important to recognise that a cell is dynamic in nature and not a static structure. At any
are made. The movement of different molecules depends on the nature of the substances point of time, numerous activities are occurring in the cell. In a plant cell, photosynthesis and
through transport processes such as osmosis, diffusion and active transport. Membranes respiration can be occurring simultaneously. This causes biochemical changes in the
allow cells to create and maintain internal environments that are different from external cytoplasm of the plant cell. If it is necessary to produce more chlorophyll pigments or increase
environments. the amount of cellulose, the rate of protein synthesis in those biochemical pathways will
increase.
Eukaryotic cells also contain internal membrane structures -that partition the cell into
specialised compartments so that cellular processes can occi.tr with optimal activity e.g.
chloroplasts and mitochondria. The endomembrane system, consisting of rough and smooth
endoplasmic reticulum and Golgi apparatus, ls responsible: for protein processing and
vesicular transport within the cell.

Prokaryotes generally lack such membrane-bound organelles and endomembrane systems;

yet they survive and reproduce. In the endosymbiotic theory,·organelles like mitochondria
and chloroplasts represent formerly free-living prokaryotes that were taken inside another
cell, and this could explain the link between the two domains in the tree of life.

In contrast to eukaryotic and prokaryotic cells, viruses lack several of those cellular structures.
They rely on eukaryotes and prokaryotes to reproduce. In this r'egard, viruses are considered
obligate parasites and there is debate as to whether viruses are living or non-living organisms.

Proteins, which are a class of biomolecules, play significant roles in cells

Proteins play a variety of roles in cells including structural, transport, enzymatic and signalling
functions. They are essential for biological processes and functions, such as chemiosmosis,
protein synthesis, cell signalling, immunology and blood glucose homeostasis. Protein
structure can be affected by temperature and pH. Enzymes are an important group of
proteins that control many biological reactions. The functions of these proteins will be
revisited in the other core ideas.

Stem cells have the potential to divide and drrferentiate into different cell types ◊

Following fertilisation, a single-cell zygote develops into a multicellular organism. Tl

can replicate its ONA, divide its nucleus and divide into two genetlcally-ldenti
potency describes a cell's ability to differentiate into other cell types. The zv1
formed from the first few cell divisions during embryonic development (u_
stage) produce totipotent cells. Beyond the eight-cell stage, One of th
remains undifferentiated, retaining the ability to divide indefinitely a
other daughter cell differentiates. After the eight-cell stage, the
pluripotent stem cells. Pluripotent stem cells undergo further spe
cells, which can further differentiate to become unipotent stern cells.

Environmental signals trigger the differentiation of a cell lnto: a more specialised form. Cell
differentiation involves changing or regulating the expression patterns of genes. Each
specialised cell type in an organism expresses a subset of all the genes that constitute the
genome and this expression is regulated by various rnechanisms resulting in differential gene
expression of the same genome.

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Organelles and Cellular Structures Biomolecules of Life and Cellular Transport

This concept discusses the typical cell model of prokaryotes and eukaryotes, including plants
and animals. A strong understanding of the structure of the following organelles and cellular
structures in relation to their function is necessary: rough and smooth endoplasmic reticulum,
Golgi body, mitochondria, ribosomes, lysosomes, chloroplasts, cell surface membrane,
nuclear envelope, centrioles, nucleus and nucleolus.
This concept focuses on how the structures of biomolecules give rise to properties that allow
these biomolecules to carry out their functions. One of these functions tnvolves regulating
the transport of substances into and out of the cell. This regulation is afforded by the
properties of the cell membrane which comprises phospholipids and proteins. Regulation of
the movements is important for several biochemical processes to occur.

Learnin£ Outcomes Learnin£ Outcomes

{a) Outline the cell theory with the understanding that cells are the smallest unit of life, all (g) Descri~e t ~ u r e and properties ~f the following monomers:
cells come from pre-existing cells, and living organisms are composed of cells. i. e and ~-glucose (in carbohydrates)
ii. ,S:f}l o\ and fatty acids (in lipids)
(b) Interpret and recognise drawings, photomicrographs and electronmicrographs of the it~~ino acids (in proteins) (knowledge of chemical formulae of specific R-groups
following membrane systems and organelles: rough and smooth endoplasmic reticulum, of different amino acids is not required).
Golgi body, mitochondria, ribosomes, lysosomes, chloroplasts, cell surface membrane,
nuclear envelope, centrioles, nucleus and nucleolus {for practical assessment, candidates escr!be the formation and breakage of the following bonds:
may be required to operate a light microscope, mount slides and use a graticule), glycosidic bond
ii. ester bond
{c) Outline the functions of the membrane systems and organelles listed in (b). iii. peptide bond

{d) Describe the structure of a typical bacterial cell (small and unicellular, peptidogtycan cell (ii Describe the structures and properties of the following biomolecules and explain how
wall, circular ONA, 705 ribosomes and lack of membrane-bound organelles). these are related to their roles in living organisms:
i. starch (including amylase and amylopectin)
{e) Describe the structural components of viruses, including enveloped viruses and ii. cellulose
bacteriophages, and interpret drawings and photographs of them. iii. glycogen
iv. triglyceride
{f) Discuss how viruses challenge the cell theory and concepts of what is considered living. v. phospholipld

(j) Explain the fluid mosaic model and the roles of the constituent biomolecules (including
phospholipids, proteins, glycofipids, glycoproteins and cholesterol) in cell membranes.

(k) Outline the functions of membranes at the surface of cells and membranes wr1:hin the
cell.

{I) Explain how and why different substances move across membranes through simple
diffusion, osmosis, facilitated diffusion, active transport, endocytosis and exocytosis.

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Proteins Stem Cells

Proteins play a variety of roles in structural, transport, enzymatic and signalling functions. This This concept highlights the diversity in cell type and the morphology in an organism. ln an
concept focuses on the structure and properties of proteins and how temperature and pH organism, all cells except the gametes are genetically identical. Yet, a liver cell, a rod cell in
may contribute to the denaturation of proteins. The structure -of a protein is related to its the eye and an epithelial cell in the ileum differ significantly in terms of morphology and
function. function due to differential gene expression. The same genome gives rise to a wide range of
cells which further form tissues, organs and systems in an organism.
Leamin_! Outcomes
The ability of stem cells to divide and their potential for self-renewal allows for growth. Stem
(m) Explain primary structure, secondary structure, tertiary structure and quaternary cells replace cells that die or are damaged. During embryogenesis, cell division and
structure of proteins, and describe the types of bonds that hold the molecule in shape differentiation allow-~evelopment of an entire organism in utero from a single•cell zygote.
{hydrogen, ionic, and disulfide bonds, and hydrophobic Interactions).
Stem cells hold grg_~~;tial as medical treatments. Haematopoietic stem cells are used in
(n) Explain the effects of temperature and pH on protein structure. ~lants in cancer treatments. Skin stem cells are used to culture skin cells
ith massive burns. Ethical debates over the use of stem cells are primarily
(o) Describe the molecular structure of the following proteins and explain how the
the use of embryonic stem cells. The use of adult stem cells faces fewer such
structure of each protein relates to the function it plays:
i. haemoglobin (transport}
ii. collagen (structural)
iii. G-protein linked receptor (signalling)
(knowledge of details of the number of amino acids and types of secondary structures Describe the unique features of zygotic stem cells, embryonic stem cells and blood
present is not required.} stem cells; correctly using the terms totipotency (zygotic stem cells which have the
ability to differentiate lnto any cell type to form whole organisms and so are also
(p) Explain the mode of action of enzymes in terms of an active site, enzyme-substrate
pluripotent and multipotent), pluripotency (embryonic stem cells which have the
complex, lowering of activation energy and enzyme specificity using the lock-and-key
ability to differentiate into almost any cell type to form any organ and so are not
and induced-fit hypotheses.
totipotent but are multipotent} and multipotency {blood stem cells which have the
(q) Investigate and explain the effects of temperature, pH,' enzyme concentration and ability to differentiate Into a limited range of cell types and so are not pluripotent or
substrate concentration of an enzyme-catalysed reaction by measuring rates of totipotent).
formation of products {e.g. measuring gas produced: using catalase) or rate of
(u) Explain the normal functions of stem cells ln a living organism, including embryonic
disappearance of substrate (e.g. using amylase, starch and iodine).
stem cells and blood stem cells.
(r) Describe the structure of competitive and non-competitive inhibitors with refer~:
(vi Discuss the ethical implications of the application of stem cells in research and
to the binding sites of the inhibitor. ,- ;!CJ
medical applications and how human induced plurlpotent stem cells (iPSCs)
(s) Explain the effects of competitive and non-competitive inhibitors (inclu overcome some of these issues (procedural details of how iPSCs are formed are not
inhibitors) on the rate of enzyme activity. required}.

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2.2 CORE IDEA 2: GENETICS AND INHERITANCE
An understanding of Genetics and Inheritance helps make sense of the transition from
molecular to organismal levels. Genetics and Inheritance provides the molecular basis to the
understanding of how variation in populations arises and this is important in the study of
biological evolution. At the cellular level, expression of genes involves structures such as the
nucleus, endoplasmic reticulum and ribosome. Many essential products of gene expression
are enzymes involved in biochemical pathways whlch control physiological functions. As such,
mutation of genes may give rise to dysfunctional proteins which In turn could result in
diseases. Sickle cell anaemia and cancer are some examples of genetic diseases.
Students can frame their learning using the following questions:
• How does the genetic make-up of an organism and the environment influence the
organism's appearance, behaviour and survival?
How does the inheritance of genetic information ensure the continuity of humans as a
species?
Heritable information, in the form of DNA (and in some cases RNA}, provides for continuity
of life
Genetic information is stored In an organism's DNA; expression of genes results in the
synthesis of functional products, such as rRNA, tRNA and proteins. These products play a role
In intra- and extra-cellular biochemical pathways and influence the physiological processes in
organisms.
Genomes contain heritable information necessary for continuity of life at all levels: cell,
organism and system. This Information is stored and passed on to subsequent generations via
DNA. Reproduction can occur at the cellular or organismal level; each progeny needs to
receive heritable genetic information from its parent(s).
$ genetically identical cells and this is important for growth, repair and the asexual reproduction
An understanding of how eukaryotic, prokaryotfc and viral genomes are organised
implications on how gene expression in organisms is controlled. The genome of proka1
typically comprises a large circular chromosome and smaller plasmids. Generally,
genes, whtch code fol" proteins essential for bacterial survival, are found
chromosome while genes that confer advantages to bacterial sun.,.
environments are found in the plasmids. Prokaryotes reproduce by binaryfi
genetic material can be transferred between bacteria through transf1
and/or conjugation. This transfer of genetic material gives rise toge
bacteria population.
In contrast, eukaryotic genomes are organised in a more complex manner. DNA is wrapped
around histone proteins and compacted to form linear chromosomes; the number of
chromosomes varies between eukaryotic species. Structurally, linear chromosomes have
centromeres and telomeres, and their ONA consists of coding and non-coding sequences with
the latter being in larger proportions. Coding DNA is expressed to give functional products
(e.g. proteins, rRNA, tRNA) while non-coding DNA, e.g. control elements and centromeres,
are involved in regulation of gene expression and nuclear division respectively.
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Unlike prokaryotes and eukaryotes, the genome of viruses varies greatly; they can be ONA or
RNA in nature and single or double-stranded, depending on the type of virus. Viruses undergo
different reproductive cycles: some bacteriophages Ukethe T4 phage reproduce via lytic cycle
while others like the lambda phage, reproduce via lytic and/or lysogenic cycles; animal
viruses, such as influenza virus and HIV, reproduce through other mechanisms. Again, unlike
their prokaryotic or eukaryotic counterparts, viruses do not photosynthesise or respire, and
they require host cells {bacteria, plants or animals) to reproduce. As such, there is much
debate as to whether viruses are considered to be IMng or non-living organisms.
rmation involves molecular mechanisms and gene regulation
pression
genes contained in all the nuclei of somatic cells are exactly the same,
r morphologically and functionally. The differences between cell types
it genes being present, but due to differential gene expression, i.e. the
ifferent sets of genes by cells with the same genome,
on of gene expression gives a cell control over its structure and function. It allows cell
1tiation to occur. lt may be controlled by the way DNA is packed in chromatin and at
e various steps of protein synthesis, i.e., from the transcription to post-translational
modification of a protein. It is the basis for cellular differentiation and morphogenesis which
gives an organism versatility and adaptability. Gene expression can be studied using
fundamental techniques of molecular biology such as the polymerase chain reaction {PCR),
gel electrophoresis, Southern blotting and nucleic acid hybridisation.
The cell cycle is tightly regulated
The cell cycle comprises lnterphase, nuclear division and cytokinesis. There are two types of
nuclear division: mitosis and meiosis. A cell cycle that involves mitosis will give rise to
of organisms. This cycle ls coupled intricately with another important process of the living cell:
DNA replication, which occurs during the synthesis phase of interphase. The mitotic cell cycle
is tightly regulated at various checkpoints that control the rate of cell division; uncontrolled
cell division could result in cancer.
A cell cycle that involves meiosis occurs in the reproductive organs of organisms and is
important for sexual reproduction. Meiosis results in gametes having half the amount of
genetic material present in somatic cells. The crossing~over of non-sister chromatids and the
independent assortment of bivalents in meiosis, together with the random fertilisation of
male and female gametes, contribute to genetic variation in populations. Genetic variation is
essential for natural selection to occur. Homogeneity of a population can result in the entire
population being wiped out by diseases or climatic change.
16
Mutation arises from imperfect replication of genetic information; together with other
biological processes, such mutations increase genetic variation
Based on the central dogma, a change in the sequence of the DNA nucleotide, Le. gene
mutation, may affect the amino acid sequence In the polypeptide and hence the phenotype
of the organism. Many mutations are detrimental to the individual since they affect the
normal functioning of the gene product, e.g. genetic diseases such as sickle cell anaemia.
Others are neutral, often because they have no effect on the phenotype, e.g. a change in a
DNA triplet which still codes for the same amino acid. Occasionally, mutations may be
beneficial. For example, individuals that are heterozygous for a mutated haemoglobin gene
that causes sickle cell anaemia have a selective advantage in areas where malaria is common.
Besides mutation of genes, chromosomal aberration and changes ln chromosome number
may also occur. Down's syndrome arises due to the presence of an additional copy of
chromosome 21.
The Structure of Nucleic Acids and Gene Expression
The structure of DNA was proposed by Watson and Crick in 1953. With an understanding of
DNA structure, experimental evidence supported the proposal that DNA replicates in a semi~
conservative manner. The central dogma states that genetic information is encoded in the
ONA and transferred to the mRNA during transcription. In addition to mRNA transcription,
tRNA and rRNA are transcribed; tRNA is needed during translation while rRNA is a component
of ribosomes. In eukaryotic transcription, pre-mRNA is synthesised and then processed to
produce mature mRNA. Subsequently, through translation, the information on the mRNA is
used to synthesise polypeptides, which are folded into functional proteins.
(a)
'
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rUcture and roles of DNA and RNA {tRNA, rRNA and mRNA}
·mitochondrial ONA is not required) .
Mutation, meiosis and sexual reproduction give rise to genetic variation within a population.
There are two kinds of genetic variation: continuous variation involves many genes, which he process of DNA replication and how the end replication problem arises.
have an additive effect in controlling a characteristic; and discontinuous variation, which
involves one or just a few genes in controlling a characteristic. Besides these, environmental :ribe how the information on DNA is used to synthesise polypeptides in
factors are known to influence the phenotype of organisms. rokaryotes and eukaryotes. {Description of the processes of transcription,
formation of mRNA from pre-mRNA and translation is required.)
The expression of genes gives rise to functional products that affect the biochemical reactions
arid physiological functions of organisms. This demonstrates how the genotype and
phenotype of an organism are related. Besides its genotype, the environment also plays a role
in determining the phenotype of an organism and this is related to the field of epigenetics.
Some examples of environmental factors include the availability of nutrients and changes in
temperature.

The chromosomal basis of inheritance sheds light on the pattern of transmitting genes from
parent to offspring

When Gregor Mendel first started his investigations into inheritance, the concept of gen. •
had not existed yet. He used the term 'traits' in place of genes. By using genetic diagram.
phenotypic and genotypic ratios of filial generations can be predicted for crosses
monohybrid or dihybrid inheritance. ln line with Mendelian genetics, pedigre,
be used to predict the probability of inheriting genetic diseases such as h
Huntington's disease.

Non-Mendelian inheritance involves more complex traits. For example_fOrg'

on sex chromosomes while others involve multiple alleles. For example~les of some genes
exhibit co-dominance or incomplete dominance and some genes have multiple alleles or are
found on the sex chromosomes. Furthermore, phenotype may depend on interactions
between two or more genes, e.g. epistasis. In addition, the inheritance of linked genes does
not follow Mendelian laws; in predicting the phenotypic and. genotypic ratios of filial
generations for linked genes, the occurrence and frequency of crossing over has to be
considered.

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Organisation of Genomes Control of Gene Expression

The nuclear genomes of eukaryotes differ greatly in size, number of genes and gene density
from one another. The number of chromosomes differs between species and, in addition,
certain organelles in eukaryotes possess small amounts of their own DNA. Eukaryotic
genomes generally have a higher proportion of non~coding DNA to coding DNA. In addition to
a large, circular chromosome, bacteria also have several plasmids. Even though bacteria
reproduce asexually, they exhibit a great deal of genetic diversity through mutation and
genetic transfer. In contrast to eukaryotic and prokaryotic genomes, the viral genome varies
according to the type of virus: the genome may be DNA or RNA in na.ture and single-- or
double•stranded. For RNA viruses, they may possess either positive-sense RNA (i.e. identical
to viral mRNA and thus can be immediately translated) or negative.sense RNA (i.e.
complementary to viral mRNA and thus must be converted to positive•sense RNA by RNA
polymerase before translation).
Learnint Outcomes
(d) Describe the structure and organisation of viral, prokaryotic and eukaryoticgenomes
(including DNA/RNA, single-/double-stranded, number of nucleotides, packing of
DNA, linearity/circularity and presence/absence of introns).
(e) Describe how the genomes of viruses are Inherited through outlining the
reproductive cycles of:
i. bacteriophages that reproduce via lytic cycle only, including T4 phage;
ii. bacteriophages that reproduce via lytic and lysogenic cycles, including lambda
phage;
iii. enveloped viruses, Including influenza; and
iV. retroviruses, including HIV.
(f) Describe how variation in viral genomes arises, including antigenic shift and antige
drift.
In prokaryotes, operons, Hke the trp and lac operons, regulate gene expression using
repressible and inducible systems. Regulatory genes encode proteins that control
transcription of structural genes. ln eukaryotes, regulation of gene expression can occur at
the chromatin level, transcriptional level, post-transcriptional level, translational level and/or
even post•translational level. Basic molecular techniques allow scientists to study gene
expression.
(i) expression in prokaryotes can be regulated, through the concept
,erons (including lac and trp operons), including the role of regulatory
:a distinguish between inducible and repressible systems {knowledge of
tion of trp operon is not required).
:plain how differential (i.e. spatial and temporal) gene expression in eukaryotes
can be regulated at different levels:
chromatin level (histone modification and DNA methylation);
ii. transcriptional level (control elements, such as promoters, silencers and
enhancers, and proteins, such as transcription factors and repressors);
iii. post-transcriptional level (processing of pre-mRNA in terms of splicing,
polyadenylation and 5' capping);
iv. translational level (half-life of RNA and initiation of translation); and
v. post-translational level (biochemical modification and protein degradation).
(k) Describe the principles and procedures of these molecular techniques:
i. polymerase chain reaction (including its advantages and limitations);
ii. gel electrophoresis; and
iii. Southern blotting and nucleic acid hybridisation.

(g) Outline the mechanism of asexual reproduction by binary fission

prokaryote and describe how transformation, transduction and
(including the role of F plasmids but not Hfr) give rise to variation '
genomes.

(h) Describe the structure and function of non•coding DNA in euk&

· that do not encode protein or RNA, including intrans, c{ntrpWferes, telomeres,
promoters, enhancers and silencers) (knowledge of tran~ons, satellite DNA,
pseudo-genes and duplication of segments is not required).

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DNA Mutations
Changes to the DNA sequence or amount could have huge physiological impact on organisms.
This concept illustrates how DNA mutations could result in sickle cell anaemia and Down
syndrome in humans.
Learnin_£ Outcomes
(I} Explain what is meant by the terms gene mutation and chr:omosomal aberration. For
gene mutation, knowledge of how substitution, addition and deletion could change
the amino acid sequence (including frameshift) is required. For chromosomal
aberration, knowledge of numerical aberration (including:aneuploidy, as in the case
of trisomy 21, i.e. Down syndrome) and structural aberration (including
translocation, duplication, Inversion and deletion) is required.
(m) Explain how gene mutations can result in diseases {includlng sickle cell anaemia).
◊
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The Cell Cycle
There are two different types of cell cycles: mitotic and meiotic. Cell cycles are tightly
regulated at various checkpoints. The mitotic cell cycle is necessary for growth and repair
while the meiotic cell cycle is necessary to generate gametes. Meiosis gives rise to genetic
variation between gametes through crossing over of homologous chromosomes and the
independent assortment of bivalents.
The development of cancer is a multi-step process that comprises gene mutations caused by
environmental factors, biological agents or hereditary predispositions. These mutations might
cause cells to bypass c cycle checkpoints. Normally, two groups of genes are involved in
regulating cell divisi u ur suppressor genes and proto-oncogenes. Mutations in either
or both of these o genes may lead to the development of cancer. Cancer has a much
gapore compared to other diseases and accounts for as much as 30 per
in this country. The recorded incidence of cancer is on the rise and this
:a the accumulation of mutations from one generation to the next, although
have also been proposed: increased exposure to carcinogens and increased
rates as a result of effective cancer screening programmes. As such, an
:t:anding of how cancer develops is important as this would $et the platform for
1ssion of developing anti-cancer drugs.
(n) Describe the events that occur during the mitotic cell cycle and the main stages of
mitosis {including the behaviour of chromosomes, nuclear envelope, cell membrane
and centrioles).
{o) Explain the significance of the mitotic cell cycle (including growth, repair and asexual
reproduction) and the need to regulate it tightly (knowledge that dysregulation of
checkpoints of cell division can result in uncontrolled cell division and cancer is
required, but detail of the mechanism is not required).
(p) Identify the causative factors, including genetic, chemical carcinogens, ionising
radiation and loss of immunity, which may increase the chances of cancerous growth.
(q) Explain how the loss of function mutation of tumour suppressor genes, including-p53,
and gain in function mutation of proto-oncogenes, including ras, results in
uncontrolled cell division.
{r) Describe the development of cancer as a multi-step process that includes
accumulation of mutations, angiogenesis and metastasis.
(s) Describe the events that occur during the meiotic cell cycle and the main stages of
meiosis (including the behaviour of chromosomes, nuclear envelope, cell membrane
and centrioles} {names of the main stages are expected, but not the sub-divisions of
prophase).
Learnint Outcomes Inheritance
(t) Explain the significance of the meiotic cell cycle {including how meiosis and random
fertilisation can lead to variation). This concept includes both Mendelian and nonMMendelian inheritance. Besides genetics, the
environment also plays a role in determining the phenotype of an organism. Statistical tests,
such as the chi--squared test, allow scientists to test the significance of differences between
observed and expected results of genetic crosses.

leamin1_ Outcomes

(u) 1s: focus, allele, dominant, recessive, codominant, incomplete

ygous, heterozygous, phenotype, genotype and linkage.

(v) genes are inherited from one generation to the next via the germ cells

in how genotype is linked to phenotype.

se genetic diagrams to solve problems In dihybrid crosses, including those involving

codominance, incomplete dominance, multiple alleles, sex linkage, autosomal
linkage and epistasis.

(y) Use genetic diagrams to solve problems involving test crosses.

(z} Explain the meaning of the terms linkage and crossingMover and explain the effect of
linkage and crossingMover on the phenotypic ratios from dihybrid crosses.

(aa) Describe the interaction between loci (epistasis) and predict phenotypic ratios in
problems involving epistasis (knowledge of the expected ratio for various types of
epistasis is not required; focus of this section is on problem solving}.

(bb) Explain how the environment may affect the phenotype (including how diet affects
• the differentiation of honey bees and how temperature affects fur colour of
Himalayan rabbits).

(cc) Explain the difference between genetic variation that is continuous (many, additive
genes control a characteristic) and genetic variation that is discontinuous (one or a
few genes control a characteristic).

{dd) Use the chi-squared test to test the significance of differences between obseived and
expected results.

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2.3 CORE IDEA 3: ENERGY AND EQUILIBRIUM
This core idea describes how energy is obtained, transformed and utilised in biological
systems.
Students can frame their learning using the following questions:
• How do organisms obtain and use energy for growth and survival?
• How do organisms respond to internal and external changes?
Energy is needed to drive biochemical processes in organisms
To maintain life-sustaining processes, organisms require materials and energy. from their
environment. Nearly all energy that sustains lrfe ultimately comes from the sun. Plants and
other photosynthetic organisms make use of sunlight to synthesise carbohydrates from
carbon dioxide and water during the process of photosynthesis. Light energy from the sun is
converted into chemical energy in the form of carbohydrates. This chemical energy may be
used to form plant matter or subsequently released to fuel activities within the plants.
All other organisms depend on autotrophs for energy, either directly, by feeding on
autotrophs such as plants; or indirectly, as energy is passed along food chains from one
organism to the next. Food provides a source of carbohydrates which are broken down to
release energy to phosphorylate ADP to ATP during aerobic respiration. Anaerobic respiration
follows a different and less efficient chemical pathway to provide ATP. ATP obtained from
respiration is used to drive various essential cellular processes.
In eukaryotes, photosynthesis and respiration occur in membrane-bound organelles. Many
steps in photosynthesis and respiration are controlled by enzymes sequestered in these
organelles and therefore are also limited by similar factors that will affect enzymatic
reactions.
Communication is needed for organisms to respond to the environment and main""
equilibrium
• reduction and (iii) ribulose bisphosphate (RuBP) regeneration, indicating the rotes of
Organisms should be able to detect changes both from the surrounding envir,
within themselves so that they are able to respond to these changes to main
internal environment. This ability to respond to changes is made possible d
across the various biological systems as well as communication betwee11
Communication between cells can take the form of electrical or ch
nervous or endocrine system respectively. The endocrine system fabitfi:ates communication
between different cells through the release of hormones into the bloodstream. Binding of
hormones to receptors on or within target cells initiates signal transduction and eventually
results in a change in gene expression to bring about certain physiological changes. Defects
in any part of the signalling pathway often lead to detrimental-conditions such as metabolic
diseases and cancer.
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Transformation of Energy between the Environment and Organisms
Plants and other photosynthetic organisms use sunlight to synthesise carbohydrates from
carbon dioxide and water during the process of photosynthesis. The light-dependent (cyclic
and non-cyclic photophosphorylation) and light-independent stages of photosynthesis
facilitate the conversion of light energy to chemical energy in the form of carbohydrates.
Carbohydrates produced from photosynthesis can be assembled into macromolecules or
broken down subsequently to fuel activities within the plants. Carbon fixation occurs during
the tight~independent stage and the Calvin cycle ultimately results in the synthesis of sugars
in plants.
Qe plant matter, energy from the plants is transferred to them.
r during aerobic respiration whereby carbohydrates are broken
to phosphorylate ADP to ATP during aerobic respiration. The energy
'een interacting molecules through the four stages of aerobic respiration
resent. In the absence of oxygen, fermentation occurs with the release of
o!ecules and the formation of either lactate or ethanol depending on the cell
Identify components of chloroplasts and mitochondria in drawings,
photomicrographs and electronmicrographs.
(b) Explain the absorption and action spectra of photosynthetic pigments.
(c) Wrth reference to the chloroplast structure, describe and explain how light energy is
harnessed and converted into chemical energy during the light-dependent reactions
of photosynthesis.
(d) Outline the three phases of the calvin cycle in C3 plants: (i) CO2 fixation (ii) PGA
rubisco, ATP and reduced NADP in these processes that ultimately allow synthesis of
sugars.
{el Discuss limiting factors in photosynthesis and carry out investigations on the effect
of limiting factors such as temperature, light intensity and carbon dioxide
concentration on the rate of photosynthesis.
(f) Outline the process of glycolysis, highlighting the location, raw materials used and
products formed (knowledge of details of the intermediate compounds and
isomerisation ls not required).
(g) Outline the processes of the link reaction and Krebs cycle highlighting the location,
raw materials used and products formed (in terms of dehydrogenation and
decarboxylation).
26
Learnin£ Outcomes Communication and Equilibrium in Organisms
{h) Outline the process of oxidative phosphorylation including the role of oxygen and the
electron transport chain in aerobic respiration {names of complexes in the ETC are The emphasis of this section is on how cell signalling processes can cause a physiological
response in an organism. The circulatory system transports hormones from where they are
not required).
secreted to the target cells. Hormones bind to specific binding sites- receptors found on the
{i) Explain the production of a small yield of ATP from respiration in anaerobic cell surface membrane or within the cell -to initiate the process of cell signalling.
conditions in yeast and in mammalian muscle tissue.
Cell signalling comprises the following stages: ligand~receptor interaction, signal transduction
(j) Explain the significance of the formation of ethanol in yeast and lactate In mammals and amplification, and cellular response. Various molecules such as second messengers,
in the regeneration of NAO. kinases and transcrip.t,j~n factors mediate the processes of converting information from the
signal molecule fhOrm. One) into a cellular response. Insulin and glucagon are examples of
(k) Investigate the effect of factors such as substrate concentration, type of substrate Z-' '" cell signalling pathways to bring about responses to regulate blood
hormones th~t"'t!Jgg:er·
and temperature on the rate of respiration. glucose lev;el/~,,"X
,. ✓- ·-

{l) Outline chemiosmosis in photosynthesis and respiration (names of complexes in the ":.:,_-<·c-,,.,,
lt is ,-;important to appreciate the complexity and inter-connectedness of how the
ETC are not required). comrhuPi&tion systems within and between cells interact to achieve the required response.
,':,>~ :¾ai"~tenance of blood glucose levels will be used to illustrate how physiological responses
--~:'"~ri/egulated by controlling gene expression. Sufficient glucose in the blood Is necessary to
>( ·Provide cells with respiratory substrates. The pancreas detects the level of blood glucose and
,-0 secretes either insulin or glucagon to maintain a stable level of glucose in blood. These

hormones trigger cellular responses in liver, muscle and adipose cells when the hormones
bind to receptors. Signal transduction occurs through various proteins and molecules to
amplify and transduce the signal and eventually, elicit a cellular response. Thus, cell signalling
arid communication result in a relatively stable internal environment for cells in an organism
to function optimally.

leamirlf!. Outcomes

(m) Outline the mafn stages of cell signalling:

i. ligand-receptor interaction
if. signal transduction (phosphorylation cascade and signal amplification)
m. cellular response (change in gene expression)
(knowledge of Intracellular receptors is not required).

(n) Explain the roles and nature of second messengers (in duding cyclic AMP).

(o) Explain the role of kinases and phosphatases in signal amplification.

(p} Outline how insulin and glucagon regulate the concentration of blood glucose
through the respective tyrosine kinase receptor and G•protein linked receptor. (The
outline should be limited to describing how the llgand induces a conformational
change in membrane-bound receptor to trigger downstream signalling pathways that
elicit physiological changes in blood glucose concentration. Details of different
second messengers and specific kinases activated in the pathway are not required}.

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2.4 CORE IDEA 4: BIOLOGICAL EVOLUTION The process of evolution explains the diversity of life

Core Idea 4- Biological Evolution- helps students make sense of biology and the biodiversity
of life on earth. Three important concepts within evolutionary biology are the:
1. definition of evolution and descent with modification;
2. processes of evolutionary change, natural selection and genetic drift; and
3. patterns of evolutionary relationships {depicted as phylogenetic trees or cladograms).
Changes in the gene pools of populations can occur as a result of environmental changes
(including those caused by human activities) or major natural catastrophes. A diverse gene
pool is vital for the survival of species when such changes occur, Small populations are
especially sensiti.ve to these forces. Mutations in DNA and recombination during meiosis are
sources of variation; new genes and combinations of alleles may confer new phenotypes.

Students can frame their learning using the following questions:
• Why are there so many similarities among organisms yet so many different plants,
animals and microorganisms?
Why does biodiversity matter?
Natural selection is the major driving mechanism of evolution
The essential features of natural selection contribute to the change in the genetic makeup of
a population overtime. Darwin's theory of natural sele'ction (and, in parallel, Wallace's similar
observations and conclusions) states that inheritable variation occurs in individuals in a 1·
-:-:I.--··::,.✓ •
population.
Speciation and extinction have occurred throughout Earth's history and life continues to
evolve within a changing environment, thus explaining the diversity of life. New species arise
when two population,¾llverge from a common ancestor and become reproductively isolated.
Common core biofOgici:I processes e.g. metabolic pathways like photosynthesis and
respiration and,;ih_e \Clniversal genetic code support the idea of common ancestry.
~- ""'· '{,
Phylogenet~0 t~js are used to model evolutionary relationships and 'descent with
modification'. '." ·
~-t~- ~~-:~-,~-
¢,, \\

Due to competition for resources that are often limited, individuals with more favourable
variations or phenotypes are more likely to survive and produce more offspring, thus passing
on the alleles that code for those traits to subsequent generations. Fitness is a measure of
evolutionary success as indicated by the number of surviving:offspring left to produce the
next generation. It is worth noting that individual organisms do not evolve; rather, it is
populations that evolve.

As the environment is always changing, a diverse gene pool is important for the long-term
survival of a species. Genetic variation within a population contributes to the diversity of the
gene pool. Changes in genetic information may be silent (with no observable phenotyeic
effects} or result in a new phenotype, which can be favourable; detrimental or neutral to;t_!i'e~
organism. The interaction of the environment and the phenotype determines the fitness,,Of,. -·
the phenotype; thus, the environment does not direct the changes in DNA, but aru\u'Pcin
phenotypes that occur through random changes in DNA.· These changes 9_h'19t~Jve
alterations in DNA sequences, changes in gene combinations ·and/or the fomh1,ti6.n. ·of new
gene combinations. Note that there is no perfect genome for organisms. "(:""-'t;_ ,,/.-
"{:' "'.\,>c·/
A-,·::::-..
Although natural selection is usually the major mechanism for evoluti9n;)lgenetic change in
populations can occur through other processes, including mutat"fci"n,?tenetlc drift, sexual
selection and artificial selection. Inbreeding, small population siZ:e( non-random mating,
absence of migration and a net lack of mutations can lead to a loss of genetic diversity.

Evidence of evolution by natural selection is derived from a wide range of studies, e.g. in
biochemistry, morphology, genetic information from existing and extinct organisms, geology
and physical science. Phylogenetic trees serve as dynamic- models that show common
ancestry while geographical distribution and the fossil record' provide the evolutionary link
between ancestral and present-day organisms.

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Natural Selection and Adaptation Evolution and Biodiversity, Species and Speciation

Natural selection occurs only If there is both variation in the genetic information between Genetic information provides evidence of evolution. DNA sequences vary among species, but
organisms in a population and variation in the expression of that genetic information, i.e. trait there are many overlaps; in fact, the ongoing branching that produces multiple lines of
variation leads to differences in performance among individuals. The traits that positively descent can be inferred by comparing the DNA sequences of different organisms. Such
affect survival are more likely to be reproduced and thus are more common in the population. information is also derivable from the similarities and differences in amino acid sequences
and anatomical structures.
The interaction of four factors is considered in evolution:
1. The potential for a species to increase in number; Learnint Outcomes
2. The genetic variation of individuals in a species due to mutation and sexual Y0-_,
(f) Define biologfcal evolution as descent with modification and explain the link between
reproduction;
3. The competition for an environment's limited supply of the resources that individuals mlcro•exoJ~~i9iand macro~evolutlon.
need in order to survive and reproduce; and (g) Exi;il~i;t{O'Yi evidence based on homologies identified in biochemical data (molecular
4. The ensuing proliferation of the organisms able to survive and reproduce better in that ,,~o,ITJOJogies) and the fossil record (anatomical homologies), together with
environment. ":bioge:Ography, supports Darwin's theory of evolution.
,'\;,, ,,,,,
0

Adaptation results from the accumulation of favourable genetic changes through natural -Y'1:~{.·.hi!;3'ixplalnthe various concepts of the species {biological, ecological, morphological,
selection, since organisms that are anatomically, behaviourally and physiologically well-suited \. / ">-
to a specific environment are more likely to survive and reproduce. This differential survival \; /-
and reproduction of organisms in a population that have an advantageous, heritable trait (i)
leads to an increase in the proportion of individuals in future generations that have the
favourable trait and to a decrease in the proportion of individuals that do not.
ij)
Adaptation also means that the distribution of traits in a population can change when
conditions change. Changes in the physical environment, whether naturally occurring or
human induced, have thus contributed to the expansion of some species, the emergence of
(k)
new distinct species as populations diverge under different conditions, and the decline (and
sometimes the extinction) of some species.
genetic and phylogenetic concepts).
Define biological classification as the organisation of species according to shared
characteristics and describe how evolutionary relationship is established.
Explain how new species are formed with respect to geographical isolation {allopatric
speciation} and behavioural or physiological isolation within the same geographical
location (sympatric speciation}.
Define phylogeny as the organisation of species to show their evolutionary
relationships.

(I) Explain the importance of the use of genome sequences in reconstructing

Species become extinct because they can no longer survive and reproduce in their alter~l<,._
phylogenetic relationships and state the advantages of molecular methods, including
environment. If members cannot adjust to change that ls too fast or drastic, the opport~~~\;:_,'-"
multiple sequence alignment (nucleotide and amino acid)1 in classifying organisms.
for the evolution of the species is lost. r "-<;,/ 0-,''~~~~i';

learning Outcomes ~ '\~ \\, I

f' \:. \
(a) Explain why variation (as a result of mutation, meiosis and sexuaPr,epf'Oduction) is
important in natural selection. r(j:'~'>,";+
/'"'",,-cl''
(b) Explain, with examples, how environmental factors act as force$,of natural selection.

(c) Explain the role of natural selection in evolution.

(d) Explain why the population is the smallest unit that can evolve.

(e) Explain how genetic variation (including recessive alleles) may be preserved in a
natural population.

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 -------------------~-----------

2.5 EXTENSION TOPIC A: INFECTIOUS DISEASES Learnin_g_ Outcomes

(h) Explain the mode of transmission and infection of bacterial pathogens, using
Microorganisms, e.g. viruses and bacteria, cause diseases which disrupt the equlfibrium of Mycobacterium tuberculos;s as an example.
physiological systems in humans. This extension topic explores how some infectious diseases
are diagnosed and treated. (i} Describe the modes of action of antibiotics, including penicillin, on bacteria.

Students can frame their learning using the following questions:

• What cause infectious diseases?
• How does the body respond during an infection?
How can infectious diseases be prevented or diagnosed and treated?

With an understanding of how the human immune system funC:tions, students explore the
development of vaccines and how vaccines are used to eradicate infectious diseases like
smallpox. Yet, not all viruses can be eliminated by vaccines. The HIV and influenza viruses
infect humans. While vacclnations and treatment through anti-Viral drugs are available, the
viruses are stiJI present in the population due to their high mutation rate which could give rise
to drug-resistant strains. Besides viral infections, diseases can also be caused by bacteria!
infections. Tuberculosis is caused by the bacterium Mycobocterium tuberculosis. Although
successful vaccination programmes in Singapore have kept the in'fection under control, there
have been new cases appearing in the population and it remains a fatal disease in developing
countries.

Leamint Outcomes

{a) Describe the specific {adaptive) and non-specific (innate):immune systems including
active and passive, natural and acquired immunity.

(bl Outline the roles of B lymphocytes, T lymphocytes, antigen-presenting cells and

memory cells in specific primary and secondary immune responses.

(c) ~i:
Explain the relationship of the molecular structure of antibodies to their function. , '.''
using lgG as an example. r·)/ "··/
'c__,:/',
1
(d) Explain how genetic recombination during development results in milli~fq'~_:o'f
different antibody molecules (including somatic recombination, hyper-mu~a'tion•'ilnd
. \,\. '.',,
class switching). :4'~:'"':-¢
(e) Discuss how vaccination can control disease (including the eradifB~fB~~r~·~all pox),
limited to vaccination stimulates immunity without causirig/th'e disease and
F ·>,."
vaccination of a high enough proportion of the population1,cas;i break the disease
transmission cycle. ..,,,......

(f) Discuss the benefits and risks of vaccination.

(g) Explain how viruses, Including influenza and HIV, cause diseases in humans through
the disruption of host tissue and functions (including HIV and T helper cells, influenza
and epithelial cells of the respiratory tract),

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2.6 EXTENSION TOPIC B: IMPACT OF CLIMATE CHANGE ON ANIMALS AND PLANTS
Climate change, which is attributed to an increase in the emission of greenhouse gases, has
great impact on the human population. By the year 2050, climate change is expected to cause
the extinction of approximately at least one quarter of all species on land. In the oceans,
species such as corals, which are sensitive to warming temperatures, are also at great risk.
Many species have evolved to survive within specific temperature ranges and cannot adapt
to the new temperatures. In addition, the survival of a species is threatened when the species
it depends on for food cannot adapt The Intergovernmental Panel on Climate Change (IPCC)
has predicted that by 2100, the Earth's surface will rise by up to G•c on average. The effects
of this temperature rise on species and ecosystems will be catastrophic. Currently, the
following effects of global warming are evident: the melting of glaciers; the bleaching and
dying of coral reefs; extreme storms, droughts, and heat waves; and major shifts in the timing
of organisms' biological cycles.
Climate change is affecting the global ecology and ecosystem, e.g. loss of biodiversity and
impact on food webs. The study of biological processes is important in understanding and
taking appropriate action, e.g. the observation that many species are becoming smaller in size
can be explained by fundamental ecological and metabolic principles. There are also
consequences for both crop plants and protein sources, e.g. fish that are importantforhuman
nutrition.
As a small, low-lying city-state with one of the world's most open economies, Singapore is
vulnerable to the harmful effects of climate change, such as rising sea levels and the increased
frequency of rainfall.
Trends in our local weather records are consistent with the global observations of climate
change. The weather has become increasingly hot. Since the 1970s, Singapore has
experienced an average warming rate of o.2s•c per decade. The sea level has also risen. Tj£le
gauge data in the !;iingapore Straits shows that the mean sea level has increased by abouJ3_"'
mm per year over the last 15 years. More instances of short, intense rainfall have alsq-be,~n, 'i,
recorded within the last few years. /'" ii{,/ ·
"<t::)\
Extreme weather events can lead to changes in rainfall patterns, resulting in 'mofedntense
rainfall or drier periods. Flood, haze and water management will be of greate'rfn1'~,(frtance to
Singapore. In addition, an Increase In the frequency of extreme weather·JV:nts>'may lead to
unstable global food prices and disruptions to business supply chai~f~~lth wlH affect our
food imports and business activities in Singapore. ( , <,/
'"<~J>
Disruption of ecosystems and loss of biodiversity have major impacts on the emergence,
transmission, and spread of many human infectious diseases. For example, deforestation
reduces the diversity of forest mosquitoes, which are the vectors for dengue. The species that
survive and become dominant, for reasons that are not well understood, almost always
transmit dengue better than the species that had been most abundant in the intact forests.
Deforestation can also result in loss of habitat and food for species that serve as reservoirs
for human disease. The result_ant disturbance can bring the reservoir species into closer
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contact with humans, facilitating the spread of the disease to humans. An example is the
origin~! outbreak of Nipah virus infections in Malaysia.
Mosquitoes kill more people through the life-threatening diseases they spread than any other
predators. Furthermore, mosquito-borne infectious diseases affect millions of people and
debilitated people cannot work or support themselves. Climate change has inf!u'enced how
mosquito-borne diseases have spread in the world through the effects on the diseases'
vectors. Being in a region where two of the main mosquito-borne diseases (dengue and
malaria) are endemic, an understanding of the intertwined processes of how vectors respond
to climate change ~nd how climate change affects the spread of these diseases will be
important to SingaP'ore?·>
<,, -.;, .
,("""0;., ·'>
This topic ~plOf~the impact of climate change and three main areas of concern:
* The"tl~~d,,jr a safe and sufficient food supply;
• T.~,r~_tE!:at of how infectious diseases are changing; and
* _'T~e,p,illintenance of ecosystems as reservoirs for bio-resources like medicine and food.
>r.'<0. __ >~
/4;-~~tud~nts can frame their learning using the following questions:
·' \J ~ How can our way of life influence climate change?
• Why is there an urgent need to ameliorate climate change through an understanding
and application of the sciences?
Learnin_{ Outcomes
(a) Identify and explain the human activities over the last few centuries that have
contributed to climate change through increased emission of greenhouse gases
{limited to CO2 and methane) includirig burning of fossil fuels Unked to increasing
energy usage, clearing of forests and food choices (increasing consumption of meat).
(b) Explain the effects of climate change as a result of greenhouse gas emissions,
including the melting of polar ice caps, rising sea levels, stress on fresh water supplies,
heat waves, heavy rains, death of coral reefs, migration of fishes and insects, and
release of greenhouse gases In frozen organic matter.
(c) Explain how climate change affects plant distribution (vertical and latitude) and plant
adaptations, including morphology and physiology.
{d) Discuss the consequences to the global food supply of increased environmental
stress resulting from climate change, including the effects on plants and animals of
increased temperature and more extreme weather conditions.
{e) Explain how temperature changes impact Insects, including increased temperature
leading to increased metabolism and the narrow temperature tolerance of insects.
{f) Outline the life-cycle of Aedes aegyptl as an example of a typical mosquito vector.
36
Learnin_g_ Outcomes
(g} Outline the development of viral dengue disease in humans, induding host-pathogen
interactions, human susceptibility to the virus, pathogen.virulence, transmission and
drug resistance.
(h) Explain how global warming affects the spread of mosquito-borne infectious
diseases, including malaria and dengue, beyond the tropics.
(i) Discuss the effects of increased environmental stress (including increased
temperatures and more extreme weather conditions) as a result of global climate
change, on habitats, organisms, food chains and niche occupation.
Ol Discuss how climate change affects the rich biodiversity of the tropics including the
potential loss of this rich reservoir for biomedicines and genetic diversity for food.
◊ •
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3. PEDAGOGY
Teaching science involves tapping on the learner's innate curiosity and desire to answer a
question or solve a problem relating to science. Besides developing a strong conceptual
understanding of scientific models and theories, students are given opportunities to use
scientific inquiry and cultivate the ability to think and act in ways associated with scientific
inquiry. This includes students asking questions about knowledge and issues that they can
relate to in their daily lives, society and the environment; collecting and using evidence; and
formulating and communicating explanations based on scientific knowledge.
·et~an acquiring the facts and the outcomes of scientific investigations
Science is also a way of knowing and doing. Through the Practices of
Ould acquire an appreciation of the nature of scientific knowledge, the
~ as well as an understanding of the skills and processes in scientific inquiry:
of scientific knowledge: Students understand the nature of scientific knowledge
icitly through the process of 'doing science'. To complement this, an explicit
proach may be used. This approach utilises elements from the history of science or
the processes in science to improve students' views of the nature of scientific
knowledge.
• Science as a_n inquiry: Broadly, scientific inquiry refers to the different approaches by
which scientists study and develop an understanding of the natural and physical world
around us. lnquiry~based instruction could be used to develop the different aspects of
the Practices of Science together with the understanding of science concepts as well as
the dispositions and attitudes associated with science. Strategies that could be used to
support inquiry~based learning in science include questioning, demonstrations, use of
technology, as well as models and modelling.
Relating science and society: Students should appreciate how science and technology
are used in daily life. Learning science in a real-life context accessible to students can
increase their interest and enhance their awareness of the interconnections among
science, technology, society and the environment.
Science practical work supports the teaching and learning of science through developing the
Practices of Science, experimental techniques, practical manipulative skills and conceptual
understanding. It also cultivates interest in science and in learning science. In addition,
attitudes like objectivity and integrity, which are important in the learning of the discipline
of science, are reinforced.
38

4. ASSESSMENT
Assessment is the process of gathering and analysing evidence about stlldent learning. This
information is used to make decisions about students, curricula and programmes. Assessment
for Learning (Afl) is assessment conducted constantly during classroom instruction to support
teaching and learning. With the feedback about the state of students' teaming, teachers then
adapt their teaching strategies and pace based on the students' needs. Assessment of
Learning (Aol} aims to summarize how much or how well students have achieved at the end
of a course of study over an extended period of time. The A-level examination is an example
of AoL
This syllabus is designed to place less emphasis on factual material and greater emphasis on
the understanding and application of scientific concepts and principles. This approach has
been adopted in recognition of the need for students to develop skills that will be of long term
value in an increasingly technological world rather than focusing on large quantities of factual
material which may have only short term relevance.
Experimental work is an important component and should underpin the teaching and learning
of Biology.
4.1 ASSESSMENT OBJECTIVES
The assessment objectives listed below reflect those parts of the Aims and Practices of
Science that will be assessed.
A Knowledge with understanding
Candidates should be able to demonstrate knowledge and understanding in relation to:
1. scientific phenomena, facts, laws, definitions, concepts and theories
2. scientific vocabulary, terminology, conventions (including symbols,
units}
3. scientific instruments and apparatus, indudingtechniques of operation a
safety
••s. scientific quantities and their determination
scientific and technological applications with their social, econo
implications.
The syllabus content defines the factual materials that candidates need to recall and explain.
Questions testing the objectives above will often begin with one of the following words:
define, state, name, describe, explain or outline.
39
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B Handling, applying and evaluating information
Candidates should be able (in words or by using symbolic, graphical and numerical forms of
presentation) to:
1. locate, select, organise, interpret and present information from a variety of sources
2. handle information, distinguishing the relevant from the extraneous
3. manipulate numerical and other data and translate information from one form to
another
4. present reason~xp1anations for phenomena, patterns, trends and relationships
5. make compa.«5~'that may include the identification of similarities and differences
6. analyse a~'\iajuate information to identify patterns, report trends, draw inferences,
reportp~ions and construct arguments
7. jusf~ions, make predictions and propose hypotheses
8. ·ledge, including principles, to novel situations
skills, knowledge and understanding from different areas of Biology to solve
lems
organise and present information, ideas and arguments dearly and coherently, using
appropriate language
These assessment objectives above cannot be precisely specified in the syllabus content
because questions testing such skills are often based on information which is unfamiliar to
the candidate. In answering such questions, candidates are required to use principles and
concepts that are within the syllabus and apply them in a logical, reasoned or deductive
manner to a novel situation. Questions testing these objectives may begin with one of the
following words: discuss, predict, suggest, calculate or determine.
C Experimental skills and investigations
candidates should be able to:
1. follow a detailed sequence of instructions or apply standard techniques
2. devise and plan Investigations which may include constructing and/or testing a
hypothesis and select techniques, apparatus and materials
3.
4.
use techniques, apparatus and materials safely and effectively
make and record observations, measurements and estimates
S. interpret and evaluate observations and experimental data
6. evaluate methods and techniques, and suggest possible improvements.
40
4.2 SCHEME OF ASSESSMENT Paper 4 (2 h 30 min, 55 marks)

All candidates are required to enter for Papers 1, 2, 3 and 4. This paper will assess appropriate aspects of objectives Cl to C6 in the following skill areas:

• Planning (P)
• Manipulation, measurement and observation (MMO)
1 Multiple Choice 15 30 • Presentation of data and observations (PDQ)
2 Structured Questions 2h 30 100 • Analysis, conclusions and evaluation (ACE)

3 Long Structured and Free-response 2h 35 75 The assessment of skill area P will have a weighting of 5%, and the skill areas MMO, PDQ and
Questions ACE will have a weighti~f 15%. Candidates will require access to apparatus, as stated in the
Confidential Instruct~. hr some questions, candidates may be allocated a specific time for
4 I Practical I 2h30min 20 55
per 4 may include data handling/interpretation questions that do
ln order to test the skill areas of POO and ACE.
Paper 1 (1 h, 30 marks)
l
1T allowed to refer to note books, textbooks or any other information in the
This paper will consist of 30 compulsory multiple choice questions. All questions will be of the
direct choice type with 4 options.

Paper 2 (2 h, 100 marks)

This paper will consist ofa variable number of structured questions, all compulsory, including i/~t1i1~tl ::?ffA~i~t19~i~~i~~:#Jrtf~t7::~:,! i.i~~t,r~?:: ~~~~~~t~ffiitf~~~:;i
data-based or comprehension-type questions. These include questions which require
knowledge wit~ understanding 32 Papers 1, 2, 3
candidates to integrate knowledge and understanding from different areas of the syllabus.
Handling, applying and evaluating
Paper 3 (2 h, 75 marks) B 48 Papers 1, 2, 3
information
This paper will consist of a variable number of long structured questions, all compulsory, C I Experimental skills and investigations 20 Paper4
including data-based or comprehension-type questions and one free-response question of 25
marks. These include questions which require candidates to Integrate knowledge and
understanding from different areas of the syllabus.
◊
For more information on assessment, please refer to the Singapore Examinations and
Assessment Board http·(lwww.seab.qov.sg/.
Section A {50 marks) comprises two or more compulsory long structured questions. Th1;
be one or more stimulus materials which may be taken or adapted from a source
scientific journal or book which may not necessarily relate directly to the c1
syllabus. Questions may require candidates to explain terms used in the
data,justify decisions, perform calculations and draw conclusions based on'
stimulus material.

Section B (2S marks) comprises two free-response questions, fro

choose one. The quality of scientific argumentation and written communication will .be given
a percentage of the marks available.

41 42

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 Reece, J.B., Urry, L.A., Cain, M. L., Wasserman, S. A., Minorsky, P. V. and Jackson, R. B. (2011)
5. TEXTBOOKS AND REFERENCES Campbell Biology (Ninth Edition) (Pearson Higher Education) ISBN 0321739752

Students may find the following references helpful. Russell, P. J., Hertz, P. and McMillan, B. {2013) Biology: The Dynamic Science {International
Edition of Third Revised Edition) (Brooks/Cole) ISBN 1133592058
Alberts, B., Bray, D., Hopkin, K., Johnson, A. 0., Lewis, J., Raff, M., Roberts, K. and Walter, P.
{2013) Essential Cell Biology (Fourth Edition) (Garland Science) ISBN 0853696470 Sheridan,J A and Bickford, D P (2011) Shrinking body size as an ecological response to climate
change. Nature Climate Change 1:401-406
Alberts, B,, Johnson, A., lewis, J., Morgan, 0., Raff, M., Roberts, K. and Walter, P. (2014)
Molecular Biology of the Cell (Sixth Edition) (Garland Science) ISBN 0815344643 The National Center for Science Education. Climate Change 101.
http://ncse.com/cli'.(~mate-change-101
Alley, RB (2000) The Two-mlle Time Machine {First Edition) (Princeton Science Library) ISBN
9780691160832 he US National Academy of Sciences {2014) Climate change:

Bickford, D, Howard, SD, Ng, 0 J J and Sheridan, J A {2010) Impacts of climate change on the .org/toplcs-policy/projects/climate-change-evidence-causes/
amphibians and reptiles of Southeast Asia. Biodiversity and Conservation.

Dobzhansky, T (March 1973) Nothing in Biology Makes Sense Except in the Light of Evolution,
American Biology Teacher vol. 35 (3)

Jones, M. and Gregory, J. (2001) Biology 2 cambridge Advanced Sciences (Cambridge

University Press, www.cambridge.org) ISBN 0521797144

Krebs, J.E., Kilpatrick, S. T., Goldstein, E. S. (2013) Lewin's Genes XI (Eleventh Revised Edition)
(Jones and Bartlett) ISBN 1449659853

Lodish, H., Berk, A., Kaiser, c. A., Krieger, M., Bretscher, A., Ploegh, H., Amon, A. and Scott, M.
P. (2012) Molecular Cell Biology (Seventh Edition) {W H Freeman and Co) ISBN 142923413X

National Research Council (2010) Advancing the Science of dimate Change. The National
Academies Press. ISBN 978-0-309-14588-6 {book). 978-0-309-14589-3 {PDF}
•
National Research Council {2012) Climate Change: Evidence, Impacts, and Choices. ISBN
0-309-27842-3

Nova {Australian Academy of Science), Earth and Environment.

http://www.nova.org.au/category/earth-environment

Pfopper, G., Sikorski, E. and Sharp, D. {2014) Lewin's Cells {Revised Thiri
Bartlett) ISBN 1284029395

Pomerville, J. C. (2013) Fundamentals of Microbiology (Tenth Edition) (Jones and Bartlett)

ISBN 1284039684

Raven, P.H., Johnson, G. B., Mason, K. A., Loses, J. and Singer S. (2013) Biology (Tenth Edition)
{McGraw-Hill) ISBN 007338307

Reece, J.B., Taylor, M. R., Simon, E.J. and Dickey, J. L. {2013) Campbell Biology: Concepts and
Connections {Seventh Edition) (Pearson) ISBN 1292026359

43 44

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How to study Biology
Study Skills for Biology
Your previous learning skills may need to be changed as you advance to 'A' level. Leaming for 'A' level
Biology is not simple regurgitation but requires in-dept understanding and application. You cannot
simply reproduce standard textbook answers.
You need to think, connect, relate and apply to the appropriate situation. You are like a car mechanic
who is familiar with his tools and skill sets. If you encounter a problem with the hydraulics of a car, you
will know what tool to use and how to use it. If you change the model and make of the vehicle, you are
not stumped, because you understand the mechanics and workings of a car. The "tools• here refer to
your in~depth knowledge of Biology and your understanding. The mskill setsn is how you apply this
knowledge and make connections to solve problems. Teachers cannot possibly giVe you every
permutation and combination of ~model answers• for you to memorise! Would a customer rely on a
mechanic who simply memorizes protocols or a mechanic who is able to think, and apply his/her
knowledge to a right situation? You decide on who you want to be.
Revision Skills
When you revise, you need to balance your time between:
Studying your notes/summaries
Practicing past paper questions
Reviewing tutorials, tests and exam questions that you have already
done and learning from your mistakes.
Before you start:
Make sure you have a copy of the syllabus. The cover page of
every topic of your lectures notes has the relevant learning
outcomes (outlined in the syllabus) for that particular topic. Make
sure you read through them carefully and keep them in mind as you
are reading through the notes
Some helpful ideas
1. Work out your best way of learning. Some people learn best from diagrams/,
computer while others prefer listening and making up rhymes and phrases.
something active with information like answering questions or making poster
learning techniques can be very helpful.
2. Test yourself! Just reading through the notes will not make them someone to test you
on a section of work. Alternatively you could write down some especially using the
learning outcomes and then try to answer them. Check your notes clarification if you are not
sure.
3, Teach others! If you can find someone to teach, especially your peers, then it is the best way to
learn. Questions asked by your "students~ may challenge your understanding of the concepts and
prompt you to learn more. You can take turns to present a topic to each others.
RV Biology/ Prepared by Mr Low Chor Meng
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4. Make sure that you understand completely! It is unlikely that you will remember much biology if
you do not understand itl However, there are still things you need to learn by heart e.g. a
triglyceride is made of 3 fatty acids molecules and a glycerol molecule. There is no way to work
that out from first principles so know your facts! Also it is good to memorize as well as understand
your definitions as the wrong use of a word may lead to a totally different meaning.
5. Link concepts of different topics. To understand a topic more thoroughly, you should not
consider each topic to be independent of another. For example ATP is linked to respiration,
photosynthesis, plant transport, nerve impulse transmission and any process that requires energy.
6. Come to tutorial prep~d. Complete all the tutorial questions you are assigned to do on your
own1 It is not expec~iGI o u to answer an the questions correctly so that 1s what tutorials are for.
Raise questions du~ orials to clarify your doubts. If you have the time try all other questions
besides those yoecl>to complete for you lessons
Some Revisio~"31,iques
1. Get an ~~1twiew of the topic first. Before you start revising a top1c, quickly read through the
whole tc11l\,_sa"that you have a general understanding of it and of how the different bits of it connect
~ther. A good place to start is the summary shown at the end of each chapter of a
,xt. The contents page of your notes may also help.
hlight Key Words* and phrases in your notes using highlighter pens in different
·colours.
Make notes/summaries. Rewriting and condensing notes is a good and active way to learn and
then understanding what you need to learn.
4. Make yourself cards with notes on one side and a diagram on the other. Test yourself by looking
at the diagram and seeing if you can recite the notes.
5. Visualisation. When you are memorizing material, always
try to get a bold and bright picture in your mind that will
help you to remember. It helps if the picture is something
which is important to you such as your girl/boy friend, rock
group. Sometimes imagining something outrageous that
can be connected to the fact may help.
6. A Poster. You can summarize a topic which you can put
on the wall of your bedroom. Include key words and
phrases in large, bold letters. If you are a visual person .6-'~.,;..,, ~J),t<,,..;...., c.,.~;,'le,o~~
then include bright, colour diagrams which illustrate the
Use visualisation
ideas.
7. A Mind Map. This is a poster which summarizes a topic by showing the links between the different
concepts that make it up. Making a mind map forces you to think about the topic and help your
understanding of it.
8. Use Mnemonics, rhymes and phrases.
Some people are good at rhymes or raps and this can be a way of memorizing work. e.g. King
Philip Came Over From Greece Singing for taxonomy of Kingdom, Phylum, Class, Order, Family,
Genus, Species.
Rlf Biologyf Prepared by Mr Low Chor Meng
9. Animations using computer. Making a revision timetable
Use internet to search for animations that can illustrate a concept clearly. Some recent research suggests that some students do better in exams than others because they;
Start their revision earlier
10. Practice calculations. Use better techniques for learning work such as testing themselves,
Calculations are involved in some topics such as Genetic crosses. You can learn by rather than just reading their notes ,i
looking at a worked example, understanding the logical steps b8tween the Jines, covering it and Get help from others rather than working alone
trying to solve the problem and referring to it if you are stuck. You should then try other questions. Have a planned revision timetable which includes working on their
weaknesses. ,1

What will you revise?

You will divide your time between:
1. Studying your notes. sr.,,r:,-.,.-,,..,r.y
2. Practising questions to gain experience in answering questions. It also tests your own
understanding and helps identify weaknesses.
Sources of questions include those from text books, past years 'M level Qs, past years common
You can use these idea
1. Start your revision
¥P
you plan a revision timetable.
rib-time before your exams (at least 10 weeks).
test and promo exam questions and prelim exam questions from RI and other colleges (from Plan to spend ot of the last 2 weeks before your exam on
library). revising ,pies again.
Organising Revision 2.
Do you have difficulty starting revision and feel that there is so much to do that you will never complete
it? Do you constantly put off revising and find other things to do? These are some ways to help time on your weaker areas. Try to get extra help on them
yourselt 1cher. (Don't just do the things you are good at already!)
1. Think about the positive effects of starting

-
yourself enough time to do past exam questions.
When you have finished a session you will feel good that you have
made progress and will feel less anxious about getting enough work Schedule in consultation time with someone who can help. l)o~"""' '°"""'~ ~ ~
done,
Have breaks in between revision sessions, so that you don't go
2. Think about the negative effects of delaying completely crazy!
Don't let problems compound until it becomes unmanageable later➔
snowballing effect
How long should you revise for?
3. Give yourself rewards Research suggests that your efficiency in learning declines with time. See first graph.
Think of the things you can reward yourself at the end of the session
e.g. a cup of coffee or listening to some favorite music.
Four 25 mins sessions with a break of 10 mins in between
4. Get help! them is better than one 2 hr session as refer to the second
You can involve a few friends in group discussion or graph,
consult your tutors for difficult concepts that will make
subsequent revision easier.
1hour 2hour
""'

0 1 hour
,.,.
2 h«ir

ShOrl revision sessions are more effective

RI/ Biology( Prepared by Mr Low Chor Meng 3 RI/ Biology/ Prepared by Mr Low Chor Meng

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.<1',,
The 3 rd graph shows what % of the revised material is 7. Write neatly and in short sentences that will be easier for the marker to understand. Try to be
remembered after you have stopped. precise and detailed without writing too much, so that you don't waste time.

8. For structured question, always write within the lines provided. If you are writing much more, you
As it shows, you very quickly forget material that you are wasting time as the number of lines usually determines the amount of words needed.
revised.
9. If diagrams are required, make them clear and neat Annotations are acceptable as part of the
10mln 1doy 1week time- answers but not just labels. Do not spend too much time on drawing. If you decide to include
diagrams yourself they should supplement your answers or make them clearer.
Recan /alls rapialy aftfill' one revision session
required questions. Some students may miss a question on the last
The 41h graph shows that if you revise work again after 1O
mins, then the amount you remember increases.
11. in if you finish earlier.
So what should you do after you have your 10 mins break
after working for 25 mins?

You should briefly review what you have been studying

10min 1 week time
making mental summaries.
""'
(Hotizonrar axes not r.Jrawn 10 scare!)
!f you then revise the material again after a day and then
after a week then you remember even more of the work, as
shown by the last graph.

The trick is to make short notes/ mind maps and use these
·,,,.1~,"'~°"'r,:;l;,oo~-~""'I"""""""'""' ,,,. .,,,.,c,<>·.,, ..,.,•...,... ,,
to briefly revise a topic again at regular intervals!

Some hints on answering questions

1. If the question is worth 4 marks you must have at least 4 points.

2. For structured questions, if it carries 10 marks it means you should spend no more than 10-12 mins
Exam Technique on that question. An essay question of 20 marks requires approximately 20-24 mins.

During the exam
1. Don't waste time when you get the paper! Read through the instructions on the fro1
exam.
2. Once the exam begins, read each question carefully and underline important
have a choice for the questions as in essays, read through all the q
Remember that some later parts of some questions may be easier or your,
3. Use correct scientific key words in your answers.
4. Questions that involve calculations require you to show the steps. And don't forget the correct
units.
5. In MCQ, narrow down your options by .crossing out those answers which are wrong. Also read all
options as you need to choose the best possible answer. If you are not sure ... guess.

3. Don't dive into a question without reading carefully and know what the~ Co./: 6. When a question requires you to read the graph, quotes relevant figures to support your answer.
Also remember to write down the correct units accompanying these figures.
4. Don't spend too much time on any question! It is not Worth as it is easier to get 50% on all
questions than 100% on half of them. 7. When attempting question that compare 2 things, you are to point out the similarities and
differences. In a question that requires you to contrast 2 things, you point out the differences. Do
5. Do not leave any blanks, put in your best answers even though you may not be sure. You may just so in a table form so that you make point-to~point comparison. (But answers must be written out in
get 1 or 2 points correct. complete sentences). Avoid ~have" and "have not" statements. It is good to have a column stating
the "point of comparison".
6. Sometimes you are stuck on one part of the question. Check to make sure there are no later parts
which you can do easily.
RI/ Biology( Prepared by Mr Low Chor Meng 5 RI/ Biology/ Prepared by Mr Low Chor Meng

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{A) POTENTIALS
in \M~Oc m\'=: lo,v'&l'f-'--'l'[,,',c-r=~~-~~~~
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NAME: CT GROUP:
a. "Water Potential

The water potential, 'l'w or simply 'f' of a solution refers to the net tendency for the water molecules
WATER POTENTIAL to leave the solution by osmosis. It is measured in the unit of pressure kilopascal (KPa).
f.,=O
At standard temperature and pressure, pure water has a water potential of zero kPa.
This is the maximum value for water potential unaer these conditions.

The presence of solutes lowers the water potential, making it negative.

Candidates should be able to: . ,? "'- YM~ tf:- Wr.W/' V1\'Q'1Al'I~ -.:\ltt) Ulr"
When solytes are dissolved in water, these molecules/ions interact with water molecules, forming
hydration shells around the molecules/ions. This lowers the number of free water molecules that can )
Investigate the effects on plant cells of immersion in solutions of different water potentials.
To determine the mean solute potential of cell sap in a sample of plant cells using the diffuse out of the solution. (Fig. 1) SC) (~ctreele(.---\'iOYi~i\VV) lWTI'II fretr ¥%"
method of incipient plasmolysis. ,,: '
M\ H at _....~---·
• Use the knowledge gained in this section in new situations or to ~related problems.

* These points above, although not explicitly mentioned in the syllii'""·'~ critical knowledge for
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TABLE OF CONTENTS "flri'M M"tW'C'ic.tfOYto V\llfvl o~{)-13 o l o o
<o • Qi v,Jf@Y ~o:w!Ollnl!"aliol'I Hlgheoncentral!oil
(A) Potentials .. n,;:_ ✓ Hydration ~%dso!Ulemo1Elcules otsa1Utern018Cu18s
,:,;_v D shell '\,v U'Wconcellrm5on

:: : .:.~:::::,-:::::::::::::::::::;~::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::: :
High~
~ ,\' ofwatarmolecoles ofwatormoleall&s
~ ~ Highwaterpolel"llial LD,Vwa1erPolential
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,.,, a.
Fig 1.: {a)A dilute solution and{b) a ~centl-ated
solution. lncfrvidual sucrose "'1,~lltes are
NetrnoY8f119111:olwalefmol!!Wes
fig 2: C-ondrtions on the 2si-des of the
membrane and the terms used to
hydrated by water molecul~'('§flrrounded by descnbe them. The large black blobs
(C) The effects ofwaterpo~6f:!J~n cell ........................................................................... 7 hydration shell). More wa~olecules are free represent sucrose while the .smaller
o'v to move about in a dil~lufion as compared
to a concentrated
white circl~ represent water molecules.

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The higher the solute ntration, the more negative the water potential.
The lower the solute tion, the less negative the water potential.
- ·+· ' .
•® The higher the water potential (less negative) of the solution; the greater the tendency for the solution to
lose water to its environment.

The lower the water potential (more negative), the lower the tendency for the solution to lose water to !!§.
environment

Water diffuses from a region c,f high water potential to a region of low water potential, down its
water potential gradient.
E.g. Net flow of water is from region that is less negative (e.g. - 700 kPa) to the region with more negative
water potential (e.g. - 800 kPa).

Osmosis = the net movement of free water molecules from a region with higher (less negative}
"This handout is the effort of several Biology teachers at RI. It has and will continue to be updated. water potential to a region with lower (more negative) water potential through a partially permeable
"" Any information given in a double-lined box is for your information only. membrane.(Fig 2)

Last updated by Mr Low Chor Meng, Mdm S Cross, & Mr Derek Tan
Last updated by Mr Low Chor Meng, Mdm S Cross, & Mr Derek Tan 2

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Raffles Institution H2 Biology (Student) 2018-2019
Raffles lnstib.d:ion H2 Biology (Stlldent} 2018-201!:l
~--------------------------------------------------------------,
I I cell wall pushes against eel surlaca
: Q1: Which cell has a greater potential, cell X or cell Y J
memb(2r11>" pressure potential
I ~~~,-_~-,,7:~ I

:I yJ:J>;l{:'.):J\\ A: 00\\ \ :I Fig 3: Pressure

: A~s'il1i 'I,: c.i,ii1f'; l.'t~1aei~1:I Q2: Look at the three cells X, and y z. In which direction will l potential in plant
cells. cell GIJ!!ac8 membrane
! osmosis occur within these cells? 1 ~es against ce~ wan

Gt~~~~~~~~~~
Turgor P,renura

:I . . A: ffS'\IVI Y\~fi)[cff :I
L__________________ trnwlO?F _______________________________________ J

b.:'.'s·orute 'Potelltla1 cell surface

membrane
central
vacuole
tonoplalst

Dissolving solute molecules in pure water reduces the concentration of free water molecules and hence
Hence, water potential is the sum of solute potential and pressure potential:
lowers the water potential.
Water potential = Solute potential + Pressure potential
All solutions therefore have more negative water potential than pure water. '('
'f!w = 'f!, + 'f!e~~
The extent by which solutes lower the water potential is known a! ~ t e potential, 'l's.
I
----------------------------:0·
~. if"'
·-------,I t
I
The value is always negative. ToefffiOfe}olute molecules/ions th~e, th~ more negativefihe ~elute I I
potential. · ~ ' I
I
I
I
I
-----------------------------------i -----------------------,I I lnanim~ I
J
I
Q3: Does 1M NaCl or 1M sucrose solution have a more n solute potential. Why?
I
) a --r po en 131' = Solute potential I

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~~ ~sine,
!1________________________ _ there is no cell wall)
____________________ [I
: A, IM NO Ct. NO(t ~'°"1)\ye, 1' !,c,vi NA-,. a - fllVlS (-lli\e,,m,, ~" """1,eeo1)1 wn,tw,ch,,c
: k, 2x "". 11\1\Yibe,r Vf rat< foYYl'l h~~vP,if!)V) si,,Mi<, ctoesi M/r
J W'Wi'ftlveol -te &IA "."¾.\ d1&soC{a_\tc,
: 4 ,w~I 10 " 0""'ter v,,te,,l-
IIM'&.r ,so1utt, ~trc I
1 1

L--------------------fl.'-o---------------------------------------
I

V
~•

q . -f"'a)'
:

c.\J,_reSSUfe:pajei,'ti,S:J';..·_6:,r.'.P~nly: HI.J Vel1}nl!L..........._c,\,j0/~

• Since plants have a cell~an additional factor, the pressure potential ('Pp), needs to be considered
when calculating wat~ential in plants.
U · AA& '°
~ ~l<\f of- W"flN 1,-j ,;w,o;(S
Pressure potential, 'Pp, refers to the pressure exerted by the cell wall on the plasma membrane. /\

When a plant cell is in a solution with a higher (less negative) water potential, there is a net movE!ment
of water into the cell.

Due to the presence of the cell wall, the pressure of water inside the cell builds up and_e_ushes the cell
membrane against the cen ~11 (turgor pressure).

The cell wall in turn will exert an equal but opposite force against the protoplast. Th·1s is the pressure
potential. (Fig 3) U) , 11
\Jll!.tfTT \P II>
The plant cell will take up water until the)solute poten@fthe cell contents is matched by th Pressure
P0tent1al. )l1.e. the tendency to draw water into the cell is equal to the tendency to force water o of the
cenr-
Pressure potential is equal in magnitude to turgor pressure but opposite in direction.

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0
c;cncentra110n 01 ~mal so1Ution oeereasing,---- water enters vacuole expands
Cell VO!UIM increasin,-
'400 vacuole by cytoplasm pushed outvv"ards

c,llowall
□- - ·o· - ·o
•300 ~ell placedrn eaernal oosmoso stretched
·+200·

•100 ., :i=~::~
than that of the cell sap ·
i
--~ ~ •

§!
cellulose / ~I:~~~
I ·100

·200 wall~
cytoplasm
·- partially
·300 turgid
··~ • -·' plantceTI
~00

o. ."'. !:~#oves.
000 ,
vacuole
conr.aining ~water leaves :£,,,.,(',,
\, .
Full pl~smolvsfs '
lllcl)lle11t~Jasm11lysis ,,,(j ' cell sap vacool? by
osmOSts .. G0
: ~" '
i ~·:
o·•·.,}
oleshrinks, inwards
8
@•
m '
-
Zaro-lurgor
'l'p = 0 ~
~
"S::,,"'-1:j
l"h:
:~ {_ __
Fullturau
'l'p = ·'I's
Ce11 placed io ""'mal
solutionwhosesolute
concentratfon is hfgher
than that of the cell sap
·
.
.. · ,·
c=='\\
--+~--+ ·
."
,,..(',p"l ient
..,eo,V""'tasmolysis
F0,
· -~-+

Fig 5: The effect of immersing a partially turs~ant cell in (A) pure water and (8) a solution whose
lk::#

full
plasmoJysis

'Yw=&·"" 'Yw=O solute concentration exceeds t h ~ t h\" cell sap in the vacuole. Since the cell wall is fully
permeable to both water and so the external solution passes through the cell wall and
Fig 4: Graph showing the relatio~~~een the water potential, solute potential and pressure
potential of a plant cell at d ~ n t stages of turgidity and plasmolysis.
0 ~·
fills the space between the c~ll vi • and the cytoplasm.

'>.Cj What is 1:uri:jidity? · -;:;Cj

I {B) THE RELATIONSH1lfJ-lE-tWEEN 'Yw 'l's and '¥p
Fun turgor occurs whe~~t cells reach tlie maximum size permissible by the rigid cell wall. Full
"
What is]da_Sn101'ysi_S?(;if turgidity, that is maximu , is achieved when the cell is placed in pure water. At this state, there is
no further net water u and the cell is in equilibrium with the surrounding.
Plasmolysis is the shrinkage of the protoplasm from the cell wall of a plant cell due to loss of water
from the cell. Experil"lient to determine th8--ffll!'al1 'SO"iiite· DQte.ntial of·tlie· ce\fS3p in a sample of plant cells.
To detennine the solute potential of cells, you need to find out the point when all cells reach and remain
o Full plasmolysis occurs when the cytoplasm shrinks to the extent that the cell membrane pulls away in the state of incipient p!asmolysis.
from the cell wall completely. In this state, rehydration is not possible to revive the plant cell, the
shrinkage is pennanent and the cell will die. (Fig 4) ( vt711C· M rnllQlUwi = /Al\f1C• lV! ce,./1) In reality, solute potential varies between cells in the same tissue and so they may plasmolyse in solutions
- hrrt At "'lr/1,\ 1m.w,,. w, ner
wiove,1111,nt "'H~JD
of slightly different potentials.
o Incipient plasmolysis occurs when the cell membrane is about to begin to puh away from the It has been found that incipient plasmolysis is reached when 50% of the cells are plasmolysed while
cell wall. At this point, the pressure of the protoplasm against the cell wall is zero. Thus, at the other 50% of the cells are unplasmolysed. Thus the average cell is said to be at incipient
incipient plasmolysis, '¥P = 0 kPa . · p!asmolysis. At this point, there is no net movement of water in and out of the cells.
lt makes use of the following relationships:
~~
a . ~

At this ~ressure potential is zero since no pressure is exerted by the protoplasts against the cell
walls, s ~ J Z J ; g ;,;;§iii)¥¥ f -&Bil& i.e. the solution that causes incipient plasmolysis
has the same solute potential as the cell sap.
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Samples of tissue being investigated are allowed to come to equilibrium in a range of solutions of different
concentrations (water potentials). I]§ THE EFFECT OF WATER POTENTIAL ON-CE[_b$
Aim is to find the concentration (water potential) of the solution that causes incipient plasmolysis.
Erid(i'sirlOSis : Net entry of water into cell
Thus the concentration of the solution that causes incipient plasmolysis can be obtained by plotting a ExOSmosiS : Net loss of water from cell
graph of percentage of plasmolysed cells against concentration of the solution (fig. 6}.

I 100
_?;,

i
0.
50 1------------
0.38 (molarity at which 50% of
''
a 01 ,
0.1
::::r::::::::,
0.2 0.3 0.4 05 0.6 0.7
,(
,1
cells are pfasmolysed)
, , 1

Fig. 6 Percentage of onion

Molarity of sucrose solution
epidermal cells plasmolysed
~~ "'"'
~'"
i'! {t~ent concentrations of
sucrose solution ~,
~ ''"
plo.sma'
Another graph of solute potential against the molarity ofth, ,n (e.g. sucrose solution) using data in
table 1 can be plotted and used in finding the correspond] potential at a particular concentration mt~
of the solution. 1~

After plotting the graph using the values below, f i n d ~ corresponding solute potential when molarity
1Y.
of sucrose solution is 0.38M. •" ~f]j (a) (bhl)><$:' (c)
Table 1. Solute ootentials r. "&.'bi'ven sucrose solutions at20 °C
O.Q ' ~"
~

.
Concentration of sucrose 0.2 0.3 0.4 0.5 0.6
solution/ molarity
G (j)
Fig. 7. Effect of wate~Qntial on animal and plant cells.
Solute potential/ kPa

:S
( t;'":260 -540 -820 -1120 -1450

~~f61'1 ~ frvt'1
lit h,H't!t dJn::'IMJ
-1800 • When the cytoplasm of a cell ha
environment surrounding it, this

Thus the
# er water potential (less negative water potential) than the
the exosmosis of water into the environment. (Fig. 7c)

(Q protoplasl'IJ~lant cell shrinks away from the cell wall and the cell is said to be
u~o tm,tw,s,<,°tl""o '1'- <til,- plasmol~he plant cell retains its shape due to the rigidity of the cell wall.

(ii) animaGn becomes shriveled or crenated due to the absence of a cell wan.

•@When the cytoplasm of a cell has a lower water potential {more negative water potential) than the
environment surrounding it, this results in the endosmosis of water into the cell. (Fig. 7b)

Thus the (Q protoplasm of a plant cell expands and the cell becomes turgid.

{ii) animal cell expands and may burst or lyse.

If the cytoplasm of a cell has a same water potential as the environment surrounding it, the
cytoplasm has a '¥wthat is equal to that of the environment. (Fig. 7a)

Thus there is no net movement of water between the cell and its environment. The cell thus remains
visibly the same.

[Note: Terms such as hypertonic, hypotonic and isotonic should not be used. Instead, refer to the
relative concentrations of the solutions and how water moves due to the difference in water
potential between them.J
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Cellulose cell wall

Solution with low

water potential
nucleus

You may not always get c~

identify plasmolysed ce~
(j

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Raffles Institution H2 Biology (Students) 201s.2019
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CORE IDEA
I (A) INTRODUCTION

(1) The Cell and Biomolecules of Life Carbohydrates are organic compounds consisting of the elements carbon, hydrogen and
oxygen.
Biological Molecules Carbohydrates are carbon-containing compounds that are hydrated. Hence, their general formula
can be written as~W~'IW where m and n are variable whole numbers.

CARBOHYDRATES They are the most abundant biomolecules on Earth. Most carbohydrates found in nature occur as
polysaccharides.

Content Carbohydrates
The structure of carbohydrates and their roles in living organisms.
Simple Complex
Learning Outcomes
(g) Describe the structure and properties of the following monomers : A
(1) a•glucose and ~•glucose (in carbohydrates)
(h) Describe the fonT1ation and breakage of the following bond:
~' ~
Q
Monosaccharides Disaccharides Oligosaccharides I ~ty,saCChandes
(1 monomer) (2 monomers)
(i) glycosidic bond (in carbohydrates) ~ G
(i) Describe the structures and properties of the following biomol~~ and explain how these are
(3 .1 0 monomers~
. ' '
~'loo monomers)

'~
related to their roles in living organisms:
(i) starch Qncluding amylase and amylopectin)
(ii) cellulose
~-..--
;f;:;J
KV
(B) MONOSACCHARIDES ;s;,,·
(iii) glycogen 0 Characteristics:
(a) a carbohydrate which cannot be hydrolysed ,(\,,.
~l;'..···;
'a-
'!'c«l'O :+- Carbonyl group
Other important learning outcomes not speci~cpf~ntioned in syllabus to simpler carbohydrates ~"" •1-·-:
Cany out tests for reducing and non•reducin)t$._~~e{including semi•quantitative use of the (b) has a carbonyl group :r::
C = 0) .. ~ H-r+:OH1+- A hydroxy! group
Benedict's test), and for starch (potassiu~'Rxlid'e solution test) (c) has multiple hydroxyl groups ( - 0 ~ _ ~~ HO-c-'..:.1-1_.,
(d) general formula -11(,l§Jlf'q©J;fwhere n = 3 t I
(e) most names for monosaccharides end se, H-r-OH
References \,_ with pentoses (with &-carbon atoms~ exoses H-C-OH
(with 6-carbon atoms) being mos.h:ommon I
Campbell, NA and Reece, J.B. r ~ t Biology (9 th edition), Pearson Benjamin•Cummings, San
e,.,,fiCJ.,,
n,"S' H-C-OH
Francisco
Taylor, D.J., Green, N.P.O., ~~Ltt; G.W. and Soper, R. (1997), Biological Science 1 (3 rd edition),
C:;iv ~
~ GIUC08e

---
Cambridge University PreS€,"Cimbridge
Brooker, R.J., WidmaieJ;,.,,.~ Graham, L. and Stiling, P. (2008), Biology, McGraw•Hill, New York
Classification: fl'!,..Q Tlio$C sugars H~x-c sugars
3 different ways based' IC,.H,,O,.t ICsH1aOal (C11H 1:i;O•I
(a) number of carbon oms (size)
(l'anQEi':' 3· to7 carbcimfl0ng) "y H.\;(O ",(o
TABLE OF CONTENTS
o triose (J..carbon)
o pentose (5---carbon) H-rOHI
H-i-OH HH+- H-t"°H
(A)
(B)
(C)
Introduction
Monosaccharides
Disaccharides
o hexose {6-carbon) H-
!
OH H-y-oH
H-y-oH
HO-y-H
S--y-"H :::;:::
H-rOH
:=F::
(D) Polysaccharides ........... . GfYi;l:raldchydc H-C--OH
I
H-0-0H
* This handout is the effort of several Biology teachers at RI. It has and will continue to be RlbcGc !
updated. Glucose Giilll.i:toll'!l
- Any information given in a double-lined box is for your information only.

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(b) location of carbonyl group

(Q aldose (aldehyde sugar) (ii) ketose (ketone sugar) o ct- and \3-forms
H R, When the linear carbon chain of glucose forms a ring, the hydroxyl group (-OH)
I I
attached to carbon number 1 (C1) may be below or above the plane of the ring. Hence
c=o c=o the only difference between the a.- and \3-forms, is the position of hydroxyl group (below
I I and above respectively) about C1.
R R, In a. * glucose, the (.OH) group attached to C1 is below the plane of the ring, whereas
in the J3 * glucose, the {.OH) group attached to C1 is above the plane of the ring.
The three forms of glucose (ct-, !3- isomers and linear forms) are interconvertible in
aqueous solution.
Carbonyl group ·~·--;01' H-loH Carbonyl group ," ",

- •-+- -
at the beginning of the
carbon skeleton is H- -OH
' :-t::;;1
'-1----.!
is nested within the
carbon skeleton, and '1'"" ?
tl-C--OH '"""·~
~
called an aldo group.
Ho-y-H HO-'i'-H is called a keto HO-~H
O,!Y
This is an aldehyde H-y-GH H-C-OH
groi..p.
H-C-OH '°~ "'
sugar or aldose. This is a ketone " o,
H-C-OH

H-y-GH
I •-i& sugar or ketose. 11Gtucose
H-rH
H--WOH
H . (J. Additlona1 Info: ~v
Glue,ose ~ru-. 0 isomerism - same molecular formula, different structure, diffe1 .~erties
In this example, both have the same molecular fo1 ~H120a) but they are structurally
(c) spatial arrangement of atoms (or isomerism) t-rfi:'9..;::j, different The sllght difference in position of the hydr!
to give the two sugars distinctive shapes and
p (-OH) at C4 is significant enough
properties. Glucose is sweeter than
o linear and ring forms ~ galactose. Glucose and oalaciose are isomers i.e rent compounds with the same molecular
- In an aqueous state, the linear forms osaccharides can bend to form a more formula. H..._ ;o ~!
stable ring form. At any one time, m ntoses and hexoses exist in the ring form
(>99%); only a small portion of pentQ.se nd hexoses exist in the linear form. H~;-OH \ ~,?-OH * indicates the
"Web link: See 3D model of glucose at http:IIMliiotopics,co.uk/JmolAppletfglucosejdisplay.htm!
"°,r~ ~"i:oTH carbon position
Additional info: (doesn't mean it won't be tested as Info help you answer questions) H-1,rn' . HO.. !._y-H where there is a
change in
Formation of the 6 carbon glucose ring ( ) K--OH H-1?-0H orientation of the

,,,,• ~· ~rOH
'IV I
H-,y-OH hydroxyl group

,:-··"
if •
H-2c-OH
~I II
•I -ti
H
0 H
- .,,, .. ___
H
Gnlactose
i
1*'
110-7-H, ___._ • ,cf -,=!,
•.-"b-011 ..-- rn,_"' 1 .~ / 'o I
tt...!'~w,=-r OH HO '
·,C
OH

H-~.~
,v
(a) Ullflllr 111\d ringiorma
H Otl " ""
(b)Abb,,,.lalcd ring:~
SmaWin"size;and h 1t9ny-,hyd,roxyJ ·grOupS that can fomi hydrogen bonds with water.
- readHy soluble in er
- transported easily in water in animal-and plant transport systems.
(a) Chemical equilibrium favours formation of rings. The open-chain form of glucose cyclizes when the CS
hydroxyl group (circled) attacks the oxygen atom of the C1 aldehyde group. Only the a-isomer is shewn. 2 I Uriearform poSsesses a fl'e'e C8rbonYf9r0lip·(C=O)'
(b) Abbreviated ring structure. Carbons in the ring are omitted. Thicker edges indicate that you are looking at - gives them reducing ability and hence are called reducing sugars.
the ring edge-on. Components attached to the ring lie above or below plane of th~__ rfQ:
3 I Pentoses and hexoses can exist as-rings..-
- rings are stable building blocks for larger molecules (disaccharides and polysaccharides).

4 I Ring structures exhibit a~- a'nd 13~iSOmeriism

- the same chemical formula gives rise to structurally different molecules.
- increases diversity of monosaccharides which can become building blocks for different
molecules.

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I(C) ''.DJSACCHARIDES Examples_9f cl_isaccharide_synthesis:

Characteristics: Maltose I a-glucose + a-glucose A bond is formed between C1 of an o:-glucose and C4
of the other a-glucose. The bond is thus called an
(a) Disaccharides consist of two monosaccharides joined by a glycosidic bond or linkage.
a{1-4} glycosidic bond.
A glycosidic bond is defined as a covalent bond formed between two monosaccharides by
condensation that involves the loss of one water molecule.
:CH,0H H ~CH,OHH .C",OH
H .CH,OHH
Conversely, the glycosidic bond can be broken by hydrolysis that involves the addition of
one molecule of water. -4 1 - 1 4
+ H20
iO>
0

Removal of a water molecule

to synthesise a glyosidic bond
a--D OH HO
~ Hydrolysis
Addition ofa water
molecule to b~k a bond
-!:,,.,"'-"'
~ H3
HO

aglucose
0~

4lE)
H OH OH

a glucose
HO H OH O

maltose
H OH OH

Condensatio:1
H,O H,o • cP Sucrose a-glucose + ~fructose A bond is formed between 9',~n o:--glucose and C2
of the fructose. The Qo~'¼s" thus called an a.(1~2)

~
glycosidic bond. ~
.t."¾..
~••/o~ (For your info only: 'f!l'-l%J:itlsitlon for fructose is defined as
the ~OH being on tb@~e side of the ring as the C6. The
"--/'o~Qi:-,:S: a~position for f .t&et"is defined as the -OH being on the
o osite side ·n as the C6.
(b) have a general formula oliimi!iiiiiiil'te.g. Cd-~f/J:' ~CHiOH 1CHOH . C
OH CHOH

(c) each monosaccharide unit of a disaccha~ monomer. -4 H

1 ~
2 'H
$ \ . ~ Hf ~2 'H

+ H 2Q
(V HO
~
H 0~
•
i 3
QH ~H
6
C~'HO
Q~"% H OH
O
lo\u)wrro!TU OH H
CHzOH

Disaccharide Monomers ..-\. Jl Remarks

·i11_1,ajt_QSe' l3D ~ r.1/r/J
·1actose ,, ?> nv\ MY
:· 91iiC®ei.,.~l'-.!W~
· gWCo$8"7"!"§i'blactose
sugar important in brewing beer
sugar present in milk
a glucose G> .
r~
~~,ctose ""'"
Sucrose
.

sl.icfoSE! '0'1lftrl\\&tJ6\-1 g_!t:JCIW!f._.,.:"fructose·. > sugar involved in transport in plants Exercise • ...,C,:J 0..,."
1. Describe the hydrolysis o~cosidic bond in a molecule of maltose will produce 2 a-glucose
0 molecules'.... .,,_""'
t§ Cll,OH !~OH
G
~H H
H ~• 0 H
~ H + H20
=Itas•
-----+ +
ffQ::-.ff
:o Oll H :
HO
~
H OH H OH
OH

a glucose
f 'f
a glucose
Maltose

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Tests for reducing and non~reducing sugars:

Additional info: Benedict's tes~: Test for'reducing-sugar {all monosaccharides and most disaccharides'.
What is a reducing sugar?
o A reducing sugar "reduces" certain chemicals - the sugar acts as a 'reducing agent' by being oxidised. Principle I
Ability of reducing sugars to reduce CU 2• to Cu"' ~{S
o ln Benedict's test, Cu2', is reduced to cu+ by a reducing sugar. ➔ reducing ability of a reducing sugar is due toffree gacboo\d gm1 rps)
➔ alkaline solution of copper (II) sulphate (CuS04) [blue] is reduced to

-
o Recall Benedict's Test:
tests for reducing sugar where the presence of a reducing sugar is indicated by a coloured insoluble copper (I} oxide (Cu20) [red ppt]
precipitate (green to brick red with increasing concentration of reducing sugars in a solution). h~t
o What makes a sugar reducing? R - C = 0 + 2CuSO-. + 4NaOH RCOOH + C1.120 + 2H:z0 + 2Na:i$0.
reducing ability of a!dose (only in the chain form) is due to the proton (wH) on carbonyl carbon which
can be oxidised to -OH. Thus, oxidation of aldose gives them the ability to reduce Cu(ll) to Cu(I). '
H
Reducil'l9 sugar
'----y-----"
Benedict's reagent Red pp!
ketose cannot be oxidised directly (which means that they cannot act directly as a reducing sugar). (blue solution)
However, in the presence of a base (present in the Benedict's reagent), ketose is converted to
aldose, which have reducing abilities. C..~ ~ U.~...:, v.0to.- ®1Ut.m'D ~ f t
E.g.: fructose is a ketose, and does not possess a proton at the.carbon I carbon. However in the c~- c,-
presence of the base in Bene I s reagen , ructose isomenses into glucose or mannose {both -+ R,d
eIue
aldoses), which has reducing abilities. A.. --
hence aU monosaccharides will test positive in the Benedict's Test. ~ "&,' Procedure (a) Place 2 cm~ of test solutt011in a test tu~,.,,,
(b) Add equal volume_ofBenedict's re~.
H R, 0 (c) Shakethemixture. ,..<;,...(j
aldose (aldehyde sugar)
I == O..
C
base
+-- C
I == 0--~·G
ose (ketone sugar)
(d) Heat it by immersing the tube ~ m g water bath for 3-4 minutes.
4 .,_ rwl>O"Vl'ff
Ctbil-ltla
I .. I :S Observations and Presence of reducin 1ted by a coloured precipitate.
R f,<,i"¾~ on amount of reducing sugar present;
deductions ➔ colour of precip~
Glucose Fructose Rf,!!g Open clnlln in otherwo1··•- - ;t is--p·~·rtl,8!1¥,lij.U~-qlit,3,_tiv-e~r
1~_,,/<fH,oH', CH.OH ➔ the colour ,itate itself varieS~m:im yellow· to brick red,
eUOH
i;/W=\H Benedict's solution affects overall colour.

~~I
CH,OH 1-2~_
O , . ,H •~ H H\ ~H ~\j\~ ,ro\l'\1\lhS'

~- oy OHH f"' OH H *'1,f

/;", H HO tit-w l'f\"'I,, ""~ _['l~!~asing [reducing sugar] ➔ ➔ ➔
~
OH O C",00 ~ ~ ~ .... ...!:!., OH
0
"'"ii.
~'rel ( ·Green Yell6W ·o_-r~'r:ige ~-.
HOH

0
. ,....
(Q b-oH
\,< <,-------~-=~~-,.-;b-o
OH

,:;._
H (")
"-V
The
Malloso
i
residue at this end (label 'ring')
altemates between the ring form and open
chain form. When in open-chain form, the
carbonyl group, Is exposed for reducing
~ ~ Acid hydrolysis test, lben Ben I! · &test: Test fo(non-reducing sugar {eg: sucro~e"-)_ _ __
Principle .:-.. ucing sugar has to be hydrolysed into its reducing sugar
~ by boiling with dilute hydrochloric acid first or by
action. likewise for lactose. igesting with hydrolytic enzymes.
H-t-OH so•~ HO-t-H
if afhegative-result for_ Ben edicts test ts obtained ·for the test solution,
HO-C-H gifro~nof H-C-OH Procedure
H-r
I OH

H-C---OH
Ci
(
die
d
I
H-C-OH
ut-ltt et,.~ tt-LoH
"O'"'°"011
O I IO~<' " • '
OH
O"OS
then
(a)_ b_oil equal v.olume of a new sample of.test solution with dilute
hydrochloric acid for about 1 minute to hydrolyse disaccharide to
b-OH
H-1
..,.-,.;i•o\-\,
m~)
I
H OH OH
monosaccharides,
Lactose (b) cool contents of tube,
H _ Fructose (c) neutralise acidic content with sodium bicarbonate solution, and
GI~ 'YNOl{~R:EDOCINGJ ?.RED.BCiNG
, '·(sUeTOSe) • (maltose, lactosEI) d) carry o~ Benedict's test for reducing sugar.
Observations and Observation Deduction
deductions A blue solution remains when Benedict's test is first Non-
carried out reducing
Examples of reducing and non-reducing sugars:
(a) Maltose is a reducing sugar because it has a free carbonyl group on one of the glucose After acid hydrolysis, Benedict's test is carried out sugars
again. present.
residues. Lactose is also a reducing sugar.
(b) Sucrose is a non-reducing sugar because it has no free carbonyl group. Both carbonyl Tfirsfime, a green/ yellow/ brown/ brick red ppt fonns
carbon groups of grqcose and fructose are linked together during the fonnation of glycosidic in tM:_l;!_lue solution
bond. Hence it loses its reducing function and 1s a non-reducing sugar.

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(D) i)'•O(¥SACCHARICiESi
Characteristics: Point of Amylose Amylopectin
(a) Polysaccharides are formed by condensation of numerous monosaccharides. Glycosidic Comnarison
bonds are formed between the monosaccharides, e.g. o:(1-4), a(1-6), ~{1-4) etc. The process Monomer/ Made up of o.-glucose monomers Made up of «-glucose monomers
of condensing many similar molecules to form a large molecule is called polymerisation. Each branching forming unbranched polymers. forming branched polymers.
monosaccharide component in the polymer is called a monomer.
Bonding Glucose monomers are linked by Glucose monomers are linked by
(b) The general formula for polysaccharides i - w h e r e n ranges from! 100s !o 1000s./ o.(1-4) glycosidic bonds. o.(1-4) glycosidic bonds within a
branch and o.(1-6) glycosidic bonds
Classification:
at branch points.
Polysaccharides
No. of Each molecule consists typically of Each molecule contains up to 106
units/shape 200 to 20,000 glucose units. glucose monomers. Similar in
Storage Each amyfose molecule is coiled into structure to amylase (helix), except
a helix as each residue is bent in that there ~helical side chains
one direction with respect to the attach~t'b,ranchpoints (-every
Starch 11· Glycogen 11 Cellul previous residue. 20-30 u e units) along each
(a-glucose monomers) (a-glucose monomers) (l3-glucose"1
- :S he~

~~
-Q--0-"~'• $;'~~:"",~-'
Amylopectin
..(). Y'_OHH OIIH
As seen in the flow chart above, carbohydrates can Qlil~sified according to their functions, either
as storage (e.g. starch, glycogen) or structural~'cellulose) polysaccharides.

;tor~·g·e··.P()_!~~~~~~-a!}~:e,S ·_~_~~~~h:·_-;;~•,to-
" "L
Amylose
"N
~ (1),-v c;:itzoH
" :i()H a

~ "" vf-\,
(a)
o starch is stored in plants as gi-anul · hloroplasts and amyloplasts
~~'¾; \;
,J,
II
o enables plants to store surplus gf!J e which is a respiratory substrate oxidised during

0o M"
cellular respiration to yield en~~n the form of ATP (adenosine triphosphate). Maltose II 011
is first released from thi,~Q56hydrate bank by hydrolysis of the g!ycosidic bonds by
enzyme amylase. Gluc~Vthen released by hydrolysis of the dfssacharide maltose by
~,. ~ Amylopectln

enzyme maltase. _ G.;

o starch from plant~de of 20% amylase and about 80% amylopectin. test for starch: f3
""~'Q
.Test for sta·rch e test, 1 lodine in notassium iodide testl
;S, Principle ri,_'-.,--3/ iodine (yellowish-brown) is not very soluble in water, therefore iodine
r".(., reagent is made by dissolving iodine in aqueous potassium iodide.
%J This makes a linear triiodide ion complex which JS soluble.
➔ triiodide ion-fits into centre-of each tum of amylase helix, forming a
starch-iodine complex which gives a blue-black colouration.
11\lodl.e! i""
~•Wltl""M/i''J<

Starch helix
(a)Sta,ch
Procedure Add a few drops of iodine solution to 1 cm 3 of test solution (or a piece of
Starch: the two forms of starch are amylase (unbranched) and amytopectin (branched). White ovals in test specimen).
the micrograph are granules of starch within a chloroplast of a plant cell.
Observations Presence ofstarch is indicated by blue-black coloration.
and deductions

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{b) c~torage pqly:$13:_csh~ricf9$. ~--&f(Y_Cog·en
•· o glycogen is in ariimial storage 'J)O!ys'abcharide.
o structure very similar to that of amylopectin, except that it is even more extensively branched.
o a-glucose monomers are linked by a. (1-4) glycosidic bonds within a branch and a. (1-6)
glycosidic bonds at the branch points. Branchpoints occur about every 12 glucose monomers.
o each glycogen molecule is coiled into a helix as each residue is bent in one direction with
How do:structures of amylose; amylopectin and glycogen determine their function as storage
molecules?
1 All are made up ofmany glucose-residues
➔ large energy store, can be hydrolysed ultimately to numerous monosaccharides when
required. Glucose is the major respiratory substrate to obtain ATP. Enzymes (amylase)
that hydrolyse these bonds are commonly avaflable.
➔ large molecule that is insoluble in water, hence will not affect water potential (1pw) of

.--~..~-..~-~.,.~. . ::ml
respect to the previous residue.
o humans and other vertebrates store glycogen mainly in liver and muscle cells. Hydrolysis of cells
glycogen in these cells gives glucose. Extensive branching gives a lot more ends for enzymes
to work on Le. hydrolyse glycogen to form glucose. 2 All comprises ofhe_tic~

Le.compactmolecule;,H-~~~e,~
➔ intramolecular hydrogen bonding an pro1]'rctlon of hydroxy
f , ,

rF'\r~~OII
. -~H~ :·: . vo ~" groups into the core of the helix formation.
➔ hence, relatively fewer hydroxyl groups are available for
hydrogen bonding with water making it insoluble in water.
Wm not affect \Pw of cells. (note: starch and glycogen ~
"'
· :
lntramolecular
hydrogen
bonding

,.., ~ hydrophilic and can still be hydrated but not dissolved). , ~

ri/i;._

~
9i>OH ~•,<Ht ~
"><V-0.<.,..
'h.~
ff
0 H 3 Amylopectin and glycogen are.branched -
➔ multiple branch ends allow multiple hydrolytic en~ (amylases) to work at the same
• OIi • - time i.e. hydrolyse amylopectin to two glucose ~ (maltose). Maltase further hydrolyses
maltose to glucose, Branching increases ~rgy generation per unit time (NOT per
~
;:,~
OH unit mass) 4

\'¾.
f Q: H<?~_do__t~\3. stfl.!cilJrE:l~ in 5!:_a_rch (amylA":Q~d amylopectin) and glycogen contribute to their
(a)
' (o)
A,,,) ----·.·properties and their function. a s ~ ~ ~olecule?
,_&/~] ~tru_q Prop_erties
Large· molecule made up of., glucose residues Large energy store and insoluble in
water_and will not affect f/1~ otc;~ls
rroxyl groups projecting into Insoluble in water and will not
~
b are involved in affect fllw of cells
intramolecular hyc/,ogen bonding. Hence relatively
fewer hydroxyl groups available for hydrogen bonding
G1}'Co9en:-(a) -E;xtenSiV8-bian·cli"tr19- OrQIYCOgeri.- (bf AriIITiaT 6ei'is.-st6CkpITe·grycog·en-as~Qi'EiriUies-·Witni ii with water:
liver and muscle cells. (The micrograph shows part of a liver cell.) (c) The extensively branched
structure of glycogen.

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 R:lfflGSlnstltution H2 Biology (Students) 201S..2019
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(cf S_trll·~.urar J?.?1_Y5,~(!~~~~~-:; ~e!lu!ose"
·o · cellulose is a ptant structural po!ys8ccharide.
o made u of ~ glucose monomers, linked via ~(1-4) glycosidic bonds
o alternate g ucose monomers are rotated 180° {invt,!rted} (NOT bond angle) with respect
o each other.
o Results in a linear, unbranched molecule with hydroxyl groups projecting out in both
directions.
o cellulose chains which are (parallel/ to each other are held together by intermolecular
hydrogen bonds which form between these hydroxyl groups.
o many of these cross-linked linear cellulose molecules come together to form a microfibril. A
meshwork of such cnss-crossmg m1cr0tlbnls form cellulose cell wall of plant cells.
o The ce!!ulose cell wall
➔ has a!8¥~~4§¥.structure due to gaps betlrveen microfibrils, making it freely permeable to
water 8ncf solutes. It a!lows free movement (DO NOT WRITE 'allows regulation') of
substances i~_ ~rn:f out of ce Is. ('
➔ is aEffi00§"."8r,ic!:,if91Cjstructure as the meshwork distributes the ~s'es in all directions.
It serv~ to enclose plant cells and protect them from physJ~~""age and bursting due to
~ U
osmotic stress.
o How do the structUres in cellulose contribute to its properties and its function as a structural
molecule?
(a) As adjacent fl glucose·:monomers are· rotated 180°with·.respect to each other cellulose
molecules are linear. The hydroxyl groups of each cellulose molecule are free to
hydrogen.bond extensively with hydroxyl groups of adjacent cellulose chains lying parallel
to it forming cable-like units called microfibrils.
➔ Hence microfibrils have high tensile strength.
(b) Microfibrils have relatively 'feviiir hydroxyl groups available for hydrogen bonding with
wat'er as only the surface of microfibril is exposed to water and many of OH groups are
already involved in forming hydrogen bonds with OH groups projecting from parallel
cellulose molecules. (note: cellulose is hydrophilic and can be hydrated but not dissolved}
➔ Hence microfibrils are insoluble in water. P't t:,.(l'm~f,'l:Jo\1A\i@.
~ t't1W1b~~fo. i'U~V\Cf, t:),\VM\Co\l\lij '11\lv)
Hence cellulose is a good structural polysaccharide as it can form micr~l9JlrS with high tensile wortW.
strength and that are insoluble in water. Q

<:~OH OH ~ OH ~
Note: Cellulose is a food source for onl certain bacteria, fungi, i
genes that express the enzyme I ulase r live symbioticall
"~CJ
and mammals that have
hose that have. Cellulases

"◊ ◊0◊ ◊" 1>''(}

0 0 are not commonly available in organisms hence cellu!os pared to starch and glycogen) is
not readily hydrolysed as a respiratory substrate. ~i
OH CH,iOH OH CH:i,OH .;:::::,
o Synthesis of cellulose molecules ....... .
tri-
~v
~(1-4) g!ycosidic bonds between glucose mo~""bf a long, linear cellulose molecule.

o Structural organisation of cellulose c ~ , . .

~-glucose ---+
~o~,f!J
residue
• cellulose
chain
(also called
motecul,
---+-
•~•
;,,~
nl

'-1' ' ..

Cellulose is synthesise~ the enzyme, cellulose s n a . Cellulose synthase forms part of a

larger enzyme ~~ called the enzyme rosette th

~.
s embedded in the cell surface
membrane of plaQPcells. Bundles of cellulose microfibrils are laid down on the exterior of the
cell as the enzyme.rosette-moves.along the.membrane.
/m 'f OH
\ "J'
r\
··*·~·~1e,_
'j»I Oll Q. Why is cellulose synthesised in the cell surface membrane and not inside the cell?
Cellulose is a macromolecule found outside the cell as part of the cell wall and therefore
mt O OH easier to simply deposit it there. Cellulose molecule may be too large to pass through cell
\ ' \ membrane.
"J'

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Additional info:
More information about structural polysaccharides
(a)Chitin
structural polysaccharide used by arthropods (insects, spiders, crustracean etc) to build their
exoskeletons
fungi use chitin instead of cellulose as the building material for their cell walls
similar to cellulose except that the glucose monomer of c~itin has a nitro!len-co~tainin!l appendaQe

CH,.OH
CH,OH' O
"- i)i"-o"'-o
~,<>H Q"'""
o o,
H
~H -~-'
~ • H NHCCH, ~ •
H OH
0" 0
Glucose monomer
,,[
M 1,10;1,-0o~
Structure of chitin
monomer (N-acetyl-D- Glyco¢ia}bonds between
glucosamine) chi~nomers
(b) Hemicellulose
in contrast to cellulose that is ciystamne, strong, and resistant to ~sis, hemicellulose has a random,
amorphous structure with little strength. lt is easily hydrolysed i)tl1e acid or base, and there are many
naturally-occurring hemicellulases (enzymes) for its hyd·· '· ·
residues of hemicellulose include many pentoses (e.g. and xylose), and hexoses (e.g.
mannose, galactose and glucose). ,(¾,,'
(c) Pectin ~. ri:;:,.-..
: acidic structural polysaccharides, found in fru\~vegetables and mainly prepared from 'waste' citrus
peel and apple pomace .(Pomace essenti~l~~s1sts of the pulp of the fruit after oil, water, or other juice
has been pressed out, the peel, seeds a~=).

KEYWORDS (
Some of the key words you should k"""~ 1nclude:

a, ~ glucose
. 0
eJ''
Bonds: c,;(1-4) glycosidic bonsi,..,.~-6) glycosidic bond, 13(1-4) glycosidic bond
Branched chains ,rV
Cellwan qj:'
Compact (J
Condensation
Energy store/reserve
Enzymes
Helical/ helical coil
Hydroxyl groups
Hydrogen bond (with water)
Insoluble
Intermolecular/ interchain
Inverted/ rotated 180°
Large molecules
Long straight/linear chains
Microfibri!s
Parallel chains
Polysaccharides
High tensile strength
Water potential

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 Raffles Institution H2 Biology (Students) 2018--2019
Raffles Institution H2 Biology (Students) 2018-2019
NAME: CT GROUP:
I:@: INTRODUCTION TO LIPIDS
CORE IDEA:
(1) The Cell and Biomolecules of Life Lipids (like carbohydrates) consist of the elements carbon, hydrogen and oxygen.
Lipids, compared to carbohydrates, have a much smaller proportion of oxygen to hydrogen and
Biological molecules carbon.
Lipids are insoluble in water (due to their Ion~ non-polar, hydrophobic hydrocarbon chains) but soluble

LIPIDS in organic solvents such as alcohol or acetone{-e"fW11'1.efl

Lipid~ can b~ classified into
(1) tnglycendes
~ ll'f- efrlcwlo\-<)M.Vc\!r\Ul-1 te.8t
(2) phospholipids
(3) steroids
Content (4) waxes
The structure of npids and their functions in Jiving organisms.

C@: TYPES OF LIPIDS

'"'
Learning Outcomes
'&<::,
Candidates should be able to:
0 a. Tri I cerides
g,Y , , , s,io. tf.\\',\\\l1el ,..,,.Q~ e-9. IN.Nl\110
g) Describe the structure and properties of ~G 1. Structui"e,oftriglycerides JI (~~U,W ~Y
ctClV\ 11\1,!r,WWle,,YiJ
CTi) glycerol and fatty acids On lipids) , " Triglycerides, are not polymers (like complex carbohydrat~ -Elnq "proteins) but large molecules
h) Describe the formation and breakage of the
QQ ester bond.
i) Describe the structures and properties of the fo!lowin ·
# ~

o!ecules and explain how these are

(macromolecules). XV
Triglycerides are formed when 2 types of smaller mo!ecu~~"'i:ogether:

~~

~,v
related to their roles in living organisms: ~ o Glycerol H
(iv) triglyceride ~"
$,.,t'/i H-b-OH • ~
(v) phospholipid
I
H - ~ Fig.1. Structure of a glycerol molecule

~·
Other important !earning outcomes not 5A,~Uy mentioned in syllabus
Carry out test for fats (ethanol em~si~~t)
Hj~H
References C:)e,"~
St.-uctu,e, Alcohol w;~~~ns.\ each bearing a hydroxyl g,oup.
Brooker, R.J., Widmaier, ~f-ll~ham, L. and Stiling, P. (2008), Biology, McGraw-Hill, New York
Campbell, NA and Ree~.B. (2011), Biology (9th edition), Pearson Benjamin-Cummings, San
Francisco _ ()},
Properties~·Glyc
molecule. This
oa
polar molecule due to the uneven distribution of electrons within the
s glycerol to form hydrogen bonds with water molecules and is, thus,
Mader S.S. (2007), Efli:dogy, McGraw-Hill, New York soluble in . lycerol is also described to b e ~ and has a higher densitY than wate~

o Fatty acids

(A) Introduction to lipids Structure: Jong non-polar, hydrophobic hydrocarbon chains (usually 16-18 atoms in length)
(8) Types of lipids with a carboxyl group (~COOH) at one end of the hydrocarbon chain. The carboxyl group is the
a. Triglycerides ...... . functional group that gives the molecule the name fatty acid. Fatty acids may be saturated or
b. Phospholipids.. unsaturated.
c. Steroids ............ . ➔ saturated fatty acids contain only C-C single bonds and C-H bonds (besides the
d. Waxes ......... . carboxyl group).
(C) The Test for Fats..•.. ➔ unsaturated fatty acids contain 1 or more C = C double bonds. The double bonds are
(D) Links formed by removal of hydrogen atoms from the carbon skeleton. The fatty acid molecule
will have a 'kink' in their structure wherever a cis double bond occurs. No kink arises if
the C=C are in trans CC)_nfiguetron.
"' This handout is the effort of several Biology teachers at RI. It has and will continue to be i,.w , ~ ""'i'1v\ee!
updated. "ff3t IY\ 0
<'M\e,tJA\el
- Any information given in a double•lined box is for your information only.
Last updated by: Ms Eva Hor, Mr Ganison, Mrs C. Khoo, Mr WY Ngan, Mrs S. Nair, Mr A Chan
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 Raffles Institution H2 Biology (students) 2018-2019 H2 Biology (Stud<>nts) 2018-2019
Raffles Institution
Saturateo fatty acid eg: stearic acid Unsaturated fatty acid eg: ![noleic acid
2. Fomi'ation ·of a triglyceride molecule
~ ~ ~ ~ ~ ~ ~ ~ ~ ~ ~ ~ ~ ~~· ~ ~ ,,.o ~~~~~~~~~~~~~~~~ ~. 0 • Three fatty acid molecules eachJ°in to one ~lycerol molecule by an ester linkage. An ester
H-c-c-<::-c-c-c-c-c-c-c-c-c-c-c-c-c--c-c H-C-C-C--c--c-c-c-c..c-c-c-c-c-c--c-c-c-C' linkage is formed between a lh droxyl grou (-OH)]and a lcarboxyl group (-COOH)l via a
HHHHHHHHHHHHHHHHH 'oH HHHH H HHHHHHHH 'oH condensation reaction. One water molecule is removed for each fatty acid joined to the glycerol.
Skeleton formula This rt,ulting molecule is called a triglyceride.
Skeleton formula 0 e.(~CQi,tluV!
/\/'\ . . . ,.__ f'J'/1 • Triglyce"rides can be easily hydrolysed into the components fatty acids and glycerol.
~c~o v- ~ -....., '-oH
'oH Kink occurs because of the{cis double bond )in
hydrocarbon tail. Glycerol Non-polar, hydrophobic
MOo<~'ls'W'"11.0,fJ?, H~S backbone hydrocarbon chains
c,;CB!')l1'" ,_ Fig. 2. Saturated and Unsaturated fatty acid molecules
o,,,J..LJJ.• H~-b-c-&-H
"' ,-
~c.tc ~011'1 ~ Her" AAhA h h
'.:j·I_:·~_:-:.--:' ~
El
._Properties: Fatty acids are generally non-polar due the presence of numerous non-polar C~H H
ol)\u\,)e "'
w•~
bonds in the hydrocarbon chains. Thus, triglycerides are insoluble in water as a large part of
"i-o• + n""" r·.
the molecules are non-polar and cannot form hydrogen bonds ~water. Fatty acids are
%- c-o-H therefore hydrophobic in nature. Fatty acids are also weak aci~), the carboxylic acid can
dissociate to a small extent to form W ions in aqueous solut~io~Wever, as the length of the
l l,Ulc,S€/ it ;,/bl non~polar, hydrophobic hydrocarbon chain increases, the s" · of the fatty acids in water 71~
70)1
~
. A AA~ AA-H
~-<--H
n"""
c,,,_oo_ ·.'.. ·9:P ' ' ~ ·
Hy-drolY$1$

.
, · '·--
....: H~
-". .·.···1.'.<r-
-:··~,,~
Jl.;.c-l,~
··'·,\:7~~:s h h
H H
~-'
-H
,.w
i!>!f.-"11,

a«A AA
~~,·--
""""' i'lq~ll>- decreases very rapidly, so that the longer-chain fatty aci~av minimal effect on the pH of anH K '¾
C.lio"'1 u.,w1\) aqueous solution. ~, ..__ 11 1 1 3water
\-1 H,.,&l't- · , i".: -y-c·=-y-y- Glycerol 3 Fatty acids mt>kN:ules

'~,.,,
.
H K
-c -:,:(}E-C.,- H
Foryourlnfoonly:
Both cis and trans fatty acids are ~nsaturated,
i.e., both have double bonds.
~
ri:.,.,""
The Latin prefoces cis and trans describe the orie«&rof the
H
[E1 ~
.-,. t', ~·/.:c'• ) '
3. Pic)p:ert1es,oftriglycerides
Triglycerides are non-polar. In other wor~s,
Fig. 3. Synthesis of #eride molecule

~,fjj
\,._8{e' is no uneven distribution of charge within the
hydrogen atoms with respect to the double bonN molecule. This means that they do not fo rogen bonds with water molecules, i.e. they are
••
theotherside". . uV
cis means "on the same side" and trans me~~across" or "on
~ • hydrophobic, and therefore are insoluble · ter.

~· Jl-ansCOnflguratlon

(O\ct'O~@\ih'
C/s ConTJguratlon

~i\'1£1 81)/(Vl-e, n"zl..£,)

,wiey Si
,erature while oil remains liquid at the same temperature?
i' '11\W;~· -- >\- "'liM!\W ,\\-~W,IO,V Cllteh'\C.--,,,o
A: Most afliiJial fats ( . , butter) contain saturated fatty acids. These fatty acid chains are able
to pack closely to o another enabling the fat to solidify at room temperature.
Conversely, fats from fish and plants are generally unsaturated with double bonds in their fatty
acid chains. This gives rise to kinks in the structure preventing the chains from packing closely
to one another. Hence, they occur as liquids at room temperature, forming oil (e.g. olive oil, cod
liver oil). '--".) p{tJe.& 11.(!\" Vltlve> f¥t'eN16V9' M.tmvvlOle[t{IAv" ~C:tt"'Ji'k'l
Triglycerides can be further classifte~o~s or oils depending on their state at room temperature. Fats
occur as solids at room temperatur~"t) while oil exists as a liquid at the same temperature.
4 •. ,F~ri~:fiO•riS oftriglycerid=0
f ~"t • Major function ..:)Hie rage (38 kJg·1)
o A gram of fat ~ t o re than twice as much energy as a gram of glycogen or starch.
Fats are less ed than carbohydrates and hence yield significantly more energy upon
oxidation. •
They have a higher proportiOn of carbon and hydrogen atoms and lower proportion of
oxygen for an equivalent mass of carbohydrates. Thus, lipids have a higher proportion of C-H
bonds than an equivalent mass of carbohydrates from which energy in the form of ATP can be
released during oxidation. As a result more energy will be released from an equivalent mass of
fats and hence it is said to be a compact energy store.

Animals are mobile and need to carry energy stores with them so there is an advantage to
having a more compact reservoir of fuel - fat. whicfi is stored their adipose cells. Plants are
relatively immobile so the can function with bulky energy storage in the form of starch, a
carbohydrate. Oils are generally found in seeds where compact storage is an asset to the plant.

o The long hydrophobic hydrocarbon chains in triglyceride make it insoluble. Thus, they will not
affect water potential of cell nor will they be easily transported out of a cell. This contributes to
its efficacy as a storage molecule.

La$!: updat!ld by: Ms Eva Hor, Mr Ganison, Mrs C. Khoo, Mr WY Ngan, Mrs S. Narr, Mr A Chan Last updated by: Ms Eva Hor, Mr Ganison, Mrs C. Khoo, MrWf Ngan, Mrs$. Nair, Mr A Chan •
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compam energy sources
b. Pho:3'_pholipicts,
Energy Source Calories per gram
1. Structifre' of phospholipids
Fats 9 Phospholipids are similar to triglycerides but have only two non-polar hydrophobic hydrocarbon
tails (from 2 fatty acids) attached to a glycerol backbone rather than three. The third hydroxyl
Proteins 4 group of the glycerol is joined to a phosphate group (phosphoric acid) which has a negative
electrical cha.me. -
Carbohydrates 4
Additional small molecules (e.g. choline; see below), usually charged or polar, can be finked to the
::J:)rodi.ictiCfri_Of)TI_eta_bC:Hi# water -·, phosphate group to form a variety of phospholipids.
o Oxidation of triglycerides will produce metabolic water. This occurs because the ~ydrogen
atoms will combine with the oxygen supplied during oxidation to form water molecules.] The stn.icture of a phospho!pld
Metabolic water is particularly important for desert animals, such as the kangaroo rat, as the PHOSPHATIDYLCHOLJNE Fig. 4. Structure of a phospholipid.
external water supply is limiting. A phospholipid has a hydrophilic (charged)
j
...r<:' "
fHr.-.,.Y.
r· } """M { head and two hydrophobic (non-polar) tails.
This particu~phospholipid, called a
other functions
o tgfOfe,pt;{Q@lpQfOjgari_S,'-' cushioning organs such as kidneys froO"'echanical damage. Iif'--r1-.... } Phc,sphal!I { phosphatidyl~'btin'e, has an attached
choline g ~ 'fhe kink in one of its tail is
o /Thermai-:insulation,-'by subcutaneous fat (the layer of fat..._@ath the skin). This layer is
especially thick in seals and other marine mammals, pro~~~'1fiem from cold weather.
o ?Jm'Pi-ai,iif'J,:l.l!)ycin_cy lipids are less dense than wat~elps improve buoyancy in marine .. ,..,..
. •0*•0
due t o ~ ouble bond.

(~)~ctural formula follows a common

."
-R
~ ?',
mammals like the whale. ~ ical convention of omitting carbons
o Lipids can function as a reseivoir for storage of fat ~ e vitamins like vitamins A, D and K. attached hydrogens of hydrocarbon
'.i~
.Q~
~
P':, ~~ s. (b) Space-filling mode!. (c) Simplified
'.2';". ~ ~ I iv symbol for a phospholipid with a head and
Foryourlnfoonly: ~/;; !~ ~~Cl/, two tails.
To release energy from starch and glycogen~en ~....Q};rst break them down to glucose. Glucose is then :,,,".'\,

metabolised via a series of respiratory reactions ~a;;~is, link reaction) to form 1#icefyl-coA. \ •·
::C';",

~
'."•
Cl/,
., Cl/,
"!',

To release energy from fat, enzymes fir§t_~ r k down triglycerides into fatty acids and glycerol. Fatty ~ 't.
acids are metabolised to multiple un~~~.etyJ--coA by the beta-oxidation pathway. In this pathway, two
carbons from the end of the fatty aci~ain are repeatedly clipped off and combined with coenzyme A to
formlacetyl coA.\The tonger the fa!!01ti carbon chain, the greater the amount of energy that it yields
e;
':j
Energy from acetyl-coA is th~eased via Krebs cycle and oxidative phosphorylation (OP) -to yield
energy in the form of ATP~ Q 2. Fonn81:ion- of a phospholi& Im,iiiiliilGt"'I
~ ,L,
H ci i.· .· ....•, ·.· ('..fJi,
H
- I
1"'°~ -· a~....
. . . . .~v•. Condensation
.H~C: ·-·•·
H~t~'0'VV"'v'.
Triglycerides f------~·Fattyaelds 2 """'"
intermediate H-C-~~...,..
r ..·-··o;:;····..r
. ···. ···~ H-c-~~,..~.y",..
L-~cetyl CtlA~Krebs~OP
I .
~
I • ,,
t I
-
Cycle
I €} .~y:
Glucose Glucose ~Pyru:vate Pyruvate - - H-C HO-P-OfE_, r,,10"-\
D :
H,O H
The breakdown of triglycen·des_ and glu~ to yield energy in a cell G!~rol~: Ph:phori~
~
Phosphollpid
with two acid
fatty acids •..1 L___
111"" ""'"'1'
'U'1>"' jj\jc,,,<\

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•
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3"' PiriPE!rtieS,of phospholipids / COwll-1-IJ'\" 'f0v'lvl 1-t-bonol& Wf-Jln. th.A)

• Phospho!iplds are said to be amphipathic 8s they have(both hydrophilic (negatively-charged
c. Steroid$
phosphate head} and hydrophobic regions (non-polar hydrophobic hydrocarbon tails}. For your info only:
o The hydrophobic (water-hating) hydrocarbon tails are excluded from water.
The hydrophilic (water-loving) phosphate head (and its attachments), being charged, have an 1. Structure of steroids
affinity for water. They can interact with water molecules. IW\Slll p}l)ittol ¥J hlb'\teV· Structurally steroids have little in common with other lipids.
o When phospholipids are in water, they self..assemb!e::?nto aggregates such as phospholipid Steroids are characterised by a carbon skeleton consisting of four interconnected rings.
has a hydrophobic core that is shielded from water. Cholesterol, vitamin D, testosterone. progesterone and bile acids are examples of steroids.

•~i!<f'lro
h'f'(\®11 ~ Fig. 7. Examples of steroids

4. ;"FU_ncti_ons of phospholipids 2. PrOpertieS'ofsteroids e.g. cholesterol ~'

Major component of membranes of cells and organ
o The hydrophilic heads face out.vards and i
interior or exterior whilst the hydrophobic
phospholipid bilayer.
Hence they act as a boundary betweeo
the aqueous environment of the cell
Is, away from the water, giving rise to a
·acellutar & extracellular aqueous environment
• Steroids are insoluble in water and soluble in organic s o ~
• Cholesterol has a characteristic four fused ring I
re and is largely hydrophobic.\ Like
phospholipids, it is slightly amphipathic, havin~ drophilic hydroxyl (OH·) group and a
hydrophobic ring structure.
3

} "°'"
and allow compartmentalisation within a'c •
(Note: Compartmentalisation allows e fonnation of unique environments in a cell where head
groups
there is s tial separation of bio I recesses e.g. within specialized vesicles, such as
lysosomes, m t e certain cells, is an accumulation of high concentrations of the hydrolvtic Cholesterol
enzxme. ,,;, OOJ.ttnJls ~ilfttt'*Wf1; ~o.110V$ SG'l'le:~i~~ qC,C,\Af11u\ecte,to stiffened
11 } region
The phospholi id bila er a hydrophobic core region ~ t 1.Jlortif}iernfeable to· small
hydrop o 1c solutes an a very low permeability to polar and charged molecules/ions.
Mo,e
Therefore, the nature hospholipid bilayer allows it to act as a barrier to certain molecules ,,!j
fluid
and is thus partiall eable. ;, t l ' l ~ ~ f d "'r } region
o Phospholipids t locked in place but can move laterally in the menfbrane. f'Rus
membranes a id and allow the movement of incorporated proteins within the bilayer. ~O(:'reci. ·
(b) Cholesterol in the phospholipid layer

~
o Hence, ph lipids are a major component of the cell membrane, and they can fonn a
i\l'i'll1);11""' phospholipi Hayer in an aqueous environment Major component of liposomes, which are
The· hydr6xy1 grollp ·of chOlesteirol aliQnS with phosj:)hate h'eads of phbspholipids while the remaining
*¥n~ll-' vesicles surrounded by a phospholipid bilayer.
portion of it is tucked into the hydrophobic core of membrane. The{!lydroxyl group of cholesterol
"f)cis o Liposomes are artificial lipid spheres with an aqueous core that can be used to carry therapeutic
interacts with the phosphate heads of phospholipids by hydrogen bonding)vhereas thE(hydrophobic
DNA into a target cell. The phospholipid bilayer of the target cell and the liposome can fuse and
ring structure interacts with the hydrocarbon tails of the phospholipids via Van der Waals forces.)The
hence allow the therapeutic DNA into the target cell during gene therapy.
fused-ring structure of cholesterol is rigid, and so the presence of cholesterol gives mechanical

(-
stability to the fluid lipid layer.

3. ' Flihcticin' of steroids e.g. cholesterol

Fig. 6. Liposome made up of a phospholipid Cholesterol regulates membrane fluidity i.e. it stabilises membrane.
bilayer and an aqueous core The membrane is prevented from being g_yedy f111id at higher temperatures as cholesterol restricts
phospholipid movement through its interactions with the phospholipids.
The membrane is prevented from being overly firm at lower temperatures as cholesterol prevents
PhO'"Phollpld
____molo~ulo close packing of phospholipids and hence prevents its solidification/ crystallisation.
Therefore, cholesterol helps prevent extremes, whether too fluid, or too firm, in the consistency of
cell membrane.

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For your Info only: Try this using your smart devices
Other functions of steroids (Download the Zappar app from Google Play or App store to view)·
o As a precursor of other steroids, including bile acids, sex hormones and vitamin D.
e.g. Steroid hormones like aldosterone and testosterone. These are produced by endocrine
glands. Testosterone is produced by the testes and responsible for the development and
maintenance of secondary sexual characteristics of a ma!e. Aldosterone is produced by _the
adrenal cortex and it regulates sodium and potassium metabolism.

d.Waxes
1;.\$tfuctU:re'of waxes
Waxes are similar to fats and oils but their long-chained fatty acids are linked to long chained
alcohols. However the alcohols in waxes have only one hydroxyl group compared to three in
glycerol.

2.~:P'fOj:>'e,rti_es:_ofwaxes \Afire.ct~
waxes are chemically !!lfiltand msolub!e m water. ~~

3:- Functioo of waxes ~Q

■ In plants, a waxy coating known as the cuticle covers the epide leaves and stems to prevent
excessive Joss of water. • '-,,,
■ Insects have a waxy cuticle to help cut down water tos:g.V
In humans, sebaceous glands m our skin release seb the epidenms Sebum rs a mixture of
waxes and triglycerides. It helps to keep the epiderm~
which would otherwise grow on skin (J
le and inhibits some species of bactena
r:,_ •o·
:
·.··GET ZAPPAR
• ZA!' THE CODE

I (C) THE FAT TEST (ethanol emulsion tesi\"--

. r»' : . . a · . . Clilllil llliliW
(https://yout~dDNJNwsilc)
The principle Q~..,. ·
Lipids dissolve in organic solvents sue@ ethanol, but not in water. An white emulsion is seen when
lipid is shaken vigorously with wat~.,
I (D) LINKS ,.p
~:--'
The method · C:}0 The topic of lipids is relevant to the fol!£l~topics in the A level Biology syllabus,

3
• A~d 2 cm of ethanol t<} e
If the test sample is a solution: ""'\::
"'cfrops of test sample in a test tube. Mix well and allow it to stand for 2
Topic ',;.,, Comments

■
minutes.
Decant the ethanol
;~
C)..._ ..
other test tube containing 2 cm 3 of water.
1. Organelles and
Cellular structure
Membranes)
(Cc~ ~ membranes consist of a phospholipid bilayer.
olesterol regulates the fluidity of the cell membrane.

If the test sample is a soHd: HIV has a phospholipid envelope which fuses with the host cell phospholipid
3 Genetics and
Add 2 cm 3 of ethanol to grounded test sample in a test tube. Inheritance (Viruses) membrane to allow the nucleo·capsid (viral genome+protein coat) to enter
Mix wen to dissolve any lipids if it is present and allow it to stand for 2 minutes. the host cell.
Decant the ethanol into another test tube containing 2 cm 3 of water.

REtSUlts and conclusions

Observation Conclusion
A clear solution was fomied with ethanol;
The solution remained clear when water was added. Lipids absent.

A clear solution was formed with ethanol;

A white emulsion was formed when water was added. Lipids present.

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KEYWORDS

Some of the key words you should know include:

Non-polar
Polar
Charged
Hydrophobic
Hydrophillic
Hydrocarbon tails
Amphipathic
Hydrogen bond {with water)
Carboxyl group
Glycerol
Fatty Acids
Ester link.:ge
Bilayer
Barrier
Regulate membrane fluidity
Cell--cell recognition
Energy
Oxidation
Water Potential

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 ------~~·---~"-~"~-------

-----------·-· ----------~- ----

Raffles Institution H2 B!o!ogy (Students) 2018-2019
Raffles Institution H2 Biology (Students) 201e-2019

CORE IDEA A. INTRODUCTION !l"te.1>.t .,.,_,_/ l?j~~es-si,,H\c <"',

(1) The Cell and Biomolecules of Life While there are relatively few carbohydrates, the number of proteins is almost limitless. They
are specific to each species and vary from one species to another. Indeed, it is the proteins
Biological Molecules rather than the fats or carbohydrates which determine the characteristic of a species.

PROTEINS B. COMPONENTS
■
■
DIWC~s
Proteins consist of the elements carbon, hydrogen, oxygen, nitrogen and sometimes sulfur. ( 0t10N&)
The basic structural units or monomers of proteins are called ammo acids.

Content C. AMINO ACIDS ;, i:<llm>t\ ~w,,,, a,e, "'"'' crot

The structure proteins and their roles in living organisms. There are\, 20 amino acid§ that are used in the biosynthesis of proteins in cells.
An amino ae1d consists of an a.-carbon atom that is covalently bonded to 4 groups (Figure
Learning Outcomes 1):
(a) Describe the structure and properties of the following monomers : 0) a hydrogen atom
(iii) amino acids in proteins (chemical formulae of specific R groups of different amino acids are (ii) an amino group (wNH::i)
not required) (iii) a carboxyl group (wCOOH) and
(b) Describe the formation and breakage of the following bonds: '$,,,~ (iv) a variable R group, also called a side chin-
(iii) peptide bond Q
(a) Explain primary structure, secondary structure, tertiary s~c.lnd quaternary structure of HI
proteins, and describe the types of bonds that hold the
disulfide bonds and hydrophobic interactions). ~
ule in shape (hydrogen, ionic,
~ (ii'
(b) Explain the effects of temperature and pH on protein ~ r e . ©"Amino.
G('oup .
(c) Describe the molecular structure of the following pr~s and explain how the structure of each
protein relates to the function it plays: ~
(i) haemoglobin (transport)
(ii) collagen (structural)
~
i~ ofan amino acid
"" ' 'l""""'· 2,M .J'4 l<,.JIM)IA~
~.~,p)➔ """' ,,. "I"
Every am·1no acid (except praline) has ~sit one amino group (-NH2) and one carboxyl
other important learning outcomes not s ~ mentioned in syllabus group (-COOH .
• Conduct biochemical tests to identify nee of peptide bonds using biuret solution. Each rou that vary in charge, hydrogen-
.,,_, . ban I
o A
gure ).
of the R group. Hence the physical

References
Campbell, N.A. and Reece, .ha)
;a""'
011), Biology (9th edition), Pearson Benjamin~Cummings, San
and chemical properties
and the polypeptide~<'.:,
o All proteins in all s
R group determine the uniqueness of each amino acid

· , from bacteria to human, are constructed from the same set of

Francisco &Q 20 amino acids. ~
Brooker, R.J., Widmaier~-., Graham, L. and Stiling, P. (2008), Biology, McGraw~Hill, New York
(;f/j

Table of Contents
A. Introduction 2
B. Components of proteins 2
C. Amino acids 2
D. Polypeptides 6
E. Levels of organisation 8
F. Classification of proteins 12
G. Properties of proteins 15

*This handout is the effort of several Biology teachers at RI. It has and will continue to be
updated.
.,.Any information given in a double-lined box is for your infonnation only.

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1'.,-:N~n-~le(sl_de ,chal_ris; bydi'ophoblc

(a) Classification of amino acids
Side chain ~~~· 1. Classification according to human nutrition:
. ~cii~
(Rgroup)'--· (i) -Essefltiaf amino acids
I_H_, .fl : '::'i, These amino acids cannot be synthesised from simple substances by humans and must

111111 ,. tlr~~~~;I be obtained from their diet.

~·
(ii) Non-essentiafamino acids
Glycine Valine Leu, These amino acids can be synthesised from simpler substances by humans.
(GtyorG) (Ala or A} (Val orV)

!t:
53Jloo,L) (Q ·"Nriutrtil amino acids
""'
2. Classification according to properties of R group I side chain: (VIO ri({'Miilfffur V'fftU)
i"' ~ '-\of fayh,. \-1'4:iOrd( wit½ w!llt'e!('
\,\f,Jftt \ ~rvo These amino acids have non-polar R groups are hydrophobic, or polar R groups
:. CHi_ ~ 'k ) ~which are hydrophilic. They are electrically neutral as the sum of positiv~ and negative
!il,~.· v'k,u'f-1.t\\ ~~ charges are equal. l:,.fuwv1 "1-\:otlu1& ltfitt-1
i!~ll ~--(t1cill¥ti/41 CA (ii)' Efectric:ally-charged·amino acids ===~== WO\tw ~foy Ow
~\Methionine
-- • • Acidic amino acids have R groups that are(oegat1vely-crgirged! due to the presence 1]1171.trrr)
Tryptophan
{Met O:f_M}_ !!_rp orW) of a carboxyl group, which usually dissociates to form CO - at c.ellularr9;H.
Basic amino acids have R groups that are generallyfpositi~-'6ha eaJdue to the
"fiOiii'Sri:1tt"chalns;'t1ydl'ophmc;: _,'] Vt~ci~ presence of an amino group, which accepts W to form NH2 {)
'("'1Vtit1'cl-i<J 1 ~ o Note that an amino acids have carboxyl and amin0 ~ s ; the terms acidic and
~~vii'/ basic in this context refer only to the R groups/ si~ains.
As they are charged, acidic and basic amino acid~~1'.""1'1Ydrophilic.

;Vldt~'l\\l() ·on: What's the difference between hydrophilic/hydrophobi_"

k',Y"AfS Threonine Hydrophilic = WIVIWJ:•• Aftrntm ~ w"l1JV qj
A"<,
'.vmW>t.l-'
{Thror_]_ Hydrophobic= ½vmi,t"' <'lil<\\iJ'i ~-~ ~•tvr····c~' k
~.::h r tj:~!~~ 1•AeS.1fM!
<'fSi~ca11y::~liar9iiifSid8-ch8ii$i 'iiydrop11m~
},101.vt\'lvl
J;;'s,--;;'--==7
f'~t O" I Electrically-charged amino acids I
~\"1'1.l
c",¼OJ'C'ilr>) . ~·
(7,
G . _,,,.,.. ............
L, 81) tt:vO Acidic amino acids Basic amino acids
WM 1%' Neutral aminoa~
Charged at Charged at
'"' °"""
W\V
M.EM-tbrqne,i
Uncharged@,,,..,
physiol~pH
beca~ ey have 1
physlological pH
because they have
physiological pH
because they have
more carboxyl than more amino than
Lysine Arginine Histidine amin oup and 1 carboxyl groups (R
amino gro.ups (R group
(Lys or K) _ (Arg or R) (His or H) carboxyl group group contains ~NH2)
contains -COOH)
0201,_,..,,.E<locn!lolt,lne. Lv-ti· Ntt,. w\1.l!;yl t1lflevt6
( e•l',J· ~i\\ """" .~~ Ht i<l mm ,%~)
Figure 2. The 20 common amino acids classified according to R groups. . ./" -........... ! l
l»"t1> e,,,n< +i-) Non~polar R group; Polar R group; Negatively-charged Positively--charged
hydrophobic hydrophilic R group; hydrophilic R group; hydrophilic
R group does not form R group forms R group forms R group fonns
hydrogen bonds with hydrogen bonds with interactions with interactions with
water water water water
Figure 3. Amino acids classified according to R groups.
(Since all amino acids have a carboxy! and an amino group, acidic and basic characteristics here refer to the side
chains. Physiologlcal pH is the pH within a cell (pH 7.2).)

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(b) Properties of amino acids

1. Exist aS•A"fi~tiQJ~S/{ lil.U D. POLYPEPTIDES
Amiflo adds are generally soluble in water and become ionized {Figure 4). Amino acids are the monomers that form polypeptides.
In solution, ·the un-iomsed-amino group (-NH2) receives an-H"" ·and becomes-positively- • Amino acids can be joined to form: dipeptide (2 amino acid residues)
charged (-NH 3 ~). The carboxyr group (-COOH) dissociates, releasing an Wand becomes tripeptide (3 amino acid residues)
negatively-charged (-COO·). o/igopeptide (i:::a 3-10 amino acid residues)
Ionised amino acids in solution thus cai,y both positive and negative charges and are pofYpeptide {>10 to a thousand or more)
called dipolar ions or zwitterions (+HsNRCHCOO·). In this dipolar form, an amino group Amino acids are joined via condensation that links the carboxyl group (-COOH) of one
is protonated (-NH3"') and the carboxy! group is deprotonated (COO-). amino acid to the amino group (-NH2) of another (Figure 6), with the removal of one water
0 0 molecule. ,
I! + II ttt-c(fiMt-1~ This fonns a peptide bone( covalently joining the 2 amino acids and each monomer is then
H;N-CH-C-OH ~H3N-CH-c-o- I)\ WPlttM known as a residue. / ~'it!At h'1\:.Ct,~ •
j
R
OI.Clf/Pt Ht ! ( ~ li~bu),~ "'1iin. WVl:-t-er-"\
i'llWV!i'VVR ..J
uncharged structure dipo!nr iOTI. or zwittcrion R R'
(minor <:oinponeoti (major component) I I
Figure 4. In solution, amlno acids mainly exist as zwitterions. H-N-c-c-BIIII--N-C-C-OH
I I Q + I I 11
2. Act as,'.lii.iffefS
■
~ HHO HHO ~'V'
When amino acids are dissolved in water, the amino and ~ ! groups act as bases is.HO
2 ~
and acids respectively (Figure 5). Therefore, aminQ Se\i"r·are considered to be hydrolysis +H20t { condensat!o!('¼J
\:io!trl.ttre.{-w ~ NV
~7 "Mi'I I ~
amphoteric i.e. able to act asan acid or as a base.
R'
~~ ■ Being amphoteric enables amino acids to act as bl.!ffe,_1'$ in solutions. Amino acids in a - • WI' I

□6
solution can donate or accept W, allowing them k~
as a buffer to minimise changes
c-•-Jc~c;;....&i!
Such property is essential in biological syst
adversely affect the performance of protei
f@)t
in pH of their surrounding when a small am~un 'acid or alkali is added to it.
here any sudden change in pH could
enzymes.
H
I
II j ~- f'Y I
,t To !:"t mt """""f1-t ;f::-, .
•C\.flj,R O . °"'o1'1 f<;,--<W1"'1M""' Figure 6. Fonnation of a peptide bond between 2 am!,"~c\,_dsVia'condensation. The converse 1s hydrolysis which
Nt....J-c.v- neutralzwitterionform !',) Gt)~& fl) i1,{"10'f01. breaks ~~epude bond •
~ . l 'o-
VQ H Further addition of amino acids {;)~ In the formation of a nnear polymer called a
polypeptide (Figure 7). ¾."- ;
'°'"'°" maJ;J;t';-}/ ""~'""'mmsd•'™'' P.~~
c§!
~ 1/ H+ added
.
OH""added
o The regularly repeating_ main chain, is referred to as the backbone
o Variable part comprise~istinctive R groups
~
,£:
OK

(')fo
G~•: -c-c
H R 0 i.,
,,O
I
- .--ml.... ,
-~-~"11141
1 '-oH" 'I'! '"'fl' ,,,,,mt:
'-N-6-c,V"
H/( I
Wl'!WlO '!J'ff
'-er ""'- H- """'i"'V
,0
·~
I HJC,.,-ett.
Ctt
y(?I,
H t H t ~"1te,j <mo '1)iq1joV,.
When acid (H+) is added to the solution, COO- When alkali (OH·) is added to the solution, NH3"
ofzwitterion accepts a H+ and becomes of zwitterion !Q§§..a..H+ and becomes NH:~.
COOH. The H+ neutralises the OH· and prevents a
o/';,
i
_cr::,.P.",
H+ is removed from the solution and there is no
change in pH ofthe solution.
change in pH ofthe solution.
The amino acid becomes·negatively-charged.
(a) "-• _,
~SJ (11,1.1,'o\ ,~.
,,e, {
4°t--ry'/~I .,,•~
n 1?

The amino acid becomes positively-c_ba_rged. /,mi',>(' ~ ,.j(J

Flgure siAmino acids are amphoterlc. ,~ ~ef,-"''~
~~~.,,- ~ w"
"- ..._,.,,,_.
/¢
Side dlalna
OH
¢~
H,C ct¼ ;
\;,/i \
I J

CH:/
~~
\A<"
't',''

~
TH
~
#~·~""'
rtr,11~·:!;1 r,yti::•fi'f fC'-l'
,_r -'\\ t 611,l'O
" ',-,r1u;,,cr
"'·1· "
--l
"aptlda Carbo:tyl em!
'""""""'
(N-tolmJnw,) M\'l<l<clv,.> bond (c-tl<mlnugJ

Figure 7. Formation of a polypeptide.

AA~"' I

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A polypeptide chain has direction, i.e. 2 different ends. &<efi\,Q</10• ol- ~~-
o Amino-terminus (N-terminus) with a free amino group at the start of the polypeptide E. LEVELS OF ORGANISATION U\oillv~ f>\M~\Qq~€11W>t'jp<,f-~~.--,, t'{i,-e;:i(
chain. There are,4 _l~yels .of organisation in tbe structure of proteins: \WlttM tf- o¼~Vt\ ('(lten'1CifGYIS-, ~ tf- _
o Carboxyl-terminus (C-terminus) with a free carboxyl group at the end of the polypeptide (a} Primary structure (IIYtfPII" l!-1'1'\®rel) ~\o\Mfl ➔ V9!±WYrM'\fW1 y1.rni'qi,1V b\1vUZ:ief€M.ffi:$'
chain. • Primary structure refers to number and sequence of amino acids in a single i:tf\'ITIQAl'l
e.g. in the tripeptide lysine-cysteine-arginine: ,&to polypeptide chain.
* lysine is at the N-terminus. W The primary structure is maintained by oP~ttrlPJ fo®di~ between successive amino
"' arginine is at the C-terminus. acid residues. lll '!'I' ,,t ""''""
M t'e,\>\tij~ bo,wsl
Each polypeptide chain is unique in its se uence, number and type of amino acids.
A polypeptide folds into a specific three-dimensional conformation/shape. li o It is this sequence of amino acids (and their groups o I po ypeptide chains
~
o 'Confonnation' refers to the three-dimensional arrannement of atoms of a protein
molecule. that determines the type and location of chemical interactions, and hence the
When proteins fold into specific conformation, there are complementary surfaces and clefts pattern of folding.
that can fit only with specific molecules. On these surfaces and clefts, different R groups o The pattern of folding determines f&:IQ:f!MMO)j'f0/1 and unique characteristic of
enable proteins to form bonds with other molecules - controlling precisely the orientation, a particular protein.
strength and duration of these interactions. e.g. enzyme-substrate interaction, ligand- Primary structure of a protein is specified by nucleotide sequences in genes (Refer to:
receptor interaction. Core Idea 2 Genetics and Inheritance). L,. ~ ~IA½1~-
Thus, a protein interacts only with specific molecules.
l··························-·······································-··•·-···········-·(.rJ ····••·•·········••·········•··•·······
On: How many different polypeptides, each consisting of r amino acids-li'.~ be made if the !
· · · · · · · -· · · -· . .
Hence, a protein's function is determined by its conformation~h is dictated by its
nr -O"''
1:-fl~• .,.;:0'ntl . . . . . ..
amino a~jd sequenc~. .. Q
'-? e-"c). HIV rro,&21;Se : number of different amino acids available is n? i
~G
, ~eM:··· b~~
G '
~.,. Tn~"((e,- ~e,-~)•'°" ~11-lel i:; NUf ii'\~~~
018 l""h'I'<.- ~ljcMe, ~ (._ ~lqfVi'\ldl'I ~~- 19
(<l<l"!MeiJ,~I
-<O H\Vell l<l<,1"~ to
l-) '-"'i- Hi~dV\19
m<>k
~~ 6Wl.(t1\lJrt,: : ; ~ I;,; c:;;;;.;:.K:.& JAiriJWi. ,;;,., r,:w,.;., b ?~

19
Q. l\M~ ~~t~ ,r[>¼1t!Y" l"Myt? IMli\o NJct!,.S NGio-i::::,- ,a
w 'f7--/ ., 17

lwmj~o -30 /
;,r Rael<! iYl - p ls<1".¥<i<l!;:)
· <Ntto\ce) ;--c/41&
A.~
.-Ci,~
;-ovw\!- ~ l<ne.r ?<>ll)ie-ptit:/0'
8 - -:'\~-- -
9ft &,'11 12 13
14 15
16

w Figure &ary structure of a protein.

~
Wvlf,m,t~~ ~00 %o\ Wf> i""- W<M 3D .\¼pc, c,m-Or1
._. hlow P. ~ "" ~ n,,~iW
-Ji (bfSeCOnda strUcture -:c_~\ro\veb \i~ WW
l1;>- • • ~ -r, 1"'Vl~o\!.C/A\aj /J\ Secondary structure (usua!l ers to regular coiling or pleating of a single polypeptide
1\-i,vo;w,, f!Aact\'Wl c i ~ OY]
""1Cls
ov'::i \'Y<)t,.,1/1
11\\WI(;! Wifu \t,--,ie,:rl[c "'1fo,-w\~1i<1Yl
chain.
It is (usually ai~i
NQTl\ @)
hydrogen bonds formed between CO and NH groups of the

,§, J polypeptide ackb

V ~1Y\e& i,n\~ltt\l
~"Nl\y) of-w,M"
;. ~1111>1 """"""'"'
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An exception is
groups are not involved in formation of the hydrogen bonds.)
en - although it has a secondary structure (and a quaternary
structure), its hy~en bonds are not conventionally formed between CO and NH groups.
Examples.of secondacy structures are:
~ 1. '<X:~~li~ (Figure 9)
o Made Up of a single polypeptide chain which is wound into a coiled/spiral structure.
'""°'"'1 o Tums of the helix are linked together by
\)fil:C1l f;!Wf ofonetumand I-IGf:NBrtf·
h~~
.ofthenextturn.
between \modi§
111
These hydrogen bonds form between groups at every 4 peptide bond 0.e. amino
acid 1 would be bonded to amino acid 5, number 2 to 6, and so on).
Hydrogen bond is formed between O of the CO group of one amino acid, and H of the
NH group\four ammo acids away(in a single polypeptide chain.
o All main chain CO and NH groups are involved in hydrogen bond formation, which
confers considerable stability.
o There are 3.6 amino acid residues in every tum of the a.-helix.
o e.g. of a protein whose only structural motif is a.-helix is keratin (structural protein of hair,
wool and nails).
li) i>lltv,- R 'il't>
(;i.)
7
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~1}1
H H H 0 H "!'lft'/'• @._,,.,.____,.
.,,·
H H 0 H
N-C_;-C N-c-c N-c-c N-c-c N-c-c
' R,'
H
r" I J°' IT I°° II (clustering of hydropl>cblc
groups away from wator)
R, H R 0 3 Rs 0 end van <fer Waale
CH lntoni.dlons

"-.,.,,,_':,
Ci) bi --Polypeptide
Hydn,,gon l;I ,,,gl backbone

0 "". o/- 11m,1J \ bond ''\

~
·1i,..
~
Alpha-carbon atom
e f
y-oH CH~-
e
Carbon atom
)i ~
-CH,i

t9,J ;,,~~'\
--------]- 1.s il Nitrogen atom CI Ii:! ~llllid<> bridge
J,),,.
_ 100., rotation
3.·G t'tOl nst'l;l.l(.e.5
e
0
o,..yi;ien atom
Hydrogen atom
] ,_ ~,1-~
, , , , ,, , ,
. '01

Po
IYtlJ/&<, -
11-Mix
of.- @lo Amino sicid side chain
Hydrogen bond )3 ~'l.--
~
i;\...-~,.
-~
~~--·1Ji!. .··:-\\_:-
: ~- -~,(~
\.Ai, 1_;.;, .Jil. ,,,lii.
'-~-CH~-Cfi:i-Cti,i~,~l-ett~-
® lo~k: bond

~ ~ " .::¥;,_ ~ - - ~ ' ~ ... -~ " .

Figure 9.,ix-helix. /
~ ""·"" p..-... ... _ ' ·,,~' .:
. ·•······· ········· ··• a"'¾~ Figure 12. Combination of secondary strucb.Jres in a Figure 13. 4 types ofmmolecular interactions in a
2 .. -13~ple~.t~~-s-~~t(Ftgures 10-11) _('"}-' tertfary level protein. tertiary level proteezu "
o 'Fonh.·ed Wheri two or more regions/segment of a sin9la:r,1ypeptide chain lying side
by side are linked together by hydrogen bonds. ~' ~ P¥!\,l¾ types of interactions help to stabilise conformation of a prot~~
o ~01:!t:R'Nl bt1Ylf1 is formed between Clo :'le~~.,. of one region/segment ~ 1. Hydrogen bond•. '<,S.
and N)j /lm)l/f, of an a · ent of a single polypeptide chain. 'N~~~\--1-1~ !<:IA!\ o / Oxygen (e.g. 0 of C=O group) and nitrogen (e.g. h-.ot.-NH
o Chains may run parallel (same direction) or a
flat sheet which becomes folded.
o e.g. of a protein that has 13-pleated she
rffe
rallel {opposite directions), forming a

cture is fibroin (found in silk produced by

1\{IAA'lK1\-cow'rro11~, .f group) are electronegative (~H- Hydrogen of -
~v,,1t1_e--eoi.~, group is electropositive (6+). The e!ectc.:f
r -OH
tive and

--~
a.Mtr,t>- Vl~c\\'t11!1 electronegative atoms form hydrogen bo
silkworms and spiders), ~"\.; /•:- ··:···. (.~•fl: l.i'rtcff~) _ o Formed between R groups of __ \.~ amino

~ ~
acids at tertiary structure (or betwee and -NH groups
of peptide bonds in the case of sec~ structure).
··-.. vQ o Individually the hydrogen bond(!, •eak, but collectively

~-
,.,_ strong. ~9
2. Ionic bond J$.
o Fonned b"etween o~Yely-charged R groups of
amino acids. ~- aspartlcacid
• COO- and wF.IJ
are found on R groups of {addle amino. acid)

,..,_,,o 1ce,,1
f
otLtll)\~ and b-&'J.W., amino
acids res ely. '0"·
• They are also found at the ends of a polypeptide )
ionic bond ✓H
":,I H
chain.
Figure 10. !3-pteated sheet- 4 regions of a single Figure 11{a). Hydrogen Figure 11{b). Anti.parallel and !yslne
polypeptide chain are linked by hydrogen bonds. R bonds between CO and NH o A((£hange ~n pttJ of surrounding medium can alter these (baslcaminoacid)
parallel segments in a polypeptide,
groups are not involved. groups of adjacent regions of charges an hence ionic bonds. '"'!:!'-''" ""•'"'"'u""-""""'-'•
forming a ~pleated sheet
the polypeptide backbone. Excess [H1 or [OH·] may affect ionisation of R-
groups of charged amino acids e.g. excess W results
{c)ITEifti8i'\(StffiCture· in-coo- groups becoming -COOH and excess -OH·
· Tertiary structure refers to further extensive-folding and·bending of a single polypeptide results in -NH 3+.becoming -NH2
chain, usually forming a compact, X(lbR,\(\"01) molecule, giving rise to the specific
@ fuvni1.?t111711 of a protein: 3. Hy_droP~obi_c inte~a.c_tic>n -_(moires+)
As a result of the folding and bending, residues that are far apart on the polypeptide chains o Formed between 'OOJJ-p610\\"" R groups
as well as those that are adjacent can be brought closer together. which are hydrophobic. They interact and cluster at
Structure is maintained by all 4 types of interactions - hydrogen bonds, ionic bonds, core of the protein to avoid water.
hydrophobic interactions and disulfide bonds - formed between o This causes the polypeptide to fold such that as many Hydrophobic
amino acid residues.
of "-!4""1fl of the hydrophobic R groups are shielded from R group
aqueou_s environment as possible:

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• Most hydrophobic R groups tend to point inwards towards the centre of the roughly
spherical molecule. Most hydrophilic R groups face outwards into the aqueous F. CLASSIFICATION OF PROTEINS 17 t,u,1w,w fl\ V1Alif
environment. making the protein~ Proteins can be classified into fibrous or globular proteins. Fibrous proteins have structural
H H 0 roles while globular proteins have metabolic roles. J.. _rilbl-4'<\ ~! "\.l 'l-'lt;
4. j)isu_lfi(ie_ bor,1d__I _bri~gl:! J I II
-N-C-C- -N-C-C-
11i ½, ,,.,,,.,~ •V\ w~i!h' l w'Mj- l'-.'Vf]'6) ' v· :V.:, 1(L
if..~ -qi\.lM\ 1 ft,, /ti J

r
• Fanned orllY "between ·1:wo cysteine amino acids by 1 ! {a)_llaerii"ci§lobin·,_ an example of a:·globular·protein
0

oxidation of sulfydryl (-..:S.!:LJ groups, which contains ?H, Haemoglobin is a transport protein, It transports oxygen
-"41teMr SH in blood, found in red blood cells of vertebrates. Heme gm~
o Disulfide bonds are strong covalent bonds. Strongest SH ➔
In the adult, a haemoglobin molecule has a quaternary
of these 4 interactions, they contribute to the stability of I structure with 4 polypeptide subunits, namely 2 a.-
many proteins. Increase in number of disulfide bonds r"' fH2 globin subunits and 2 J½Jlobin subunits,
increases stability of a protein to heat denaturation. -N-c-c- -N-C-C- Each subunit is arranged so that most of its hydrophilic
fll~l~W"(ll!MSZ
"'••o"'° tl1 ;~~,,, t I 11
A~ i
"'™'Oii1 et •
t"'1c/i' •
(d['QU3terna:rfSlru'CUfrl?/ B-D'f\
--~·"' ~
bOYI
Quatemary structure (usually) refers to the
association of two or more polypeptide
\fy\lC, ct z l'lo>lfllJ~ .»1d
(.o)
Cysteine
-··
H H 0

Primary
amino acid side chains are on external surface while
most of its non~polar, hydrophobic amino acid side
chains are buried in interior, away from the aqueous
surrounding.
Each subunit is made up of a polypeptide component
structure
l
"'~'"'
chains into one\ functional protem molecule called globin and a prosthetic (non~protein) component
(Figure 18d). called haem group. ______ .
I o Each haem group consists of a{porphyrin rtnQjand Vf ~ ( ; ~ ~v'.'
Each polypeptide is referred to as a ]subunit lb)
re,,§f "'
V
and the subunits are (usually) held together ""'""' .fan iron ion (Fe 2 ~..:, '\VI~ l\lf'Q, l\'. 1-()\~ ~ 11 -s ➔ 4 .ams
by H,
f!LVirJ
l1M)I;
d
•~"'f;',;j"tc,
!ff ) o1s
MJj!,ti\lmS
. o Fe2+ of haem group binds reversibly to 02, so 1
haemoglobin molecule can carry up to 4 0 2, at a timi,t"..:.;:
gure 1s. structure of a haemoglobin.

Proteins with 2 subunits are dimers, others ~iedshcct

with more than two are oligomers.
e.g. of a protein that has a quat~ma
structure _is haemoglobin {see Section
all proteins have a quaternary stru
Lysozyme, myoglobin and a~bu are
monomeric proteins (they have
polypeptide unit and hence are
to tertiary level only). ~.
00
.sOv
Randomc-oil
fanning oxyhaemoglobin. ~()' (D {®
~ In haemoglobin, the 4 polypeptide subunits are hel er by ionic bonds, t(~drophobic
Terti;.ry interactions and hydrogen bond~("~ ~'ti: i wi\\ w,'1YCl,.\rtl \f'\hWYI ~~\}
pot~1:::'chrun $!ruc!Ure o This allows the subunits to move .with ct to each other, allowing a change in
. position that influences its affinity for .. en.
IBmrting of one oxygen molecule~\ to aemoglobin subunit induces a conformation
one r<11 change in the remaining 3 subunits s their affinity for oxygen increases.
ised up o Thus the initial "hesitant' loadin e 1st oxygen molecule results in the rapid loading of
Quarem.iry the other 3. This is know~~ooperatlve bindin9..of oxygen.
'"""" o Conversely, when one su Unloads its 02, the other 3 quickly follow the lead, as a
conformational change their affinity for 02.
"- ~O::i-bo..trw;
)1l!::{ ~ Sat~ration

-------------------vfli:'- H-------nn---- ----u----- Figure 14. Structural organisation of a polypeptide:

"-:-i {J,qj t
Qn The side chains fa po\y-pep~de 1fshown Whifkmd o 1nteraf·ons jean t1ese R ~roup~ form? ; ~ [
\~ ~
t 1& -¾ S G 'i- i ICI I 11 ' ,
..-1 0

-,
H~N' Va1-fA1a-fCYs Asn Se Asp G!u , G!Y+.-'.-Ser-Lys-tcoo- : :g IJ\lle, bo \tM~cl
,I I I I 11 l'li : ~ • "v,\~"l'l)l6'l'n
Coopsrativlty

~
CH
~~ I
CH 3

I sH1
CH,
I II
CH 2 C
. I
(9H¼lz
@$J
H C~ (Crf.i)l
I '
lh",~
:
: . l$l
! Low binding /-+---
after first Oz
binds
increases
c= OHi CQ0/-1 SH OH !
~ ,. l
0

Hbond I I I
1't:11
-I -Ii-I
_'
-I -I -I
i
!
,, ___ 0

1
~
affinily for 01

Ionic bond -□
Hydrophobic O
interactions
--!-----../---!
-I -I
_i_ ✓ •• •.i...
-I !
-I :
'
:<
Figure 16. Cooperative binding of 02-
[.?1_], Concentration of ~gen (moJ L" 1l
Figure 17. Oxygen dissociation curve.
1 :
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What happens when there is a change in the primary structure of (iiW,~)

haemoglobin? Assembly to fonn _fjbre,s:
Genetic disease: sickJe cell anaemia (haemoglobin o Each tropocollagen molecule cross•links with neighbouring tropocollagen molecules
containing an abnormal !3-globin) running parallel to it. Cross-linking (which are covalent bonds involving lysine
residues) of adjacent tropocollagen molecules results in the formation of fibrils.
Normal haemoglobin: 6th position has ➔ this arrangement greatly increases tensile strength.
glutamic acid (hydpjlphilic) . '(c¼~O,V ts- .swi(/J'l.tl r----< ➔ staggered/overlapping arrangement of tropocollagen minimises points of
10µm

Abnormal
..JJ.. mutation 1\1,1,rAMii'ol.V M i?Je,1'1.0
haemoglobin: 6th position has
~ - .. weaknesse:~.•.!,.QJ19 ..lh..,e,__l,e,,.ng,th of the fibrils. I\M·
Assembly to form! collagen, f!bre:, ,si{;I.~ l_ \I\\
_\\\\\
va!ine (hydrophobic} ( ~%et \Vt 1•,J')lil,tctW'{I) 1 2 3 4 5 ~abicaa,, h~d!ni-
o Many fibrils in tum unite to form a fibre. arrru-itfi')Mt¼"t
(a) Normal red blood cells and the primary p-1111/C.
structure of normal hemoglobin
Conformation of pitpeptide changes ( d.-1~ Ml.~3 •4° Source- Biochemistry and Molecular Biology
2°1 Edition emott and Elliott
,IJ. &jl\,\c\W'el) '
Haemoglobin molecules aggregate together (1\.ltM"to1

~< I<
at low oxygen concentrations. Aggregation fl"O~➔
causes red blood cells to change shape. Ol~oi.iW{I m.t
,IJ. l<'W 0,)
RSC incapable of fulfilling its function. i.e.
altered property. lAltM-e,t functi™)
~-··
~
This illustrates that it is the sequence of nucle_otides !n -f;:,-"¼Q z 3 4 s ~ ~ ~ b r r . , 1 loose helical
loose helical
3 Cross-links between lysine ibrils """· Electron micrograph of
the gene and -hence tJ:te sequence of am~no acid ,_.;:]. (b)Sickledredbloodcellsandthep~imary• ~ 9 J m - polypeptides coiled to residues of staggered
~':~d~:1
many collagen fibres
residues, that detenmne the confonnat1on anh~- structure of sickle-cell hemoglobin ::i;en trop~collagen molecul~
therefore function of the protein. t-fV th tid forming 1 collagen fibn!.
~ Ffgure 18. Sickle cell anaemla e poIypep es. Staggering minimises weak

(b)';:Conag·e·ri- .. an example of a"'fibrous--ptotei P, ,~l~i'f~hJ,,,£~~-y points along fibrils.

Collagen is a structural protein. It is ti ~abundant fibrous protein in the human body

and is an essential component of Jssue in tendons, bone, skin and teeth. Point of ·,Fl_b,i:«?,U: '"u,unu,a.- u~au,m
A collagen molecule (aka _tropo, comparison , It~-...
chains (not a-helices) wound an
molecUle) consists of three helical polypeptide
ch other like a rope. Hence it is said to have both a Made up of Ion Made up of polypeptide c'hains folded Tnto
0.
secondary and a quatema~~ 'Stiiipe forming long, stra roughly spherical shape.

Each individual helix: 0

. ,__C:;,
Solubility
Insoluble in water0"Y? Soluble in water. Why?
~e,\illlt\,,\~>\tJ 1'f<Ywl" \>o!Ptr R. ~~ u,~ed,
n.v ~
o Each.of the three he~I polypeptide chains contains about 1000 amino acids and forms fQ wtJtte-\tJM1eCWe& 1

o
o
a loose he~ix a-he!\&-,
A collagen tri
The sequ
praline, Y 1
QJ
elix has@1/esidues per tum.

~y;~UY.-hY~!PMP.f,Oline.
.
~ rt1i'OO
l'l~cirox\ff 1
is usually a repeating tripeptide unit glycine-X-Y, where X is usually
~'#°~chaMa
i,,n(ll .
l~'rollA1 --i\co co..r\ fei,m rl: bOftClS WrTlr\
k-&-~\""d' -U-\Clltlte«l ~ teo 1c,~
n,, iC\V"1 I'll dlit"""t ➔ iVKolul(,e,
wC-ttsi Mol-ect.A.1e2,.

\Mo\ellAJC I'll\ "

Assembly to fonn1tf~P~.c:<;>:{1._~_!:J~l',}the triple helix): lrMI~
o The tropocoHag'en molecule ·can form a tight triple helix as almost Less variety of amino acids are used More variety of amino acids are used to
every third amino acid in each polypeptide chain is a glycine, the variety of amino to construct the protein, hence more construct the protein, hence Jess regular in
smallest amino acid acids regular in structure. structure. 1
➔ this allows it to fit into the restricted space in the center/ interior of KOs& --wi,, ~,~v-•sq """"w l\11) ~t)Q.,,'ttfNe, ~"'l_t" AW\t\'v,,O tJ¼.~ J'e_9\\MJ\'1Jl,
the triple helix (at the very tight j110ctioi:is between the individual Dt\MMtJ ~(k
helix). l•·!• •'1"K-Y""1le'® m Goll~~)
o Hydrogen bonds are formed between adjacent polypeptide chains Length of polypeptide and sequence Length of pOIYPeptide and sequence of amlno
➔ these interchain bonds increase tensile strength (ability to resist Len9tif .. , of: I of amino acids may vary slightly acids are always identical between two
snapping due to stretching) polypeptide between two samples of the same samples of the same protein, or else protein
➔ this makes the molecule insoluble. Extensive hydrogen bonds protein, yet protein is still functional. may not be functional.
are already formed between residues of the polypeptides,
hence interaction with water molecules are Umited.
1k
Functions as structural proteins.
-I•
Functions in a variety of metabolic roles.
o The bulky and relatively inflexible proline and hydroxyproline ·Function e.g.: collagen, keratin f\ e.g.: haemoglobin, enzymes, transport proteins
residues confer rigidity on the molecule. Figure 19. 3 helical ttP\(tt"afs'
polypeptides coil to Minor point: as result of chemical bondings, fibrous proteins are more resistant to high temperatures and less
fonn 1 tropocollagen. reactive chemically compared to globular proteins.
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G. PROPERTIES OF PROTEINS
(a) Sj;jlullilif{ _
~ o f a protein is dependent on both_its~and its@lb1lltY to interact With water.!
Globular proteins are soluble in water but fibrous proteins are not.
o This is because globular proteins have mostly hydrophilic R groups on exterior of the
molecules which interact with water but fibrous proteins have mainly hydrophobic R
groups on the exterior of their molecules.
o Fibrous proteins also tend to be very large and are crossed linked to each other.

(b) ·oen.atUiati0rt
Denaturation is loss of the confonnation of a
protein molecule which causes the protein to lose
its function. --
Occurs as result of disruption of interactions
(hydrogen bonds, ionic bonds, hydrophobic
interactions and disulfide bonds) that maintain
secondary or higher level structure of proteins.
Primary structure remains unaffected.
Deriaturation tends to cause a protein to lose its U
function. This may be a reversible p_rocess. :..,...,
Denaturation can be caused by factors·. such as: F i ~ ~ Denaturatlon and renaturation.
o Hevlt which indfease kinetic '>t.V
energy and intramolecular vibrations. Thif_("h,._~ A~ ttitit Ae.!N\it,!)·e..
0
breaks interactions such as hydrogen bon;f{itds. ~U(.tt!¾t ➔ ~ e-,~ ( bf"E<'-1~ \ \'\(C1_f-i!
o Cfo0n@P/ fn-pH which may -l• \YI M'fd.\'0~1
ionisation of R-groups of charged amin
. . bod fl} •· s ~ v\;i'\
( ~\4 1
f.t+ l.fNt>t.'-"
rm,..tt: b---1,-)
"'Jl;!<>
dh
•".... ··e·.·n· ce
.•.'.o·n· 1c n s. \ '1
\_,
, -ai 1,c'A\
1. l0WP1dcie011,re,qP'!ll!l,<-JO'ls
I J ,.__, d0a
.
(cfBUfferiri"q C9i;i'1Cify .r\~ 3· 1'11.ed\0w01 ffJt(P/ L 1--l b9'.Y;1& kit:Pk:2:1"'')
See Section C. Q" +· °'ll'lnie, <ei'V'\t C!ireo\cl>cctroi)
(d)'·····.
1oenucauon
Food test , Biuret test
2 cm 3 protein solution
+ equal volume 5% KO~ olour
·'-
~ = .,

urple
I
ation
G
Basis of test
A test for peptide bonds.
.
In the presence of dilute copper sulphate in alkaline
mix. ~ develops solution, nitrogen atoms in peptide chain form a
Then,+ 2 drops 1°<~ slowly. purple complex with copper (II) ions.
CuSQ4, mix. CJ Biuret is a compound derived from urea which also
contains the -CONH- group and gives a positive
result.

KEYWORDS include
amino acid, polypeptide, condensation, peptide bonds
conformation
hydrogen bonds, C=O group, N~H group, polar
disulfide bonds, sulphur
ionic bonds, acidic, basic, charged
hydrophobic interactions, non-polar
primary structure, secondary structure, tertiary structure
tropocollagen, glycine, covalent cross-links, lysine
globular, a-globin, 13-globin, haem group, porphyrin ring, iron ion {Fe 2..), cooperative binding

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NAME: CT GROUP:
TABLE OF CONTENTS
(A) Introduction .................................................................................................... 2
CORE IDEA:
1. Definition of an enzyme ............................................................................... 3
(1) The Cell and Biomolecules of Life 2. General characteristics of enzymes ...•••.•••..•.•.•..•••............•..•••.••••••••••....•...•••.. 3
3. What are ways of naming enzymes (Enzyme nomenclature) ............................. 4

ENZYMES (B) The Active Site ................................................................................................ 6

(C) Models of Enzyme Action ••••.••..•...•....•.........•••.•..................•.•.•••••..••.........••.••••• 8
1. Lock and Key Hypothesis ............................................................................ 8
Content:
2. The Induced Fit Model ........•••.••.••••..•........•.............••••...................•..•••..•...... 9
Mode of action of enzymes
(D) Energy Profile of a Reaction ....•............•....•••••••.•.•...............•••••••..••••••.............. 9
Leaming Outcomes
(E) Enzyme Cofactors ••.•.•.•.••••..•......•......•.••••••.•••.••..•....•.....•••••••...•••.................•.. 12
Candidates should be able to:
p) explain the mode of action of enzymes in terms of an active site, e~e/substrate complex, (F) Following the Time course of an Enzyme-Catalysed Reaction •..•.•••••...•••••..•......... 12
lowering of activation energy and enzyme specificity using !o.clk1td-key and induced fit
hypotheses. rU"
q) investigate and explain the effects of temperature, pH, e~concentration and substrate
concentration of an enzyme-catalysed reaction by measurins,,_~re's of formation of products (e.g.
(G) :.•c::p: : :~.~·~·~·~·~f.~~.~:~~~:'.~.~~d. ~:~•'.~.~~.: =:00~~:: : :·.:·: : :·.·: :;
measuring gas produced using cata!ase) or rate of disapp~~ of substrate (e.g. using amylase,
starch and iodine). ~ :. ::yme concentration ......................•..................~~···························~:
r) describe the structure of competitive and non-compet inhibitors with reference to the binding 4. Substrate concentration ································-r;.~Q..................................... 19
sites of the inhibitor. ~

:E§§t§i-ii~t?::i:=:~~i::~;~
s) explain the effects of competitive and non-com&ettuve inhibitors (including allosteric.inhibitors) on
the rate of enzyme activity. :i"\.:
Use the knowledge gained in this section in ~situations or to solve related problems.
-0_
Other important learning outcomes 4'\t ~cifically mentioned in the syllabus . G
(J) Lmks ····································~·;·································································· 24
• Explain the regulation of enzy,~~ivity and the role of enzyme regulation in metabolism.
e:,0
~
~
References
I (A) INTRODUCTION {V
Campbell, NA and ~ e , J.B. (2011), Biology (9 th edition), Pearson Benjamin-Cummings, San ,,.'lF
What Are The Roles df..Snzymes In The Cell?
Francisco
Taylor, D.J., Green, N.P.O., Stout, G.W. and Soper, R (1997), Biological Science 1 (3rd edition), In living cells, hundreds of different biochemical reactions take place rapidly and simultaneously. How
Cambridge University Press, Cambridge is it possible to have such orderllness in what must be a potentially chaotic situation? How can
Hoh, Y. K. (2002), Longman A~Level Course in Biology (Vol. I), Longman reactions take place so rapidly at such modest temperatures? The answers to these questions come
from a study of enzymes.

1. ··eatalysfs Enzymes act as highly specific catalysts that speed up the rate of
· metabolic reactions.

2. ·Rejjiif;iltion Enzymes provide a means by which individual reactions can be controlled.

The mechanism of these regulatory processes includes allosteric control,
competitive inhibition, non-competitive inhibition, covalent modification of
enzyme and variation in the amount of enzymes synthesised (which we wifl
cover later or in other topics).

Note: Enzymes are vitally important, because in their absence, reactions in the cell would be too slow
This handout is the effort of several Biology teachers at RI (Year 5-6}. It has and will continue to sustain life.
to be updated.

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1. Definition of an;~IJ-;ytne
IL EnzymeSJncie'ase 'the 'rate of reaction
ii) "" @
Enzymes are bi'Ological catalysts that in'crease the rate of a reaction and are chemically unaltered Rate of enzymatically catalysed reactions are typically 10 6 to 1012 times greater than those
at the end of the reaction and thus can be reused. They are effective in small amounts. of corresponding uncatalysed reaction.
@ ? CAA b< _,,.[e<'{
2. General characteristics of enzymes
&,fb.JW!el
- W - - ~ e , f>'~Uct Ill. Enzymes operal;e-at milder re.iction_ conditions
I. Enzymes are{r:oo,st@itob:Ulaf )?r'oteiilS~-f £., °iJ.
(Mw6\• 1)1_',"<i<{) . .,,". •.• .. . (~Cl\Y,; Enzyme-catalysed reactions can occur under relatively milder conditions i.e. temperatures
below 100°C, atmospheric pressure and nearly neY1!:ruJili_normally encountered in the
organism.
In contrast, efficient chemical catalyst often requires elevated temperatures and pressures
as well as extreme pH.

JV. Enzymes eXhibit spei:ificity

An enzyme or a particular type of enzyme will usually catalyse a specific chemical reaction.
o Absolute specificity (When an enzyme catalyses a single specjµe reaction.)
Example:
Maltase
Maltose - - - - - - - 2 Glucose 0 ~(J
o~
:\"\'

o
substances, e.g peptide bond.)
Example·
. Chymotrypsin
( vve,f:.~
Group specificity (When an enzyme attacks one~<;'i chemical bond in a variety of

iVl<l!
~ ~ t,8'V!-\-tifri i...,..,,.i,,
°"'""~ If-
➔ tnO<'Q... e;ftWQ..ht to IW 1 ~'ut( rrt e,
Polypeptides - - - - . . SIT\~* agmentsofpolypeptides olf{le!.W<l0 M11ltlpl-e,,
,. ~ • ru~re,,t o\Mti!s«.)
They consist of one or more polypeptide ch~~iled and folded to form a globular unit (ref. 3.. What are the ways of naming enzymes? {E~e nomenclature) 4, torq,~ 01t Me$
tertiary or quaternary level of protein org~ion)
Except for some of the originally studied e-- ·~uch as pepsin, rennin and t~s~~, f J z y ~ ~
As globular proteins, they are extreme'i));;p!ex molecules with Intricate 3-dimensional contours
and distinct surface geometries. CJ been named simply by. adding the suffix u-~~~~e
name of the substrate.

The action of enzymes depen~~eir 3-dimensional conformation.

E.g. Amyfase- hydrolyses amy!O§,.dlj
~·
There are exceptions be~~me enzymes can be composed of ribonucleic acids (RNA), e.g. Ma/tase - hydrofyses m ~
ribozyme or complexes ._~A and protein, e.g telomerase. (to be covered in later chapters)
O The International Union of_l:(_Qemistry {1.U.B.) in 1964 initiated standards of enzyme nomenclature

CJ?:F'
Additional info: Tlltra~ymo,w thom,aphyl~ rlbozymt> !.:!:I .
which recommended tha~me names indicate both the substrate acted upon and the type of
reaction catalysed. (j
In 1987, a catalyst made of RNA rather than protein was
discovered in a unicellular organism called Tetrahymena. The six major groups of enzymes now recognised by international agreement based on the type of
reaction they catalyse.
Such catalytic RNA molecules, which have now been found in
many other cell types, are called ribozymes. Until 1987, all
enzymes were thought to be proteins.

Many natural ribozymes catalyse the hydrolysis of their own

phosphodiester bonds or those of other RNA molecules.

► Ribozyme from Tetrahymena thermophilia

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Additr9_~aljn_fg_rmatiorr
Group Enzyme
cateaon,
1 Oxidoreductase
2 Transferases
3 Hydrofases
4 /somerases
5 Lyases
C:ifl>
6 Ugases
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Type of reaction Examples
Recall (from Protein lecture notes):
Oxidation/ Oxidases transfer hydrogen to oxygen. Q: What is the critical determinant in the biologiga) function nf a pmteini
reduction E.g. cytochrome oxidase A: 1'1~ ""i'i"-" CU " m ~ of.~~ s-ll\ D(•1Qili,,r,,,; ttwp,,jU\,,> ftMCli,n.
reactions.
CytH2 + ½02 ~Cyt. + H,O m\o ,v """""""- i. mm JS ~~l'"'"~"' 1,y fue., o,wi.w f-se.q•e,ice, ol-"-"lll'1D
2 types: Reduced Oxidised
~'Wis i\'lltt .,,_it, '11' ii! ""'1~(;) ~ti'<re.
Oxidases and cytochrome cytochrome
Dehydrogenases
Dehydrogenases transfer hydrogen to a molecule other than ~ THE ACTIVE SITE
oxygen.
E.g. lactate dehydrogenase
CsHsOs+ NAO :µ:CsH40a + NADH2
The'"A'C'tive Sile is an) Enzyme's Brtil1ytic Center I
1. The primary structure of the enzyme wit! determine its secondary and tertiary structure. This in
lactate Pyruvate tum will specify the overall 30 confonnation of the enzyme.
(Note: Lactate is oxidised to pyruvate whilst NAO is reduced)
2. Only a small region of the enzyme binds w·th the substrate. This is known as the active site.
Transfers a Kinases: Transfers phosphate from (usually) ATP to another
3. There is a precise 3D groove on the enzyme at the active site which gives it a specific
functionally substance.
important group
from one molecule
E.g. Hexoklnase
~~ conformation. ro===~=~
4. The active site typically consists of 3-12 amino acr Not all are in
(',.
in catalytic function.
to another ATP+ glucose ~ glucose-6Mphosphate Some are contact amino acids res1 ues w 1c interact reversib the substrate via weak
hydrogen and ionic bonds. (Note: Active site is onl found i mes, and it is involved in
Split molecules in All digestive enzymes ~nto this category.
catalysis. Sites not involved in catalysis are binding sites ) ~
two by action of E.g. Amylase ~
water 5. The R-groups of catalytic amino a~id residues, pr~thin the active site catalyse the
Starch+ ~~tarch + maltose
_,_ {one disaccharide shorter)
conversion of the substrate to its product. v I")..'
6. The rest of the polypeptide provides a framework th~ains the conformation of the active site.
Convert one Muta~'
isomer of a E.g~ oglucomutase 7~The specificity of an enzyme is attributed ~,~omplementary ~onfonnation/shae_e and
compound into a ~ ~ between substrate and active site. ~,
different isomer by cose-1Mphosphate !:::+" glucose-6-phosphate
redistributing the ~
8. The active site is not rigid. As the sub_:rt_'.l~~ers it changes its shape so that the active site fits
atoms ~ '¾. G is occurs in the respiration of sugars. more snugly around the substrate to fv¾!:" more stable structure (ref. to induced fit model).
Addor~""
groups
Carboxylases: addition of CO2
E.g. Ribulose bisphosphate carboxylase e;,0
~·
invot~ ter
~o Ribulose bisphosphate + CO2 - 2 phosphog!yceric acid o.:s
CS sugar 2 x C3 organic acid
r§
This occurs in the stroma of chloroplasts and is the principal
mechanism by which atmospheric CO2 is turned into organic
G
material.
Decarboxylases. removal of CO2
E.g. Pyruvate decarboxylase
Pyruvate - ethaldehyde + CO2 released
3C 2C
Intermediate step in the conversion of sugars to ethanol during
alcoholic fermentation.
Link together two Synthetases I Ugase
molecules at the E.g. Aminoacyl synthetases
expense of ATP Join amino acids to tRNA during protein synthesis.
DNA Ugase joins nucleotides together during final stages of
DNA replication
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I (C) MODELS OF ENZVME ACTION

2 well illustrated models explain why enzymes are highly specific.
An enzyme consists of 4 different categories of amino acid residues:
1. Ttie L.Ockand Key Hypothesis'(Fischer, 1894)
affe'cil'ltaet/blndlng';residties\bind '1'8\11irslbly,wilh the substrate while positioning it In the correct
orientation. I he substrate is held in active stte by weak Interactions Hke hydrogen bonds and
ionic bonds. Toese amino acid residues determine en~e specificity. substrate .amves at active site o! - - - substrate frt:S rite actiVe site, - - - products leave active site
b~catalytieresidues\act on the bonds in the substrate molecule and the side chains/R~~s of B112yme wherethemolecu!esare
a few of the amine acids residues catalyse the conversion of the substrate to product rearranged to form prodvcls
c)]'stri:ictural msldU/;;);meractto maintain the overall 30 conformation of the protein for proper
4- l'\rw»\'!f11WIW. ~ R. ~lftpS.
functioning of the protein.
d) Non-essential residues are generally found on the surface of the protein. They have no specific
1subsliate I
functions.

the en:eyme as a lhTee-dimensional stJ"uc;:tun!

c..C<\rJ.\l{ttl:.~'e\v.-e&,
n, ~
product~

enz;_-me available for

~
00
+ p
E + s l '¾," ES E
Eo,y= Substrate r-0
,.;,J' En~e/Substrate Enzyme Product

... -·-·;s:-7 Premise:

Complex

Enzyme actt~'sfte has a specific surface conformationfshape and charge

----······-------····-- 1'0 ··- . produced ~ e 3-dimensional folding of the polypeptide chain. ~ 9 11t
Q: How can the two a~acids, 'A~ and 'B' that are far apart along-the polypeptide chain somehow :
end up next to each ~'rin the active site? C:4-J ! G
The substrate is like a "key" whose conformation/shape is complementary to the enzyme
1. Tl'Uv 'PWti\lll)j 6\f\i\C.W.W ~ 111\l?i l):Q.~tHW1(.e.i ()'f-GtW11Mo .11.Ud.s 11"\.1fC¥l cl.efW"l\\1es rts J.." ~M ~/ .s.mteftlre., :
active site or "lock".
1- " ~ P,,N~. nlMM Mt\l l1' ,..wvicl•"f" <11M"1<'1l' 6uci;J "' ;,-,eJTx ••• f"l""'iS'.1 sheet> : When enzyme and substrate molecules collide in the correct orientation, the substrate becomes
'\1\-i\l "jtlv>liti' b0Yld1\1"f "1',tt,.eei,t -tl1e. [,{) "'°ol Nrt ~ ' 1!(-i;il:) \'1)14i<f<1otl'e<'-' i •
attached to the active site of the enzyme.
A short-lived enzyme-substrate (ES) complex is formed.
,t1_cl<l,"1e-• :
Catalysis occurs and products are formed.
,. T~c;al6"<>A'tr"1W"""' it fl.irt11&~1;ed IYltC riO ierftla,WJ'\;ll<ft,I"' "I'<'! ,~dv,9eti 0"'1d<.., j Once formed, the products no longer fit into the active site and are released into the surrounding
lb¼tt>ioovwls, i'l~ctm'Vllw, 1V1tWtctti;w 't~oi .~,1,ul't\v r~~ """"'" "''"' fM'l,1&>\ : medium, leaving the active site free to receive further substrate molecules.
!PB- i\'ie- dd\i!,l,m,tt "- '!l"""ft <lf- ille, aM~6 ,,¢,,is : Enzyme specificity arises because both the enzyme active site and the substrate possess

~ ~0"'1lt'lr<ml,!cll!V'e' wl\"v'!>
specific complementary shape/conformation and charge that frt exactly into one another.
4. T~l2k\i;t;,w !f.- f' 'Wl"iltlVW 11lt<s ret\Altr ,w flAi!I a- !
~W\IV\O ~~'OJ& ~ All1'1 0 1'\te. il'I~ &>,,-ow/ht /A~ ~i,i½e,r ,rr -4\,e, ~ <lf1e.. i
-- - ------- ---------------------------------------- --- ------------ ------''

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2. -,The·Jnduced·Fit-Me>dei,:(Koshland, 19591
Energy is needed to contort the reactant molecules so that bonds can change.
As the substrate enters the enzyme actjve 1) Initial investment of energy = Free energy of Activation (or Activation energy) = EA-
site it induces a change In the shape of the
protein. This change allows more weak Activation energy is the amount of energy that reactants must absorb before a chemical reaction
bonds to form, causing the active site to will start.
enfold the substrate and hold it in place.
Reactants AB and CD absorb energy from the surroundings. Energy comes in the form of heat
);, ~ cit >tOt Vli~'all~ from their surroundings.
ptlrftl-t ~t
c:::)-~=I:< i,:i-\'Vl%1~e..8
Vltl\l'e.,Qi ► lnducedfitmodelofenzyme-substrateinteraction.
Absorption of thermal energy:
mol=:ile
o increases the kinetic energy of reactant molecules for more f ~ I collisions
o increase frequency of collision of reactants
o thermal agitation of the atoms in molecules makes bonds more likely to break
2) The{ activation of the reactants ~s represented by thetpeak of tne graph.]

::'.i:::' ~
:"~"" Ill<: sub$tt:>le oombln"" wJth the e"':'.yme
•l 1n<luoo,; <:luinsc of shape $.<> th.ot the aci,w:
~ o'"
latt;:cr ~nd •Jh!t(;&mpound• on: unsui1::1blc
r,,,. renctl~ltl!,"'lli'e cri,,1me
At the peak, reactant molecules have absorbed sufficient free energy to react and are unstable
transition state
Bonds within the reactants can then break once they have abso[b~ough energy to become
'$.,_v
=

~
gn,11p• oflhc en:,ymc ""' broush! ,ogc,hcr ,:¾, ~
unstable.
In 1959, Koshland proposed a modified version of the ~10Af,~ key" hypothesis.
3) As bonds break and new bonds form, the molecules s~~1t:Jlheir new bonding arrangements
The active site of enzymes is complementary in con~~~/Vshape but not a perfect fit to the
substrates it catalyses. (h,., ._ and energy is released to the surroundings = exergoni~~on.
However, when the substrate binds to t~~me, it induces a change in the [ Exergonic reactions are those in which the free ene~he final state is less than the free energy
conformation/shape of the enzyme a n ~ i ~
The change in confonnation/shape allows
for the substrate, enabling the enzyme
Msite,
ctive site to be moulded into a more precise fit
orm its catalytic function most effectively.
of the initial state. 'i'q}
I (D) ENERGY PROFILE OF A R¥@ioN I Enzymes lower the activation energy (EA) e~ enabling reactant molecules to reach the transition

metabolic reQ1tti~s b\[\(OW'erm, ·eiAC@i3ti·t>n·'.E-her, EAJJtiali'riers·

state at moderate temperatures, ~ 9
Note: An enzyme cannot change t h ~ (free energy change} for a reaction.

► Enzymes: lowering the barrier of 9:i

activation energy, Q: What is the activation e~Q'(EA) of the following endergonic enzyme catalysed reaction?
Campbell 6111 Edition
qi;
'1=• ........ v....... ;;►,t--.;_
n
·--r-
Without affecting the free energy (B)

i
_@§L_ for the reaction, an enzyme -
speeds up the reaction by reducing
c-..·: ... _.-:·•::•·-<:·,_· the uphill climb to the transition state ...............,.. ~

~
~·.
'"cfli°'."i"'~~
at the peak of the graph.

~, y l~
Fmalsrme
I-~
·(j)·. . ·.•.· ·•·•
.··.·.·.•¾i .•.
ii
~i Products
I ·:S. t·® 4:,
Prcclu~
!
IReactan
~ ......................, -
?regress ottllo mai:aon-----.,

The graph shows a hypothetical reaction: Progress of the reaction ---1►

AB + CD enzyme AC + BO

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Molecular Basis of Enzyme Action
The following molecular mechanisms contribute to anowering of activation energyj One or more of
these mechanisms may work simultaneously in catalysis.
Method ..
1.::P'fdxiriiity"'effectS:
2:•Strain effects-·-,
3. Cirie"ntatlon·.·effects
4:;MiC~fjyii'orifn'E!nt- -i
·effects ·· ;,
5.:AciQ~~ase ·cataIYSisi
i:-ti": Explaill what effect will denaiuration have on the shape of an enzyme's active site?
L ""'~1\<i,,il'OO ~ -w,,~ ,¼...~,~~ ~JI lrn1vbovJ;1.I "'<I ,miw- L'e~P "11Crticit'l,S
i\11\T J\l?t'llic" ~;?.\) ""1{C\1>1?\\IWI qyt bV\J~.
.,_.ll',_Ml~•WMI SM1e et 111e, ell"l!{Me, ,; "ltevid O'lcl"611\"l)"-\1'ltt ~ 111e active S[fe;
Comment 3_ '1"1Cb lnvilill/V 61W ~ no \~(;MM~ 1\, ~/~ 0.Wf #-
Temporary binding of reactants next to each· other in the enzyme active site cw,>,Jc, t, 1'tei <IMtt•rte-.
increases the chance of a reaction. Uncatalysed reactions depend on random
collisions between reactant molecules.
[ill ENZVME COFACTORS
Slight distortion of the reactants as they bind to the enzyme strains the bonds
which are to be broken and increases the chance of breakage. Some enzymes require additional( non-protein}substances for catalytic activity. These are called
cofactors.
Reactants are held by the enzyme in such a way that bonds are exposed to
chemical attack. ,,J u,t,lyti:,, 'i"""P'·
!Vl'o
6V
1. ·1.11orga·niC ions (e.g. zinc in DNA polymerase) COFACTOR
Hydrophobic amino acids create a water-free zone in which non-polar
reactants may react more easily.
- Many enzymes require certain metal ions to change
non-functioning active site to a functioning one.

SUMMARY:
Acidic and basic amino acids in the enzym~ihate catalysis. (Knowledge of
detal7ed mechanism is not needed.) ,.

L
1

V
-
r

o ~r:-~&t,1iV1 to ocwr-i§ Jcr].,1.JM,

I'?'
Some of common cofactors are Ca 2•, Mg2•, Mn2+,
cu2+ and Zn2+.
The attachment of the ion with the main enzyme
(apoenzyme) changes the shape of the enzyme so as
to allow the enzyme-substrate complex to form more
easily.
... _.,,
...
Sll'l<llng

Cofuc1ot blndlng

protein.
0 f?j. 2. _Ce:enzym·es·'(e.g. NAO) ➔ Pitt, Vlrrt" f'WmMt»m~ fl!l.<"1~

~ I f) Substrates held In
Substrates enter active site; enzyme
changes shape so its active site • Cofactors that are organic in nature l½'b'/~
~ ¥(!
embraces the substrates (induced fit). ;,,,.: active site by weak

..
interactions, such as
3, Prpsthetic··gfoup·(e.g. haem group of cyt~~e oxidase in electron transport chain in inner
hydrogen bonds and
1111111 ionic bonds. mitochondrial membrane) ~
• pennanently bound to enzyme uO
€) Active site (and R. groups of 0

its amino acids) can lower EA (F) FOLLOWING THE TIME SE OF AN ENZVME-CATALYSED REACTION
Substrates and speed up a reaction by
• acting as a template for You need to know how to fol ~time course of an enzyme--cata!yzed reaction by measuring the

'
substrate orientation,
• stressing the substrates
formation of products (fore
using amylase) over time. ,(, ~ using catalase) or the disappearance of substrate (for example
,..,,..a..-.i-e,. QPl~m-e/
and stabilizing the
transition state, to' ~ ~w
• providing a favorable
mkroenvironment.
The methods are as fol~s: !-rn~n.- O;~tQ.. i:+--
0 Active • participating directly in the Measuring product formation over time -Sl.lbS1'-fitt CP'!Wi.t tP-,illhsltP(tU
site is
available
catalytk reaction. ™"'""'<:!)
for two new
•· 1U11t,of cli>'lf'Ft,~oto,&-&'<6"1MW
substrate
Example: Conversion of hydrogen peroxide to water and oxygen bylhJ: enzyme catalase
molecules.
catalase
Enzyme 2H202 ------+-· 2 H20 + 0 2

Independent variable: e.g. pH, temperature, concentration of substrate, concentration of enzyme

Products no longer lit in
the active site
Measurable guantity: Volume of 02 evolved
0 Products are
released.
Constant conditions: Other than independent variable (i.e. what you are testing), all other conditions

!'", have to be kept constant

Last8fJ3~ff-~PiJJJ.ifuJl!J8Jeo YT, Mrs C Khoo, Ms E Hor, Mdm S Cross, Mrs Wong$ H 11 Last ~ l b g o l t l l ' i ~ ~ YT, Mrs C Khoo, Ms E Hor, Mdm S Cross, Mrs Wong SH 12
 Raffles Institution H2 Biology (Student) 2018-2019
Raffles Institution H2 Biology (Student) 2018-2019
Experimental set-up:
· Explaining' the trend:
gradualBd Both the substrate and enzyme molecules move around freely in the solution. They collide with
cylinder each other and quite often, a substrate molecule collides with an enzyme molecule in such a way
calalase and that it fits into the enzyme's active site - an effective collision.
hydrogen peroxide
at20"C • \At time zero,\the rate of reaction is at its maximum (steepest). This is because the concentration
of substrates is the highest and the chances of an effective collision between an enzyme and
a substrate molecule is highest i.e. Higher frequency of effective collisions between enzyme
and substrate molecules
Q: The experiment can be improved by attaching the delivery tube in the above set-up directly to a
frictionless gas syringe. Why would this be a better approach? Therefore, rate of fonnation of enzyme-substrate (ES) complexes is also the highest and the

A- ll'i'j~
· IM'!mV
---i ~\ol~)IW "'it'le,
\"<>d• <Ml.
l;'l"™i IB!Mlt111,e, !Vt ""1 c~d/ffe!H1114/Wl1 + !tie/
rate of reaction is at its maximum.

Procedure:
1. Add enzyme (catalase) to H202 , mix and start the stopwatch.
2. 02 evolved can be measured by the downward displacement o f w ~ a graduated cylinder (as
shown above} or using a frictionless gas syringe.
As time progresses, less substrate molecules remain in solution i.e. substrate concentration
decreases, so there are less of them to collide with the enzyme molecules. Eventually all of the
substrate molecules are changed into product molecules and the graph showing product
formation becomes horizontal. The rate of reaction is now zero.
N
n\{;:,,
'"' ~
Q: In the space below, sketch a graph of the rate of reaction agai'!n~'iased on the experiment
above. The dependent variable for this experiment is the rate of 0 2 0,,.~·--·

~>If\
3. Record volume of 02 evolved at fixed time intervals ~ ~

Record your data and present it in a time-course graph: ~'?j 11,[l(t'!N\ / ~

'i- 'li
ao r,..· CIM's-r ~

\OII.Jmeor 3 5.o
oxygen.tm 4.0
7.0
6.0
- - - - ,(\V

~
\ 'Vti::,,' ~
i'-1}
3.0 0~" 0~
ao Cl
1.0 '\: :---,, '
no+--~-~---,,,,,,t,---~-~
0 ~ 100 ~(Jjp 200 250 ,.$::>
i<WlB/s
Note; For this time-course &,the axes are volume of products formed against time.

Trend· ,rp,_"'.
o~
-· (f' Measuring the disapp~e of substrate over time
Example: Conversion o~arch to reducing sugars by the enzyme amylase
1. Volume of 02 evolved increases with time.
Starch amylase mostly Maltose
2. Rate of 02 production decreases with time.
[ Iodine test
'tfor starch
Q:
1. With reference to the above graph, how is the rate of 02 production determined? 1) blue~b!ack in presence of iodine -+ incomplete digestion of starch
l½ mfe. '/- "- !N'>\W:l'W' l1S Au-e,,-1111ne.el ""J ft.-e;jll")V" iV1e.- '!W¢1U1t of-ill€' ~ . 2) brown in presence of iodine -+ complete digestion of starch
l',jf, ~ i\'leJ¼[4tl1& /""••wi fer ~•1t ti'Me, •·®· C,V,3◊-1
Independent variable: e.g. concentration of enzyme, pH, temperature, concentration of inhibitor
2. How is the conclusion of decrease in rate of 02 production with time made? Dependent variable: Starch concentration,
l\j- 'Vl~li¼O% il'v&'i""'iiuft\&e o ( ~ "t1\,)le, ,"U)WV,i~I ~<¼ ¼l'i Vl>!'De;
M ~ 'il'"\~(mrf DIW'ell,e, !Mlln. ,'l.i#Wl\lity-/J"¾e, · Measured quantity: Intensity of blue~black colouration

Constant conditions: Other than independent variable (Le. what you are testing), all other conditions
have to be kept constant

Last~~~.8J'JfJ.A~nr:'gJeo YT, Mrs C Khoo, Ms E Hor, Mdrn S Cross, Mrs Wong SH

" Last ~ l b , C ~ ~ YT, Mrs C Khoo, Ms E Hor, Mdrn S Cross, Mrs Wong S H 14
Raffles Institution H2 Blology {Student) 2018-2019
Raffles lnst!tutlon H2 Biology (Student) 2018-2019
Experimental set-up:
Aliquot out reaction mixtures
at regular time intervals Trend:.

/I· ~opperwith
;od;ne
1. Intensity of blue-black colouration/ concentration of starch, decreases with time.

2. Rate of starch digestion decreases with time.

Explaining the trend:

~8888~
1min 2min 3min 4min 5min 6min

\---... Analyse intensity usin~lonmeterjand compare with A.

conversion standard to obtain starch concentration ~'\. •
Ongoing
amylase and
starch reaction
mixture
Same as for catalase reaction.
-r Sometimes you may be asked to investigate how the rate of enzyme reaction varies with one
manipulated variable such as substrate concentration [SI.
To do this you need to carry out several experiments at different substrate concentrations [S1],
[S2J, [S3], [S4], [SS] etc. To obtain a decent trend, it is recommended to have at !east 5 different
values for the independent variable. All other variables such as temperature and pH are kept
constant and optimal.
Measure the pr_ogress of the reactions _over fixed .time intervals. Plot the g~s. (Graph A)
Find the .initial .'•.t•.•.
i •. ac·h ..co.n.c.•ntra
.. tion by finding the gradient of thh_~rtQElnt at time O min for
each graph. Plot the graph of rate against [Substrate] {Graph B). Th~hs A and B should look
Procedure: •-:::,,Vo like these below: -- · ~~ij
·1. Add enzyme (amylase) to starch and start the stopwatch~·
~e1y. ~
2.At fixed time intervals, aliquot 1cm3 of the reaction mi~!f
to the reaction mixture. A.-¾;.
test tube and add 3 drops of iodine Quantity of
product formed 0 [$6]
Rateo~~ ~
3. In the presence of starch, iodine turns from yellow~0iown to blue-black. [S5]
4. lnte · he blue-black colouration can be me~M using a colorimeter and this indicates the ~11:f
.. ~ ~
oncentratio of starch present
5. se a conversion standard to convert the ~eter reading to starch concentration. '&fi
[S4]

Q: Why is it necessary for you to aliquot a~ II volume of the reaction mixture at fixed time intervals ---1sw;:,~
instead of adding iodine directly to the r@cin mixture and monitoring the colour change over time?
G
_ \ii-. "6/d!itffl «-fV~Me, 1o ~~e1t"1 Mlfi'tte, w;I rVJ Vi'"'l-\- ji1e,, o\"!)>06-tti:,,, '4- ($2]
--'iflcell lolj 01m.i101,e,, _;r:;!j'lb'
-'Ml! ~ be.,;~~,ei ~cltce- ~t~XU WiilJ ~rz;h.vtVI:/ 1>1~V prew,,it "1"1'i)IN~ [S1]
~ 111,qr 0,c;t>e},-, '""''o time/min -------~[S_u_bstrate]JM
C.l''
Record your data and present it in a time-course graph:
[S1] [S2] [S3] [$4] [S5J [S6]

Starch Additional infom,aticn:

concentration/ The number of moles of substrate converted to product per mole of enzyme per second is called the
mol drrr3 turnover number, and indicates the speed of enzyme action.

···-·-· ··-···--· -- .. -·· --·------ ·······-·.

Enzymes tum over number
- mole of substrate converted to product per mole enzyme per minute
Amylase 1X10 5
Urease 1X10 6
Catalase 1 X 10 e

Time/s The turnover number is of value in comparing the actiorl of the same enzyme in different tissues.
The higher the tu mover number, the greater the enzyme efficiency.

LastMHSa~~-~A~rM!RXe-0 y T, Mrs C Khoo, Ms E Hor, Mdm s Cross, Mrs Wong s H 15

Last u ~ l , f 9 o r r i ~ YT, Mrs C Khoo, Ms E Hor, Mdm S Cross, Mrs Wong SH 16
 -,c-•~••-·- - - - - - - - - - - - -

Raffles Institution H2 Biology (Student) 2018-2019

Raffles Institution H2 Biology (Student} 2016-2019

For enzyme-catalysed reactions between 4°C to optimum temperature i.e. physiological

[jfil FACTORS AFFECTING THE RATE OF EN2YME-CATALYSEO REACTIONS ~a_tures, the rate of chemical reaction doubles for each 10°C rise in temperature (Q,o). ➔
A\ _.,,,.. llfW111""if""? ~ o r most typical enzyme reactions.
1:Btemperature <Wf!\l'IV\e! ,-14 ¢

_
1
ralaat.....-.ehreaetiondeel'easesdt.lQ-
b~c,len%y1'1'Jetnolo!',culos
- - - ; - -.. __ .I .
rateat'Wflichrmcficlninereasesdu$
IO~l<inetic:eni,cg,ol'Sllt>St~
.ancr~'mclecule$ .
""'""'wl
I.=;, Htol't~~\;:..
<M'l>jvl1U otl'I, 1YtttC!!'f,tl-,d
.. , 1,Reaction rate increases with temperature only until the optimal temperature of the enzyme is
reached. Each enzyme has an optimal temperature at which the rate of enzyme reaction
proceeds at a maximum rate (humans 25 - 400C).
-~-.l. I O\t·Q."1V'tl"\ t \OW
-............
.
........... ✓

/
//

, ......
~ . .
"""-'< '• Some enzymes have a higher optimum temperature. They tend to have a higher proportion of
disulfide bonds (strong covalent bonds) or numerous intramolecular interactions that hold the
tertiary structure of the enzyme together.
, • ac:tu;a1tateor~asaresutt

f /.;'"
,,.
/.. :
:
i .
ol'thecoml:llned~ct.Dless
nw,,lnlluences The increase in kinetic energy at temperatures beyond the optimum te ture causes

i" ,,./,; : •a,pperentoptm,m intramolecular vibrations to increase. This breaks y rogen, ionic bonds and other weak
interactions, such as hydrophobic interactions, that stabilises the conformation/shape.=
/2/2/. ~ \ ~- . -·-;.
denaturation. (At higher temperatures, covalent disulfide bonds may also break.)

.-: !.
\:.e~~
✓-✓-
\ ~
i
molea.les~- The substrate is no longer complementary to the conformation/shab~f active site of the
: \ andlhe

_/ "' .-9
l \ - ~ ► · 1r ~..:"'tilt <4-e<rl:>f""-"-' enzyme. Failure of the substrate to frt into the enzyme active si~~1itts in fewer enzyme-
substrate complexes being formed, resulting in the lowering of~~te of reaction.
/ i i ~ ~~~eel '"-A °I~ 1
' . ' - - - r - ~ - - , - - + ·-~-=~ 1<\,11,sjmti,- ~ o-R Q: How could you use the temperature sensitivity of an enzyif!;e· ) ~eaction to determine if starch
0

-
In
10

't1on
20

Al~~the.-.zymeisineoacthlest~,1/J'
::=-~-~•"'°""°'"'""9Y ,N"
At<ipllmumtem~lhe~~ 0~
30

T..,_.....,rc
.
40

"l\.
50 .

~
(2)
~

.. tov\UVlf1'\-u
~.,ac:tive-~
~' - -- ,.,,.,:,;,..,
'-If"¾
- --~:~--

511 ~-C-_,,.~
i=-=
(AA1 G~it'vl-1

.
ifdY)

es
of- fiS ¼M~ex. ;

;,
digestion by saliva is catalysed by an enzyme? . [ &!i\\'tlvi

2.pH
<l<itil<~ ~ ool\Q,\ ~m

o"-'
"
UY<II</. tY\"'IW>eJ r Wh'!'l¾ffil-tS;

,{Ji
:-,.c-,,
~
l'Vll!lhmJ
e,,Mtllie ·
J

stJ1·..,aru11:,11Ye~{Shapel · CJ wtvl\11~ ifl¾e{s

Each enzyme has an Optimal pli,_"<aj ~ich it is optimum pH
"• . """".,. furm,n,r So ES
n~
most active. The rate of reactiQt1>)$'maximum

.. . c,,v :----,~~Ml?!~ Cei)1 '""'

t>t """'
at the optimal pH. ,g;;v §
optimum pH
of trypsin
lheetfoot'orhighel'-1em~~•o • . $_.;'/'- ·,:.(,~_%, l?lPJiYJl'H)'J~
~the3hap&an,:llb,a"blily {pr<)f(lrn} "' - of pepsin
·1
•>JS• • '-~•-
·e enzyme in the
-• . r1:t-s. . andtochangethechemicar~oflheacfi:ve,site;
·e at pH 3. Other
·ork at neutral (e.g.
V reactldos'areoolo,'lgel°catalysed chymotrypsin) or alkatlne pH, are denatured by 0
such an acidic environment.
\ Beginning at a low temperature, \
• Increase in temperature results in an increase in kinetic energy of the enzyme and substrate
[Deviation from the optimum pHlresults in the
lowering of the rate of reaction.
*
a:

molecules, which will increase the frequency of effective collisions between substrate and (l."~ru 1cit~Li
enzyme active sites. Excess [H1 or [OH·] ions may affect the 0 2 4 6 8 10 pH
ionisation of the R-groups/side chains of
• This results in an increase in rate of formation of enzyme-substrate complexes. charged amino acids e.g. where[excess W\results in -Coo· groups becoming -COCH and
(excess-OH·{results in RNHi" becoming-NHz. ----.J
(I% Wh'1/'0Y ~
Increased kinetic energy also increased the number of molecules having sufficient energy to '<'ltl\\;\\~<'\ ;, :t'i!"ftlll(c<oo"'"""'
~ the activation energy barrier to form the products of reaction. If these affected amino acids are; ··~•qi · J

1. structural amino acid residues, it may result in the disruption of ionic and hydrogen bond
•lffl#i&& WW,t=factor by which rate increases with each 1o·c rise in temperature formation which deterrriine theJertiary structure of the protein. This changes the specific 30

-
conformation/shape of the enzyme active site. The enzyme is denatured.
iliiiiki&&44 kieJi iit!trf6fff@'fl'
2. co_n~ct and..catalytic amino a_ci~. residue in the active site, enzyme-substrate interaction
= "- ( \'0(0C <M"!""J:citm1) ·maybe disrupted and catalysis may not take place. E.g. catalytic activity may require that
- =

Lastgrr~smf.lli'iJ?i\°~.WJ8J"ec> YT, Mis C Khoo, Ms E Hor, Mdm S Cross, Mrs Wong SH 17

Last u~iJPtwiilll"IN!jilun::Mllo YT. Mrs C Khoo, Ms E Hor, Mclm S Cross, Mrs Wong S H
"
~es Institution H2 Biology {Student) 2018-2019
Raffles Institution H2 Biology (Student) 2013-2019
an amino group of the enzyme be in the protonated form (-NH:t). At alkaline pH, this group
is deprotonated so catalysis cannot take place. This is because at at low (SJ, the active sites of the enzymes are~eadily available~o catalyse the
reaction ➔ substrate concentration is limiting.
3. part of the protein substrate (in the case where the substrate is a protein), charges on its
residues will change and this will affect substrate interaction with the enzyme active site
At point 2 of graph, enzyme active sites start to getlsaturatedlwhich limits the rate of reaction
and/or catalysis as well.
At point 3 of graph, a plateau is reached. -Enzynie saturation is reached where all available
The end result is a reduced rate of enzyme-substrate complex formation, resulting in a reduced
active sites are occupied by substrate molecules. Substrate concentration is no longer
rate of reaction.
limiting. Instead enzyme concentration is limiting. (Further increase in substrate concentration
will not cause the rate of reaction to increase further.) Rate of reaction has reached its maximum
velocity (Vmax).
3.:_\;En'~~~lf~()n_C~ijf~tiOn(.

The rate of an enzyme-controlled reaction

ro "~oti¼el • ~ = the concentration of substrate required to make the reaction attain half
its maximum _rate ( ½ Vmax),

~=
is dependent on the frequency of ~1~"1~ ~
f,cct,Y 'At high enzyme concentrotlons
effective collisions between molecules adding more enzyme has no effect 11m.;,x
of enzyme and substrate.

With increased enzyme concentration,

on the rate of reactlon. The rate of
reai;tlon is no longer limlt\!d by
shortage or enzyme but by other
factors.
::=--;::---=
frequency of effective enzyme-
substrate collisions increases resulting I &v ~
-½✓~~~•or

J
in increased rate offormation of enzyme~
substrate complexes and reaction rate
:_,,.c,J?
~':'. ~1'11 i. 1,~ewr,
V
I
~:~~;;,
\l;,[IIIN le,,,.-" """'
VWW-)
ed, 1!> •tm)W!I
will increase.

At the linear portion of the graph,

enzyme concentration is limiting. Any
/4 lq
0

~ oubstrate
r e '"''""
zyme coneantrallons. adding more
"'lnc.reas% the rate of reaction.

wiH binc!'"""'·
eneyroo.
" ;, mora
to an empty act;ve'""'' •"
s,le on
'
:

'
l
.L
:,.,~Mt\( ➔ \
-=
0,-"
l 'iy)

~,u
Km [SJ
increase in enzyme concentration will
result in a proportional increase in rate .. n;:.
" Enzyme concentration Ul!liilll,\Jiiili!i,~
of reaction. '0'
Km is always the same for a particular enzy.~~'bt varies from one enzyme to the other.
At the curved portion of the graph, en~ncentration is not the only limiting factor(some other
factor is also limiting)_., 51-1~ ~~· It is a measure of the affinity of the en~};;r its substrate.

At the plateau, enzyme conc~On is no longer the limiting factor. Other factors are limiting CowK.!!!. High Km
the rate of reaction. lncreasi~~me concentration no longer increases the rate of reaction High affinity between enzy1 Low affinity between enzyme and
substrate. substrate.
4.($!!0~11'.~fil~~,;~ii1ra~'5 Low substrate concentat«lin needed to High substrate concentration needed to
► Effect of substratt'c~ntration 'ilm-'lx ___ - - - - - - - - - - - - -
attain half maximun'o'lbcity. attain half maximum velocity.
on reaction velocity Wan enzyme
catalysed reaction 3
[Tu! ENZVME INHIBITION
2 At high concentration of substrate the
velocity of !he reaction is i~endent of Enzyme inhibitors
s_ubstrate concentration
Some chemicals selectively inhibit the rate of enzyme-controlled reactions
(µ~, ""'"' fl1 ~ ~ )
'M•1,,;w (,W\,• 1< 1,'M>\1llu,y !Irreversible f- inh(bitor
forms covalent bonds
At low concentration of substrate the velocity with enzvme
of the reaction is proportional to substrate
concentration. - - -
~- inhibitor Competitiye
[SJ
formsweak' bonds with Competes with
enzvme substrate molecliles
At point 1 of graph, the rate of reaction increases proportionally with an increase in [S].
Frequency of effective collision between enzyme and substrate molecules increases. Rate of for aetiVe site
enzyme-substrate complex fonnation increases which results in an increase in rate of reaction.
Non-competitive
Binds another part of
enzyme
Lastcii~=:~r:m~:run~~Yeo YT, Mrs C Khoo, Ms E Hor, Mdm S CrQSS, Mrs Wong S H 19
Last uc:!liatftloHI~~~ YT, Mrs C Khoo, Ms E Hor, Mdm S Cross, Mrs Wong S H 20
 -----"-'''"-'"'''" '' ' " ' "'" ""

Raffles Institution H2 Biology (Student) 2018-2019 2018-2019

Raffles lnstltutk:m H2 Biology (Student)

1;,~competitive- inhibi,tjon--: 2. NOn-cgmpetitive 'inhibition A substr.ite-can~Substrate

bind normally to the
Competitive inhibitors when bound to enzyme, prevent substrate molecules from binding to The non-competitive inhibitor bears no actlves!t.e of an 1 Active site
the enzyme active site. sfcructural similarity to the substrate ,;,. enzyme. .,,,,
molecule so it binds to a site other tbaR--the ( ~i;s:t~!~
In most cases, competitive inhibitors bear ~imilar shape/conformation/to the substrate thus enzyme active site. 4'" MllSltM'v ~ En,vm,
com_petes with substrate for active site. .;- n'"'' It ,\\,. <illW ,
Most competitive inhibitors bind reversibly to the active site. Bonds involved are weak, non-
It alters the conformation/shape ofthe ""'" "'"l"'~'Clwt~)
specific enzyme active site thus substrate
covalent bonds. cannot bind to active site in the correct (a) Normal binding
orientation, so rate of reaction is decreased,
Reduces the availability of enzyme active site for substrate binding and hence reduces the
rate of the reaction. Non-competitive inhibitors effectively
, A~mp,11!1,o~
inhibitor mimles the ~
...
decrease the availability of enzymes as ·1t substrate, competing -----11a.:::;,~compet1t1ve
Characteristics of competitive inhibition~ Inhibition can be overco~creasing the substrate
concentration, [S]. This increases the chances of substrate binding to active site instead of Inhibitor
forms inactive enzyme-inhibitor (i~il\VIC.il:MiN for thaa-c:tlve site-. ... A inhibitor
binding. At sufficiently high [S], reaction velocity reaches the same Vm;u. observed as in the
complexes. eNl't11l'lrrla) J
absence of inhibitor.

...
Effects of non-competitive inhibitors[cannot
Ai:fd}tion~~info:
be overcome by high concentration of
substrate~
~
Example of competitive inhibition in the body ,, (;'V ,,, ~mpalllive Inhibition

;;;~"
;:,;: The rate of reaction will continue to decrease
:,,:
The enzyme succinate dehydrogenase (SDH), an enzyme found in t h ~ cycle, is competitively inhibited by
with increasing inhibitor concentration. When
~
malonate. The figure below shows the structures of succinate and ate. The structural similarity between
them is obvious and is the basis of ·malonate's ability to m i ~ i ate and bind at the active site of SDH. inhibitor saturation is reached, the rate of
However, unlike succinate, which is oxidized by SDH to fo rate, malonate cannot lose two hydrogen reaction will be almost nil.

-
molecules; consequently, it i~ unreactiVe.

<;DO"

~~ ~
-"" \~V
-;k
1
~
coo-

GO
~
~
~"~
~
....,.,,,., away from
:k:Uve- stte-. -altering
e eonfomu,tion of
e en:r:yme so that its
active s!te no longer _
Si>H
c;:,:½~ll ""'
COO"
functions.I Noncompetitive inhibitor

c-<><r ~ • 1 ~.,. (c) Noncompetitive inhibrtfon

~,._ ' .......

roa- ,..,,..,.
SUMMARY - COMPARISON ~~~N CO"i'PETITIVE AND NON-COMPETITIVE INHIBITION
notmaf readion
~i}:,,,,,,,,,
~
succirilc
0
add
"'"""
pro::!ucts

"'"""
compe~wely il'lhil!ited

..
Cl)!TlpetitM!inhibitor
malonic

I
I ~~~~~'-~
e
l ~~~~:~~~'-: -:; -:;----
c · No inhibitot

Jc::) nore.ialon
,--I\., po,sibl~
L........,/-enzyme

~wr ·-
bloa,d
~ I ~ .

o~c--~-r--~-o ~
=
dehydrogenase
. b·" H o-
fumar!cacid

►
Substrate concentration -
Competitive inhibition
'-------
Substrate concentration -

Non-competitive inhibition

Effect of competitive inhibitor Effect of non-competitive inhibitor

Vmn the same Decrease Vmax

Lastfi1tff.&"rhf?lrt\t!ffotMgJeo YT, Mrs C Khoo, Ms E Hor, Mdm S Cross, Mrs Wong SH 21 Last ujjlHl1Mib9':irOli$1J111gjlMlislVUo y T, Mrs C Khoo, Ms S Hot, Mdm S Cross, Mrs Wong SH 22
 Raffles Institution H2 Biology {Student) 2018-2019
Raffles Institution H2 Biology (Student) 2D18-2019

[N ALLOSTERIC REGULATION Feedback inhibition I End-product inhibition

Allosteric enzymes can be regulated by inhibitors and activators.
In end-product inhibition, a metabolic pathway is
M Initial 8!,lbSb'ate
~ (tmeomne}
·:JA,i10SfefiC.:~ii,Zymes;-:usual1y consists of two or more subunits (a)AU-..icactiwt=andlnhil:»1i=
inhibited by the binding of the end product of a
Where each subunit have their own ''"41\i'M1'1MIVJ~'re)J
'-"1 J
Allosterlcenym>{I
wlthfoursubunlts
Al:tfv11sl!a
{oneorfour)
biochemical pathway to an enzyme that acts early · I /~nine
in the pathway.
1. Active site that binds substrates
2 Allosteric site that binds activators or inhibitors
These sites are at different locations within the same
•

..,.,/4 "
,
-
e.g. amino acid
threonine.
isoleucine is produced from ,,,.~.-
F",-.--
th
_-;r_-~lfii.
~_· _
reonine · ,:-:
s:;:;· )

·-r:::.
subunit. R(!lgulatwy

a) Allosteric enzymes can exist in two conformational states.

1. The binding of an\~llosteric activator
/ binding of substr'ate at the a ve sit stabilises the
functionally active conformation
t the allosteric site
~,~};'"
) Active fofflt
Aetival1:lr
S!ablU:<ec! activo form
Aslisoleucine (end product]accumulates it inhibits
enzyme threonine deaminase in the first step of the
reaction by binding to the allosteric site of the
lsoltlllclneI
~"""" l1
enzyme, Hence, the end product alters the
conformation/shape of the specific enzyme active
site thus substrate cannot bind to active site in the
::lostetlc:. _,

6
;
i
ln19mlildlate 13

lnterm~ateC
Enzyme3

2 The binding of an\a!losteric inhibitor!stabilises the

inactive conformation of the enzyme
We-r
correct orientation, so rate of reaction is decreased.
i . ~-- f'-"
b) A single activator/inhibitor 1s sufficient to activate/inh1b1t the
activity of the enzyme.
c) The binding of substrates in allosteric enzymes exhibit ~~
Q
lnh!'"
• This prevents the cell from wasting resources in
producing excess isoleucine. J
~G
.o' 1

J~•
~_edlataD

cooperativity. So the binding of a substrate to the first ~,,_l\ii;;- . 1nact1veform Note: Although the diagram shows threonine deaminase
• - '!II:"\
subunit changes the conformation of the other subunits ,,:..~ c!
or "-•~M,,..,itn-+lve
(b) Coop-uallvlty, anolhartyj)II ot alli:astenc activation
to be a monomeric enzyme it is actually multimeric as
~
~V( -,-- (Q(:
·-. _. ..,,,-~
such that it becomes easier to accept subsequent ~flj with most allosterlc enzymes.
~U""
su1>stn110

substrates (-IM1"i-ffltU JUbreq"'"" ' - i,,¼,\~ • e • . "'""'"'

d) In a rate V against [S] plot, an S-shaped sigmoi~e often ~ " · ~ ~ .. Campbell o" Edition
indicates cooperative binding of substrate site. t~-t~
e) Note that the effect of an aHosteric inhibitri
reaction is opposite to that of increasin,
rate of

concentration. Hence, in the presenge~a"n allosteric

1he
lnactlw form Stal>llndact!ve
,,m
~"
Q: Why is it important to inhibit the enzyfTI~ier in the pathway?
inhibitor, the same Vma:r. can b e ~ ~ at higher substrate concentrations.
~,%
~ 1Cf m%\>ii 1e&1 lltl/1\ll ~ ic:vc,,.0{t rl-~tre& ~ntvtvsm'vita' \/Pl\'fm1.S. ,'itt!whieJ..\ttteJ,

0'
e:,0
~o,s Q: How are enzymes regulated~ non-competitive inhibition different from enzymes regulated by
allosteric regulation? ~Q""'
V-+----~~----- 1<11~ I N!>l='
Rlll>,'l\n1J1 -r I< - I G>\I~ -

Vo V,..x
► Graph showing role of allosteric regulation.
!m>M~W
l"1'Wl-l
<>5Gl\c\i,;
1"l1<M'.,
~ I .efu•tt •
•i11,re,
Additfon of an activator can lower the apparent Km,
2 1:E+!til'lib.i.M raising the activity at a given [SJ. Conversely, >11\s,,\;tjt 11\1,1\M\i,,iO MOYl.OMtNIV
addltlon of an inhibitor can raise the apparent Km, \£o NO
producing less activity. w~

K:0.Ff' Km x:._n· t,J

Last~~~lr:~gri,~Jnr~mYeo YT, Mrs C Khoo, Ms E Hor, Mdm S Cross, Mrs Wong SH

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(J) LINKS

Tonic Comments
Proteins Many enzymes are proteins.

Respiration 1} Hexokinase is an enzyme which catalyses the first reaction of

glycolysis
2) One of the most important coenzymes in the cell is hydrogen
acceptor nicotinamide adenine dinucleotide (NAO•), which is
made from vitamin B
3) Example of allosteric enzyme- Phosphofructokinase (PFK) cell.

Organisation of genomes Telomerase is an enzyme that is made~~ complex of RNA and

protein. Q
·,G
,s
Key words include: Kt?}
ta
~ 1),~
3D conformation
• active site
activation energy ~~
al!ostenc site Q'"\,'
catalytic residues G
complementary m shape a~'rge
contact/bmdmg residues~
denaturation Q~
effective collisio7'S
enzyme~subs~omplex
lnducedfit
kinetic energy
Jock and key
optimal temperature
• specific charge/conformation

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TABLE OF CONTENTS
NAME: CT GROUP:
(A) Introduction .................................................................................................... 3
CORE IDEA: (8} The Cell Concept ............................................................................................. 4
(1) THE CELL AND BIOMOLECULES OF LIFE
(C) Studying Cells with the Electron Microscope .......••........•..............•••........•.......... 4
{D) The Study of Cell Components by Cell Fractionation ........................................... 6
CELL STRUCTURE {E) Overview of the Cell Structure ........................................................................... 7
(F) The Nucleus, Nucleolus and Ribosomes ............................................................ 10

Content a. Nucleus....................................................................................................... 10
Detailed structure of typical animal and plant cells, as seen under the electron microscope b. Nucleolus ..................................................................................................... 12
Outline functions of organelles in plant and animal cells
c. Ribosomes............................., .................................................................... 13
Leaming Outcomes
(G) The Endomembrane System ······················································t~···"··.......... 14
Candidates should be able to: ~~ a. Nuclear Envelope ............................................................. ~....•............... 15
a. Outline the cell theory with the understanding that cells a~ t~~allest unit of life, all

\~'.~::-:;~~i!~:ii'.:--~
cells come from pre-existing cells and living organisms are ~l'QPefsed of cells.

b. Interpret and recognise drawings, photomicrograph ~ electronmicrographs of the

following membrane systems and organelles: rou mooth endoplasmic reticulum,
Golgi body, mitochondria, ribosomes, lysosomes roplasts, cell surface membrane,
nuclear envelope, centrioles, nucleus and nucl . (For practical assessment, students
may be required to operate a light microscoP,~unt slides and use a graticule.). (H) Other Organelles and Structures in the Cell ... ~~............................................ 22
c.
. . ,~175- . .
Outline the functions of the membrane~ems and organelles listed m (b).

d. Describe the structure of a typical ~"riar cell (small and unicellular, peptidoglycan cell
wall, circular DNA, 70S ribos~me€J'nil lack of membrane-bound organelles).

ff2,.-.,
References g
BIOLOGY, 8th edition C~~ll N.A and Reece J.B, (2009) Benjamin-Cummings Pub. Co.
Biological Science \h,.~ and 2, 3rd edition, Green N.P.O, Stout G.W and Taylor D.J, (2004)
Cambridge (/>.
Biology, 9th Edition, Mader, Sylvia S (2007), Mc Graw-Hill

This handout is the effort of several Biology teachers at RI (Year 5-6). It has and will
continue to be updated.
Last updated by: Mr Ganison & Mrs Tan YT
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Raffles Institution H2 Biology (Student) 2017-2018
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i,i\·,n ;:\ 2017-2018

I (A) INTRODUCTION I (8) THE CELL CONCEPT ~ :::J

This section is for information only. However, it is interesting to know how our modem ideas of
According to the classical cell theory or cell doctrine credited to Schleiden, Schwann and
the cell developed through the centuries, building upon the work of countless individuals.
Rudolph Virchow in 1938 with contributions from discoveries from other scientists:
Addi60t1a/ info: 1. Cells are the basic building unit of life
1590 Invention of the light microscope 2. All living things or organisms are made of cells
1665 Discovery of cells by Robert Hooke, who examined cork tissue and 3. New cells are created by old ceJls dividing (omni cellulae e ce//u/a)
observed box-like structures, now known to be dead cells. He gave the
name cellufae (Latin for small rooms) to these structures. The modem interpretations of the cell theory consist of the following:
1. The cell is the fundamental unit of structure and function in living organisms.
1824 French botanist Dutrochet suggested that the various tissues of
organisms are composed of 'globular cells of extreme smallness', with all 2. All cells arise from pre-existing cells by division.
organs being made up of cellular tissues variously modified. He 3. Metabolism occurs within cells and it involves biochemical reactions.
recognized that growth was a result of increase ~g.~ volumes and the
addition of new cells. Q' 4. Celts contain hereditary information (DNA) which is passed fro~~ parent cell to
daughter cells during cell division. Q
1820s-1830s English botanist Robert Brown observ,7J&Qaque spot in egg, pollen 5. In organisms of similar species, the cells are made up of simH~Wlical composition.
cells and cells of growing tissues of ore~" ,_, called this spot a nucleus.
6. All known living things are made up of one or more cetls~~cirganisms are made up of
only one cell and are known as unicellular organisms. are multicellular, composed
1835 Oujardin reported that cells wer8(p~llow but filled with a thick, jelly-
like fluid. rf{- of a number of cells. ~
7. The activity of an organism depends on the t o ~ ~ of independent cells.
1840 Purkyne gave the name pn ism to the content of cells, after realising
that the latter were livi iat and not the cell walls. Later, the term
more commonly use _(C) STUDYING CEL_LS WITH THE ELECTRON'liflGROSCOPE
- cytoplasm - was introduced (cytoplasm
+nucleus = protopla~ &' -
The invention of the electron microscope, ~ e 1950s allowed cell biologists to investigate the
1855 Rudolf Vircho~ncluded that every cell comes from an already inner workings of minute cells in greater and clarity. cru1
existing cel'-:~mnis cellula e cellula' (all cells from cells).
Fig. 1~@ifve sizes of cells and their components
1866 Haecker"'~blished that the nucleus was responsible for storing and

~o ~
Q}- ~
trans~hereditary characters.
<m;,.,,
Mid-19th C
-0
~oscopic analyses established the cell as the smallest unit of life, with ::i:: ~,,_ ✓,I WI -
~ continuity of life coming directly from cell growth and division.
....,-
mo~ 1/f"'!i, WU,, "
b«te:lum -~ -~
1875 Waldeyer discovered the partition of chromosomes during cell division. [ tlli'llf t1t111J tlllt',l ll'IIIJ 1!111111 :1•1111 \lll''IJ
.lA 1 nm 10nm 100nm lµm tOµm tooµm tmm
1880 Flemming showed that the mechanism of mitosis ensured the continuity , ~-microso:,pe,.-,,.,,
between one generation of cells and another. light microscope

1880-1883 Discovery of plastids e.g. chloroplasts

An electron microscope allows us to see structures as small as 2nm:
Mitrimeter(mm): 1mm = 10'3m
"'"'' 1a;;;i
1890 Discovery of mitochondria. Discovery by Hertwig that the development of
an embryo starts with the fusion of two nuclei, one from an egg and the Micrometer(µm): 1µm = 10'3mm 1C>'m lp,,rv, • 10' '"' ti
Nanometer (nm): 1nm = 10'3 µm 10..Smm = 1Q-9m
i1
otherfrom a sperm cell.

1898 Discovery of the. Golgi apparatus by biologist Camillo Golgi. ~ 9 t f The_,~qto which th~1\15P~m.1:fg~11:ffl);filfgef.;.{rnglil4ljl)§l(§1.lelCIDJeTr.
(It is important to distinQu1Sft between resolution & magnification)
'8J1lililfLgJJ,: Theffi'l~m~ whereb~.b~~~5ttjJJ@.1~-!'![~~te.
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The electron microscope has a resolution of 2nm (Le. two points that are 2nm apart from
each other can still be distinguished clearly as 2 separate points), whereas the light
microscope only has a resolution of 200nm (i.e. it cannot distinguish 2 points that are less
than 200nm apart)
(D) THE STUDY OF CELL COMPONENTS BY CELL FRJ\CTIONA!ION
The various ce!! organenes can be isolated from the other cell components for more detailed
studies on their structure and function.
Cell fractionation involves separating (fractionating) the organelles from one another.
Cells are first homogenised in a blender during which the cell walls and cell membranes
are disrupted but the organelles remain intact
A centrifuge is then used to separate organelles based on their size or density.

- 1. The homogenised mixture is spun in

• b
~'r(lJ
¼.~'
a centrifuge at high speed (e.g.

Fig. 2. Photographs of the same plant cells seen (a) with a light micr~pe, and (b) with \~~.-.
~·:)1
1 ·.·.·-.-.'"ij
~; 10,0000 revolutions per minute)

2. The resulting ~ g a l force will

an electron microscope, both shown at a magnification of about x2~0t,.
0 I. \1.:.1~
l ~I - ri -
• r:.,.1,.·
fu'
separate the cel!ft!Q~P~nents based on
Two types of electron microscopes are used:
• The transmission electron microscope (TEM) is
cells (the electrons are transmitted through the specim
usei~ ..~CJ
the internal structures of
til , -.
Homogenlzlltlon

~ " ' - llomogcnate

~"°I
¥~ their differerrt ~or densities

3_ Thei/&~nse (which is usually the

larg~ jifganelles will sediment out
~~~
Qlllfs , _,
fi
The scanning electron microscope (SEM) to study the surface of cells (the 1000 9
electrons scan the surface of the specimen). Th~,__ 1ng image appears 3-dimensional {1000 tlm61he
fQro& of gtl!Vity) pan spinning at even higher speeds,
1 he smaller or less dense organelles
:'.t~':hDrtrC111111tlelwilrilugallol'I ,, •

► Transmission electron microsco

specimen. Here we see a sect~·

ultrastructure. ln preparing the
~,!Ji
A transmission electron micros~les a thin section of a
tfidigh a tracheal cell, revealing its
, some cilia were_cut along their
r.;1;.;
e ,, -
K';,'
1,'
, ,:.
jn="'
.
W'"l
"""•
""'"
.l:°"'"
-'>·,-,- r,0
'¾s V
~·
~~
will start to sediment out

Size of Oraanelles
Structure Average Length
/um\

n::g
©J
lengths, creating longitudinal
across, creating cross s~~
ns, while other cilia were cut straight
I;;- ' !/{!ii ,.~0 Nucleus 5-10
''", - Chtoron!ast 5-10
~o I
Pelot rleh in ; :,J .- , '" •
Mitochondrion 1-5
qj
► Scanning elect-CJ microscopy (SEM).
=~;.:... .,);11 I :i-.'f.. }l; 1
Lvsosome 0.2-1.0

Micrographs taken with a scanning electron microscope show a 3D -~iJt_. i: .} Centrioles

Ribosom·e
0.3-0.5
0.02 (i.e. 20nm)

'f' f_"',:.:f,'..
~ ::t
image of the surface of a specimen. This SEM shows the surface
of a cell from a rabbit trachea (windpipe) covered with motile ~~;ct
Pellotrlchln i·:•t1 ··.jj···•

organelles called cilia. Beating of the cilia helps move inhaled debri plootsUcolls
are m,m a phmt) · :)
~
upward tcmard the throat j Q: State the organelles/cellular
Pellet fi,;:h ln ; ;,
"nl1erosomes." _', ·i components which are visible under the
Images taken usingsea.nning and transmission eleetron mi<:rosoope
Biology by Cflmpbe/1, 7"' edition, Pearson (plec:es ol p!.1$ma ~1, ~ light microscope?
m&mbmlle:u1nd •·~
c:eHs' lnlemal 7 A1
membranes) Pellet rich In
rlbo$omes

Fig. 3. Cell fractionation

B/o!oQy bv Campbell. i"' edition, Pearson

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I (E) OVERVIEW OF CELL STRUCTURE ~ :::::J MagnlNcalion

x30000j"PPt""-)
M1CFiOVILU
A typical eukaryotic cell consists of the following:
1. Plasma membrane or cell surface membrane (ref to cell membrane notes)
Defines the boundary of a cell and retains its contents
FLA-Gi;U.UMJ
CILIUM
Mornbr~oeb0<Jf'ld
=o!GolgitlOdy
GOl..GISOOY ~-·
"'
Mngnl~ootlon x30000 (appro><.}

Nlr>!,pafroovmi<k!plLl!I - . .•
Acts as a barrier which controls the movement of various substances in and out of the t,,o:,inglemlcrolubul0>ir> :'/; • ~~
i:,,ntmofaTSolaclllurn ""rt-'"{;_
cell orlbgolurn
Moll"lf>Cal,cn
2. Nucleus x50000 (""p,o,c} M,C,o,,m...,col'lllllnirlll
m;cro111omon!S
Contains the hereditary material that directs cellular activities MICROTUSULE
ENOOCYTOSISl@(.QC'YTOSIS
3. Cytoplasm Megnll!o,ulon X300XI (appm,c.)

~,-
This consists of:
a. Cytosol ➔ semi-fluid jelly like substance. Contains ions & organic compounds e.g.
"~ .
ves;cla lomung by infoldlng
p l = rnombron&

Fc,o;,,,olin!O<n:,ivulclewl!h
p~rnornernl>rMO
sugais, amino acids, proteins "
➔
b.

c.
Organelles

Cytoskeleton ➔ a framework of protein

#::,;:
means 'little organs'; discrete subceHular ~ r e s with a specific
function. Include: ribosomes, endoplasmic reticutum()61gi body, lysosome,
mitochondrion, chloroplast, centriofe
, such as , microtubules,
Ntnotrtpl""'ol
mlcrotlJbulco;n
,___ }f:t:iitf/.'_·.'~.,-~tf'
~"5,'
>Tl-!ENDOPI.ASMIC
RETICULUM
z,...i> ·'::12
;;~"®.,. ',.,,~.,
~:~""lion
microfilaments and intermediate filaments that i}yi "~~~;ro..) '//
c9~ ~fl>,
aryotic cells their shape
~
'fJf__e·IJ,J.,
:~~~~\;; "--~
4. Cellwall
'-~~v~
• Present ln plant cells {and not in animal ~external to the plasma membrane
·':'¾,fl>,'
Compared to the light microscope, s u ~ contents are seen in greater detail under the
MJl"OCHONORION

-----~15: "~~-"!;:~ =~-

electron microscope. The term cell ul ture refers to a cell's anatomy revealed under an
electron microscope. r.
~·
C:)0
c11ttsulraaa
m11n1braoo
Hll1atoctiromm1n

c~ surfaoa mQm!Jrnne ~ oall!Jlosra

cdlwllll
«Q ~ Euc!>fomlltlt\

"""-
nucle.JS
{ ~lc:ipe
chrcmoscma

nuel<ic:ilu:s
0
Twomomi,,,,n«;ol
"""l<'"'""\/Olope

cytoplesm----\:'--;;-
0
_ .,,o ey~~: ffl \
U0f Moll!'IJl<:<ltion
X30000{"Jlp'0<.)
vacLJol:!~ chlaopl<lsl
tonopfa5t .j1 l,lamhrano round
tt>oly:;ooomo

MDll!'<lication ·,
Fig. 4. An animal and plant cell as seen under the light microscope. .~~
Longm,m A-level Couroe in Biology- Pearson Education Asia (®pro>!.) Donsel)'-$\llln"llglobulo
of !pld In IM cytoplasm
Oa,!)le membroneend Ait>ceome/,e,,ln
811acl>Cd ,ibooorneo ol rough cytQplasm
endopl(ll;miereticulurn Magnillcailon
"""'XIO{~)
Fig. 5. A generalized animal cell with details of organelles

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=w=
Magnif,cQl;on
x20ooo{appro:<.) I (F) THE NUCLEUS, NUCLEOLUS ANO RIBOSOMES
CHLORQ!'t.AST , :"'"'- • Mlddlo lomello
Magnlllootlcr, >:70000{approx.) •, ,'> rlthlnpsctln
atN:ucleus··
:"~°."c.':b'::~~-~-•-<'",..[., •.t·~~ ,:~ P!imorywull

-~·
ricnlnoollulo$o

Pl=•membrnno NIICle_!lS
Gram>'l'l•ttllCkQI Chromatin
mQmblon••endO!llng P-m•mb"""' ~
~-"" ofacjj;,""ntc:dl

MICROTI.IBUI..E

" Mognincai,;cr,
.,, .. Ribosome

..
ff,
xsoooo
laPPl<'"-l
,~;;:_oe~~\"
;,;.Q; ;.Jr \)\:,:
0-lt ~ ~ cy~
·*
. ~~r ~:,;; ~~e.
Pore compiexii"s (YEM}
e; s,_,1i-~
,7 =ni=~•~
~Membrane
~·
eio
, ,_C,,,
~·
(lp' Ttansmissicm electron micrograph
of the nucleus
~ g . 7. Structure of the nucleus
Euc:htomatln

Structµ,e: rj}Q
The largest o~elle within the "'eukaryotic cell, average 5µm in diameter
Usually spherical / ovoid
ROUGI-I ENDO!'L,OSMIC
RETICULUM Uf'10GLOSUI.E
P- r.-.e<i 0y plasma momt,rone
lorming • po,,moc!Ooma RIBOSOMES Q: Name some substances that are exchanged between the nucleus and the cytoplasm?
<Xl~U..ey!Oplll!fflOI
adlacer>tcallS Mognifi<:a~on
"30000 l3PP'O"-) A:

Mog,,mo,,1,Cn
x30000(•P?<""') Don..~inirlg
Nuclear"'enve!Ope
globuto<>fipldln
thecytt,pia,;m Nucleus is surrounded by a double membrane {inner + outer membrane). Each is a
Ooubla mom~rane aM phospholipid bilayer}
all00!1ot!rll>ooomMol!WQh
RlbOO<>mO tr.o In cytoplaom
•nc!oplosmi~•etl"-"l<,m
Magnlr.r:a?lon xeoooo (SIJprox.) It is perforated by numerous nuclear pores which regulate the passage of substances
Fig. 6. A generalized plant cell with details of organelles into or out of the nucleus

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/' chl'rirrioSOin_e5_ J. Chrriinatin:

b. Nucteolus
Hereditary material of the cell made up of DNA.
Appears under the electron microscope as a spherical mass of densely stained granules
When a cell is not dividing, the genetic material exists in the form of thin elongated threads
and fibres
called chromatin (a complex of DNA and proteins called histones). These appear as a
diffused mass under the microscope. One or more nucleoli may be present within a nucleus
Prior to cell division, the chromatin threads .condense to form thicker, shorter structures Contains a large concentration of DNA, ribosomal RNA and proteins
called chromosomes.
Site of synthesis of ribosomal RNA (rRNA), a component of ribosomes
In a cell at interphase o.e.
a cell that is not underg61ng cell division),
Site of assembly of rRNA and ribosomal proteins into ribosomal subunits occurs
❖ most of the chromatin is in the loosely coiled, extended and diffused state, called
euchromatin, and is active in the synthesis of RNA through transcription.
Q. Label the nucleus, nucleolus, nuclear envelope, nuclear pore, euchromatin, heterochromatin
❖ Some of the chromatin remain tightly coiled and stained intensely, and are called
and other membrane bound or_ganelles
heterochromatin which is not active in RNA synthesis

!{iY' '
~ .
Fig. Sa. CelJ at interphase tl'.lJ.~oag prnph.,..
containing a diffused mass of ~'111 have condensed to fonn
chromatin osomes, which are thick enough to be
~ uished from one another under the
~
V"[croscope

-~
~-,
~
~"'
~t"t .
fZ:J--~~~-
100·nm

Fig. 8. Condensation of chromatin to fonn chromosomes http://valdepem1/os.comlbooklexportlhtmV208

Significance of the nucleus:
Q: N94Q1 Which of the following is present in all eukaryotic cells?
1. Contains the hereditary material (DNA) of an organism A cellwa!I
2. Controls the activities of the cell by regulating protein synthesis (e.g. synthesis of the B diploid nucleus
various enzymes, structural and regulatory proteins needed for the cell to function C flagellum
optimally) D membrane-bound or_@anelles

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c. Ribosomes
~ THE ENDOMEMBRANE SYSTEM

CELL

l<!rge subut1it
Plasma membrane Cytosol Organelles Cytoskeleton
(Part of endomembrane system) Microtubules
Mircofilaments
Small subunit Intermediate filaments

A Ribbon model of ribosome Membraneous Organelles Non-membraneous Organelles

http:/Aw,w-tc.pbs.org/wgbhlnovatphoto51/images/pict- 1. Ribosomes
2001rlbosome.il)'1 2 Centrioles
Fig, 9. Structure of ribosome
·O
~ Part of endomembrane system
~
Structure: NOT part of endomemb'.
Consists of a small subunit and a large subunit _St,,._f/j 1.
2.
Nucleus (Nuclear membrane)
Endoplasmic Reticulum (ER)
1.
2.
Mitochondri~~V
Chloroplast~V
Each sub--unit is made of ribosomal RNA (rRN~ proteins • Rough ER

Ribosomal subunits are assembled in th~eolus before being exported out of the 3.
• Smooth ER
Golgi Apparatus
;:$:'ftj
nucleus into the cytoplasm
Ribosomes are found freely floa=i
the outside surface of the rough
...~
~he cytosol ('free ribosomes'} or attached to
lasmic reticulum ('bound ribosomes'}. Bound
4. Lysosomes & Various Vesicles
,~
·s,,_'7:i_

and free ribosomes are structur;,al entical. ao,gh '°~c,~'""m N,cle,s

Prokaryotes have 70S* ri~rg~s. each consisting of a small (30S) and a large (SOS)
subunit (l;-,,,,,;;.
Eukaryotes have 803'~osomes, each consisting of a small (40S) and a large (60S)
subunit V Q
S* = SvedbergtJ!!,-s (unit for sedimentation rate)

Function: (j
Site of protein synthesis - translation of mRNA to protein
(This process will be covered in a later topic, DNA and Genomics.)
lear envelope

Q: Why are ribosomes found in two different locations? Do they perform different functions? ar pore
,osomes
ooth endoplasmic reticulum

Secretoiy vesicle

'
.-:;-,_;:,;.,ir,i►
-------
<$.~,~-:,:,. .',.r,,:, _.,_..,
cysosome

.. _., ,.-~,· 7 Plasma membrane

Fig. 10. Toe Endomembrane System

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Endomembrane System
b. Endoplasmic Reticulum (ER)
Some cellular organelles work together to transport materials into, out of, and within the cell. Smo.oth ER
This is the eukaryotic cell's endomembrane system, a manufacturing and material transport
network that enables the cell to make, move and break down cellular products.

The endomembrane system consists of the nuclear envelope, rough and smooth endoplasmic
reticulum (ER), the Golgi apparatus as well as the cell's plasma membrane, and includes the
vesicles that bud off these membranes for intracellular transport (moving material around inside
the cell), exocytosis (material leaving the ce!O and endocytosis (material coming into the cell).
Importantly, the endomembrane system does not include the membranes of mitochondria or ER lumen
chloroplasts. Cistern~rbo-,-.-m-~S';:p
. .F I._ ~Transitional ER
Transport vesrc:le~ R 200nm
SmootJ:t ER Rough E -
a. Nuclear envelop~

..•.
Structure: ~
• It is perforated by numerous· nuclear pores. The outer m~;';,ne of the nuclear
envelope is continuous with the endoplasmic reticulum.

NUCLEUS
.. (.S:J-..
--.¥ '.
,, ·.: . .:\io·
1•-~ ,
~-"-.,''
. ~--.,~J\.)IOooomo
~
Fig. 12.:structure of i-Ough and smooth endoplasmic retie~

Structure: ~
An extensive network of membranous "t~es and sacs called cistemae (cistern =
tank for holding liquids). &'
The ER membrane separates th~_@r'hal compartment of the ER, (called the ER rumen/
or cistemal space) from the c~oSQJ)
~· .
---
--
,.... l'tClni8'lt,v5pac:.

---
TWO types of ER exist in a cell:
Rbugh ER
Structure: ~Q
-;:j
~0

:...,____J - - Has 'bound'(l'~somes that stud the outer surface of the membrane, therefore
appears roug~hen viewed through the electron microscope
Cisternae appear more flattened than cistemae of smooth ER
Fig. 11. Detailed structure of nuclear envelope
Function:
Transport of proteins, which are synthesised by bound ribosomes on its sulface, via
Function:
vesicles to Golgi apparatus
to allow regulated passage of substances into or out of the nucleus As proteins form, they enter the cistemal space and fold into their native 3D-
conformation
Carbohydrates may be added to the proteins (glycosylation) to form glycoproteins
These proteins, synthesized by bound ribosomes, are meant for
(i) secretion out of the cell e.g. cf1gestive enzymes, ·insufin etc. OR
(ii) targeted for insertion into the plasma membrane
{iii} packaging into organelles (e.g. hydrolytic enzymes in lysosomes)
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Vesicles bud off from the ER, carrying the proteins to their next destination (usually the
Golgi apparatus)
The ER is a membrane factory for the cell; it grows by adding membrane proteins
(synthesized by Rough ER) and phospholipids (synthesized by Smooth ER) to its own
membrane. The ER membrane is transferred in the form of transport vesicles to other
components of the endomembrane system, which includes the eel! surface membrane.
Smooth ER
Structure:
Membrane appears smooth as it lacks ribosomes on its membrane. surface
Additional info:
Question: Some ribosomes found free in the cytOso/ and others bound to the rough endoplasmir; retir;ulum
when both these ribosomes are /dentir;al? What determines their Jor;ation
(Please refer to the diagram below for the flow)
(1) certain proteins have a stretch of polypeptide coded in their respective genes called the signal peptide. When
such proteins are being synthesized by the ribosomes, the signal peptide is the first stretch of polypeptide that is
synthesized before the rest of the protein.
(2) - {3) The signal peptide is recognized by a signal recognition particle in the cytoplasm, which binds to a receptor
protein in the Rough ER. bringing the ribosome to the Rough ER.

Cistemae appear more tubular than cistemae of rough ER (4) - (6) The growing polypeptide is translocated into the Rough ER lumen.

Function: Proteins without this signal peptide coded in their genes will not be recognized by the signal recognition partide.

The smooth ER (SER) contains many embedded enzymes that ~ s e the synthesis Hence, it is the signal peptide in proteins that determines if ribosomes are free or bound tt~ough ER.
of a variety of carbohydrates and lipids. ()'
In liver cells for example smooth ER enables glycogen ~~stored as granules on 0Pol)'!>cptide E)Ae\SRf'blndHo E)TI,<,SRl'blndnoa,
0
(Jn.cSRP!.-.,VM,o,¾...Cb'n..,a9nal- @"n,e,esi:ol
the external surface of smooth ER to be broken down,,:\o,glucose. ')'nlhMls ""'9tr,s tt>esi;nol peptide, ,,:c:e-ptc>r protein !tithe rn polyp,,~dcsynth~"¼ deavin~ enzyme tM comp!~
or, a free Mltlng !>)'nlhMis nu,mbrane. Thi< r<!ccpto, SI1!lltaRII-'
r,e,:um..._, w l i h. cutSoff the ~ d < > lea,,.,,:
rlb<:,,ome in momcntairlly. !$ part o1 ::> protein <oml'le• oustr.insl<><ati OI' si9""I ?CPtide. t.l><> rlbo,omc and
Synthesize lipids e.g. membrane phospholipids, ch~rol and steroid hormones the eyt<>00l. {b tr.>n,r«!rtion
co1<1plc>) the rn<!fflbr • fold$ into IU final
thath.~•,. membra.nc F"''"' si~na,_l ~P~ yo . confo<=tion.
::>nda.sig~~<leav~...,:,ym':: ----
1n liver cells, some enzymes of SER help d e· ~ ogs and poison.
SER in muscle cells store caz+ ions. (The c on of muscle cells is triggered by the
orderly release of calcium ions) ~ 1j
~',;

rP
~·
Q: What kind of cells has an abu~nce of rough ER?
A: '0j
;:,.

'5,,,0
//j
(Note: the followlng term is not in the syllabus - 'translocatlon complex'". There is no need to understand the process of
translocation at in part 4}

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c. Golgi Apparatus
d. Lysosome

Fig.13. Structure of Golgi apparatus

,$'
""~V
Structure:
Enclosed by a single membrane
Q'(
"::,,,..G
Contains hydrolytic enzymes (e.g. proteases, lipas~~cleases) used to digest
"'
Structure: __ ~ macromolecules ~
• Consists of a stack of flattened, membrane-bou~~s called cistemae and associated Contents are acidic. These enzymes have t h e
o ~ 1 rpH in the acidic rarige
vesicles called Golgi vesicles : (J"
Hydrolytic enzymes and lysosomal membra made by the ribosomes on the
Has a convex or 'cis' face, where vesi,..r&m the ER fuse to add new cistemae to
the Go!gi apparatus \,,,.!J>"'"'~· rough ER -~
They are transported via vesicles to th~""tgr apparatus for further processing
and a concave or 'trans' face givi~e to vesicles which pinch off and travel to other
sites
G
o' The vesicles containing the proces~~'zymes bud off from the trans face of the Golgi
apparatus to form Jysosomes U -
Function:
Cells synthesise a large number erent macromolecules. The Golgi apparatus is integral in
W
Proteins on the inner surfaCE\_"'Qf lysosomal membrane and digestive enzymes within
them are not hydrolyse~as'tlte three dimensional shapes of these proteins shield
~ ese macromolecules for cell secretion or use within the cell
!llQQ!:Mng, sorting, and acka ·
Adds short suga~fs (glycosylation) to proteins and lipids to form g!ycoproteins
vulnerable bonds from e
::s . tic attack.

and glycollpids ~V Function {refer to diagra~Oow for processes 1-3):

Modify exi~glycoprotein and glycolipids made in the ER by cleaving a sugar
molecule trdfllJtheir sugar chain or mocfrfying their sugar{s)
Formation of lysosomes
Produces polysaccharides (e.g. pectin) which are secreted from the trans face of the
Golgi, inside transport vesicles that eventually fuse with the plasma membrane.
Sorts and targets completed materials to different parts of the cell or for secretion out
of the cell
1. Digestion of m~al taken in by endocytosis (process 1)
o LysosomeYuses with vesicles/vacuoles (see note-) formed by endocytosis to digest
the contents within the vesicles/vacuoles
o The contents include food materials, foreign particles (e.g. bacteria} etc.
o The useful products of hydrolysis are absorbed and assimilated into the cytoplasm.
The unwanted products are released into the external medium by exocytosis
- A vesicle is smaller than a vacuole and it has a transport function carrying proteins,
nutrients into, out of and around the inside of the cell. A vacuole is bigger than vesicle
and it has a storage function.

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2 Autophagy (process 2)
e. Plasma Membrane
o The breakdown of unwanted structures within the cell e.g. old organelles
o The organic products from the breakdown process are returned to the cytoplasm for Refer to notes on Membranes for a description of the structure of membranes
reuse.
Summary:
3. Release of enzymes outside of cell by exocytosis (process 3)
o For the breakdown of extracellular content The different systems and organelles described thus far constitute the endomembrane system
of the cell:
o e.g. the spenn releases its hydrolytic enzymes by exocytosis to digest the sheath of
nutrient cells surrounding the ovum, in order to facmtate ferti[sa1ion
4. Autolysis (not shown)
lumen of pa!ICIQt!-= duct
--------~·••(liwetiiymc{:eyrnasm)
o Contents of many lysosomes released within the cell, simultaneously creating an
acidic environment; cell undergoes self~digestion or 'suicide' due to the work of the
hydrolytic enzymes.

I
.~
,,..r::Jt -~digestion 0 \
~.
~ - - - - - - - 8 uocytosis- fusionorsccrc:1c:xy iranulc with
plasma membrane to ttk:ase eymog,:ns in.to
panacatie dua..(\.,

\ - 7 maturc~"\n.nulcc:on.tai<1$conttntn.led
enzy~6~inac1M rorm ('zymogens'}

r::::::
endocytosis
7/ ---rv " rem:tlninJi: ,omen 00 ~ o r y g n . n . u k { G o l g i Yesie~)budding

-SD r;ii/-liifl;;~,°'~"'" ""'' "'

~~';_<:-i- \,~- _--
,/ ~ f r o m Golgi appa:ra1us

·,,• , if! \
11
plug¢cytj, Ya,;\!Qle

0 \
X 'V
O~ S proteins mow through Oolgi appar.uus

b
~ 4 vcsidesfrom endopla5mi, n::ticulumcany
, "'¾- "\ ,gcsted v•mg
,m,ooboodooo'. ,,. "' protcim:toGolgiapparatu$
rele:is 0 oflysosomal
~ n'M.lglaendoplasmlcftlicukim-UUnoaciclsu$1:d
,-~
enzymes by exocyrosis
'_-6' 0 · ~ ·,.,mpba-;, ·' to rnakc proteins wh= signal sequ= bind
-
0~.
~ to and e:riler 1he endoplUl'llic retieulurn

~ l-- 2~~=;==~~Am~~~hm~c;_~~::

'[~-,
""11 surface membrane
. ~ "Golgi
~~ ::opla.smi'Q'.i •PP"'ru•
smooth
/
mnochondrion
~:mbrnoe fom,ea ,mood the nuckuund binds to ribosomes initi.a1illg
protein 5)'tlthesi5
:!,,Q mkolo~odopl,,o,, m;<0ohood,;o,
\ I a.minoxickpasdn:omthebloodin1otheec:U
1
- ~ \ ~r::!'~~~~~7i!~-=:nes
bytRNA
.
F;g, (i:Jf .
agram illustrafmg 3 possible uses o f a lysosome ~ ~ L!_Y-f---:l~Pondrion-$Upplicscnugyin the form

Biological Sr:ience 1, Gambn'dge University Press ~ ~ (;;;? )_~;asmamcrnbranc

Q: The hydrolytic enzymes from the lysosome will digest the mitochondrion when both the
organelles fuse (see electron micrograph below). Suggest why the contents of the cell wi\l
not be digested if the hydrolytic enzymes in the lysosme were accidently released into the
cytoplasm Fig. 16. Synthesis of protein (an enzyme) in a pancreatic acinar cell

A:

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[lffi: OTHER ORGANELES AND STRUCTURES IN THE CELL b. Chloro.e_last

a. Mitochondrion

Ribosomes

A Str-Qma

- - - - - Inner and outer ...........

:;::===-
membranes .-~

}--Granum

Thylakoid

partk:le

Mitcchondrla!
.!lli~
~~ 'tiW;ar•
1
Fig. 17. Structure of mitochondrion v
·G
v~
electron
carriers
Structure:
_$5..rf}!
('..1>Kv
Spherical or rod-shaped
Enclosed by a double membrane, each a phosp(}ut1(.lld bilayer, ~<h,aak<>Jd
~ ~.membrane

N,,r;y!?l:o::::::;~--<hylakoid
Outer membrane is smooth
Inner membrane is highly infolded to f1
rt'¾.

erous cristae (singular:crista)

granum' fipid
droplet "'""'
grain
""~~,.
The inner membrane divides the mf .. ~ Within a granum
o the intermembrane spa~~een the outer and inner membrane
Fig. 19. Structure of chloropl~ (JV
o the matrix enclose~ inner membrane
The fluid matrix, conta~ 70S ribosomes, circular DNA and various enzymes Structure: ~•
involved in the Krebs ~ r • Lens-shaped. 2 µm b y ~
The cristae provi\;le,,.~arge surface area for attachment of enzymes that function in Bound by a doubl~~brane
oxidative phosp~'ryjation
Function: ('1> The space b e ~""tti'e double membrane is known as the intermembrane space
Wrthin the c~~last is another membrane system - a series of interconnected sacs
• site of cellular respiration. They cany out metabollc processes that generate ATP called the thylakoids
through oxidation of sugars, fats and other fuels with the uptake of oxygen. (Details in Some regions fonn stacks of thylakoids = grana (singular:granum)
Cellular Respiration notes)
Chlorophyll, other photosynthetic p·1gments and enzymes involved ·1n
The Krebs cycle occurs in the matrix whereas oxidative phosphorylation occurs on the photophosphorylation are located on the thylakoid membrane. They are organised
cristae
into photosystems I and II
The fluid outside the thylakoid is the stroma (site for Calvin cycle). It contains circular
DNA, ribosomes, enzymes and sometimes starch grains.

Fig. 18. Simplified Function:

iMermembrane drawing of mitochondrion
intennembrane space S'ite of photosynthesis. They absorb sunlight and convert solar energy to chemical
C De-1-bll
ofrnffl ,f't, outer membrane energy by using solar energy to drive the synthesis of organic compounds such as
stalked particle/ sugars from carbon dioxide and water. (more details in photosynthesis notes)
ATP synthase complex
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Q: In what type of cells is there an abundance of mitochondria?

c. Vacuole
A:

Q: Are there cells without mitochondria? Give an example of such cells.

A-·

Additional info:

Peroxisomes
structure
• Spherical, bound by single membrane
• Often have a granular or crystalline
core that is thought to be a dense
collection of enzymes

Function
• Enzymes transfer hydrogen from
various substrates to oxygen producing Fl!]. 20. striicture of vacuole ~ T

hydrogen peroxide as a by-product

• E.g. peroxisomes in !iver detoxify ~: ~Qj
. _. __ ,,t;:s
alcohol and other ham,fu\ compounds
by transferring hydrogen from the
poisons to oxygen ..
-~--<;~---~----
(lj,
Vacuoles are large vesicles d. erived from th~~plasmic reticulum and the Golgi
apparatus. ~, -

• The H202 fom,ed is toxic, but the \ "\; A fluid-filled sac bound by a single memb~
organel!e also contains enzymes that A.~ Like all cellular membranes, the v ~ r membrane is selective in the solutes they
converts H202 to water ~.<;), transport ()'"'
Animal cells ➔ have smaller~dgre numerous vacuoles than plant cells
~ Plant cells ➔ have a ~~ntral
a vacuole surrounded by membrane called the
Se, tonoplast and contains II sap - a solution of mineral salts, sugars, enzymes,
pigments, waste prod~
o,::s
(;r§ !:!!n£!im1:
(Animal cells) c'l>'!-.0
Food vacuolesYormed by phagocytosis enclose material for digestion by lysosome
Fresh water protists have contractile vacuoles that pump excess water out of the cell,
maintaining a suitable ion and molecule concentration in the cell
(Plant cells)
Concentrated eel! sap draws water into vacuole ➔ helps to maintain tlirgor pressure
for support in herbaceous plants
Role during plant cell growth ➔ as a cell increases in size, the vacuole can also
enlarge (as it takes in water) with minimal increase in cytoplasm
Storage of waste products e.g. calcium oxalate crystals
Food storage - e.g. proteins stored in vacuoles of storage cells of seeds

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d. Microtubules
e. Centrioles

► A pair of centrioles
organised at right angles to
each other

a triplet

Model showing tne fonnation of a microtubule by

the addition of tubulin

Fig;-21~ Structure of microtubules

Structure:
Hollow rods (about 25 nm in diameter)

Each tubulin is a dimer- a molecule made Fig. 22. Structure of centrioles - A¾.V
Microtubules grow in length by addition ~buun subunits and decrease ln length by Structure: ~ ~"""
disassembling units ~~ A pair of cylindncal, rod-hke structu~es
~);ned at right angles to each other
Their growth can be inhib'1ted by ch~ls, e.g. colchicine Each centnole contains nine triple icrotubules arranged in a ring
They have a certain degree of ~ s s and run a straight course in the cytoplasm Found within a region known as tif,' entrosome

Function: Q:,~· Located close to the nucl~u~ ..

centrosomes are found i~cells but centrio!es are absent in higher plant" cells
1. Help maintain the s ~ of cells :
)§{h plasma membrane, providing rigidity to parts of the cell where 0.::::,.
ng as cytoskeleton Function: ~
2. lntracellul sport: During cell di~n, the centrioles replicate and move to opposite ends of the cell.
Se,ve as tracks along which organelles equipped With motor proteins can move. (e.g. Play a role in nuclear division in animal cells, by helping to organise the formation of
cytoplasmic streaming of chloroplasts, movement of golgl vesicles and lysosomes) spindle fibres
3. Chromosome movement in cell division: Sp'1ndle fibres are needed for the separation of chromosomes during mitosis & meiosis
spindle fibres composed of microtubules help in the movement of chromosomes
to opposite poles in nuclear division (MTOC) microtubule-organizing center
4. Fonn structural component of centrioles, cilia and flagella The microtubule-organizing center (MTOC) is a structure found in eukaryotic cells from which
microtubules emerge. MTOCs have two main functions: the organization of eukaryotlc flagella
and cilia and the organization of the mitotic and meiotic spindle apparatus, which separate the
chromosomes during cell division.

ln animals, the two most important types of MTOCs are the basal bodies associated with cilia
and the centrosome associated with spindle formation.

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I (ll STRUCTURE OF A TYPICAi. BACTERIA~ c~~L ITiJ: GLOSSARY

Prokaryotic cells (bacteria)
The distinction between prokaryotes and eukaryotes is considered to be the most important
distinction among groups of organisms. Eukaryotic cells, such as animal and plant cells, contain
membrane-bound organelles, such as the nucleus, while prokaryotic cells do not contain
membrane bound organelles. Prokaryotes were the only form of life on earth for millions of
years until more complex eukaryotic cells came into being through the process of evolution. A
bacterial cell is an example of a small and unicellular prokaryotic cell.
Plasma membrane
Prokaryotic cell: A cell lacking a membrane-bound nucleus and membrane-bound organelles.
Includes bacteria and archaea.
Eukaryotic cell: A cell with a membrane-bound nucleus and membrane-bound organelles.
Includes animal and plant cells (compare with prokaryotic celf).
S, Svedberg units: Svedberg units are not additive, since the sedimentation rate is associated
with the size of the particle, when two particles bind together there is inevitably a loss of
surface area. Thus when measured separately they will have svedberg values that do not add
up to that of the particle formed when they bind together.
Higher plants: Plants that produce seeds, including angiosperms (flowering plants). Lower
plants include fems and mosses which produce spores instead of flowers.

Additional info:
~~
Circular DNA found In 0
a nueleofd raglon E:ndosymbiotic Theory ·G
The theory concerns the origins of mitochondria and plastids (e.g. chloropl ~ are organelles of
eukaryotic cells. According to this theory, these organelles originated as 'prokaryotlc organisms that were
taken inside a bigger prokaryotic the cell as endosymbionts

Flagellum j r,;_ ,,.,_,.

~
Fig.23. Structure of a ~ o t i c bacterial cell
outer mltochcmdri,..I
membrane
.Q .11111,!<Ul:::,UII !>
Ut::UV<:t:11 .fall~
Litt:: _.., ......~~~~~ai<aa•uo=:o v• ,._,..,_,., 1..,.,., .. ,,.,. t::'""... ' l " ' ' " ..,~.,~•

Feature
., f
'-' .,, Eukan1otic cell
;ar DNA is present within a
Prokarvotic eel!
No true nucleus. Circular DNA
is found in a nuc1eoid region.
'lJ' inn.er mltochondrlal mel@.:. ., . , .,
htlp1/www biolggy lcip,,i e<Julh19g,11rsesJtmfll12k2gnrjQfflllJR html (a good site to explore)
Nucleus & membrane bou;s
organelles "~
ucleus and membrane bound No membrane bound ~-
organelles are present. oroanelles are oresent. Some §•moorting evidence~
• Both mitochO(!t~d plastids contain circular ONA that is different from that of the cell nucleus and that
Ribosom~~ 80s ribosomes are present 70s ribosomes are present is similar to thatJ;if bacteria (in being circular in shape and in its size).
T)'lese organelles' ribosomes are like those found ln bacteria (70S).
Plant cells have cellulose cell
Peptidoglycan cell wall New mitochondria and plastids are formed only through a process slmilarto binary fission, like bacteria
Cell wall wall. Animal cells do not have present in bacterial cells Thus, they are autonomous organelles that grow and reproduce independently ln the cell.
the nresence of cell walls.
They are surrounded by two or more membranes. and the innermost of these shows differences ln
Generally larger. May form Generally smaller. Unicellular composition from the other membranes of the cell. The composition is like that of a prokaryotic cell
Size and organisation multicellular organisms. in nature. membrane.
Mitochondria and plastids are just about the same size as bacteria.
Extrachromosomal DNA found
Plasmids No plasmids Mitochondria haVe several enzymes and transport systems similar to those of prokaryotes.
in the form of plasmids.
Flagellum used for motility & Much of the internal structure and biochemistry of ptastids, for instance the presence ofthylakoids and
particular chlorophylls, is very similar to that of cyanobacteria. Phylogenetic estimates constructed with
Appendages No appendages fimbria used for attachment to bacteria, plastlds, and eukaryotic genomes also suggest that plastids are most closely related to
other cells cyanobacteria.
"Please note that the endosymbiotictheory does not explain the existence of a double-membrane nuclear

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(K) LINKS
The topic of cell structure is relevant to the following topics and learning oLrtcomes in the A level
Biology syllabus.

Core Idea Comments

Genetics and Inheritance • Replication of DNA in the nucleus occurs
during the S-phase of interphase
• DNA replication and transcription occurs in
the nucleus. Translation involves the
ribosomes.
Energy and Equilibrium • Light dependent reactions occur on the
thylakoid membranes of the chloroplast
• Light independent reppns occur in the
stroma ofthe chi~~
• Resp'iratory ie ~ (glycolysis, Unk
reaction, ~ ' V ' cycle and oxidative
phosp~i~ which produce ATP occur
in mat( · ristae of the mitochondrion
!(0-
Key words include: .&,,f'tf
double membrane .. ~ttened
m1tochondna/ m1tochondnon ~~ studded with ribosomes
cnstae Q,"" translation
matrix G transport vesicles
srte of aerobic respiration produ~P Golgi apparatus
chloroplast g secretory vesicles
thylakold membrane Q+;j glycosylation
thylakoid space ~ modification
stroma (j sorting and targeting
smooth endoplasmic reticulum vesicle membrane fuses with cell surface
membrane releasing contents via
rough endoplasmic reticulum
exocytosis
cistemae
tubular

Last updat&d by: Mr Ganison & Mrs Tan YT 31

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NAME: CT GROUP: ~ INTRODUCTION

All biological membranes are primarily made up of a phospholipid bilayer, whether they
are the plasma membranes (cell surface membrane) that surround the cells or
CORE IDEA membranes surrounding organelles.
(1) The Cell and Biomolecules of Life The phospholipid bilayer is ~7.5 nm (nanometer; 1o·8m) thick.

MEMBRANES A prokaryotic cell" has a plasma membrane but no membrane bound organelles
within it. (Fig.1.)
A eukaryotic ce112 has a plasma membrane and membrane-bound organelles within it.
Content
• Outline functions of membrane systems and organelles in cells. A prokaryotic1 ce!I - bacteria A eukaryotic2 cell- animal cell
• The fluid mosaic model of membrane structure .
Learning Outcomes
Candidates should be able to:
G) explain the fluid mosaic model and the roles of constituent biomolecules (including
phospholipids, proteins, glycolipids, glycoproteins and choles~ cell membranes. Centricles
(k) outline the functions of membranes at the surface of cells a mbranes within the
Plasma
cell. membrane
(l) Explain how and why different substances move across~ n e s through simple
diffusion, osmosis, facilitated diffusion, active transpo~Q, cytosis and exocytosis.

Use the knowledge gained in this section in new situ<t/j~r to solve related problems. Golgi
apparatus
. "
References · ~tr
Fig, 1. A typical prokaryotic and
• Campbell and Reece, BIOLOGY, 8th ~ ~ eukaryotic cell
• Green, Stout and Taylor, Biologi~~ ce Vol 1 and 2, 3rd edition
• Hoh Yin Kiong, Longman A-Le't5 urse in Biology, Core Syllabus Volume 1 (for AS
and A-Level) -'J Nucleus
• Roberts, Reiss and Mon~., anced Biology
",
Cj' Q. Name a membrane bound ~"'ii'eue and a non-membrane bound organelle?

TABLE OF CONTENT!()'\) ► .,.,_,,. "1111..i ~'Y!;, '

""~111,\. rj!;:,-
. --l>l-~
2

::i ~~~~~~=~~:!~~~'.~~~:: : : : : : : : : : : : : : : : : : : : : : : : : : : : : 3
3
G
2. Cholesterol ............................................................................
3. Proteins •.••••.•.........••.••••••••••••........................•••••.•.••••••.•••.••.•..
4
5 """"°' """'"el"'
4. Glycoproteins and Glycolipids (Carbohydrate components) ........ . 7
(C) The Fluid Mosaic Model .....•.....•••••••••••..•..•...........•.•••••.•.••••••••.•••... 9
(D) Functions of Membranes •.••••••••••.•••••••.•.................•••••••.••••••.•••.••.•. 11
(E) How and Why Different Substances Move Across Membranes •.•••..... 12
1. Simple Diffusion .....•................•.•••••••.•.......•...........•••••••...•.••••. 13
2. Facilitated Diffusion ...•..•..••••••••••.••...............•..•••.•.•.•.•.••.•••.••••• 14
3. Osmosis ....•...••••••••••••••••••..........•.••••.••.••••.••.••..•..................... 15
4. Active Transport •••.•..............•..••.•••.•••••••.•.•.•........•.••.......•...•.•• 17
5. Bulk Transport ........•.••••••.•.•••••••••.•..•...............••.••••..•••.••••.•.•••• 18
(F) Links .••••.••.••...•.................•.•••.•.••••••••.•••••.•........•.•••••.•••.•••...•..•.•.. 20
This handout is the effort of several Biology teachers at RI (Year 5-6). It has and will 1 Prokaryoticcell - cell that lack a nucleus or any other membrane-bound organelles Le. bacteria and arch ea
continue to be updated. 2 Eukaryotic cell - cell containing a membrane-bound nucleus and membrane-bound organelles Le any protist,
plant, fungi and animal eel!.

Last updated by: Mr Low Chor Meng, Mr Arrfl'Chan, Mrs Yeo Yew;1n Last updated by: Mr Low Chor Meng, Mr Ariff Chan, Mrs Yeo Yew Tin

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I (B) C~M£0NENTS OF CELL MEMBRANES R.rffles Institution H2 Biology (Students)

''-"active
1'f and they settle in a
2013-2019

As temperature decreases, the phospholipids become less

closely packed arrangement, drawn by Van der Waals forces and becoming less fluid.
LO: us the membrane eventually solidifies. ~
U) constituent biomolecules (including) phospholipids, The temperature at which membrane solidifies depends mainly on: ~~s ;reftlC!.-<)1
coproteins and cholesterol) in cell membranes. the ratio of saturated to 11 □ saturated hydrocarbon chains and; 0 QS(Q~ ~
the relative amount of cholesterol in the membrane ctVreWIDfeM e,&
Membrane will freeze at a lower temperature if it has a higher proportion of
phospholipids with unsaturated hydrocarbon tails. Kinks at carbon-carbon double
1.,jihOSPtJQtrpid_~ ffl bonds of unsaturated hydrocarbon tails prevent close packing of the phospholipids
A phospholipid has a hydrophilic =jinate nead and two hydrophobic 1vvi!111-~IAY Cells may alter their phospholipid composition in the membrane in response to
hydrocarbon tails/ chains. (Fig.2.) t,. changes in temperature. Many cold tolerant plants (e.g. winter wheat) increase the
It is an amphipathic molecule having both hydrophobic as well as hydrophilic unsaturated phospholipid concentration in autumn, which prevents the plasma
regions. membranes from solidifying in winter.

.e;O ~"'
~~
r}flj
b} Unsaturated hydrocarbon tails
of phospholiplds have kinks
' J:..
A· "'""""''
1-<1 that keep the molecules from
packing together, enhancing
~: ,- !l';!""'~obJc

-
membrane fluidity

Fig. 4. Phospholipids can

Fig. 2. shows a ph~~~:I ch.oline: a choline is attached to the basic move and contribute to
phospholipid struc~t,,,c1t the phosphate head membrane fluidity

" ' ~ " 1 - ' l r>lttt,\

.....
-~~P">t - c.,,!,"""""""
I.., lt1\.i);s,, 11.b
2. Cholesterol 0
(a)Mtcelle
{b) Phoapl,0Upld
bilayer
flj Arrangement of cholesterol in the
G phosphollpids layer

Biology by Campbell, 7"' edition, Pearson

3,
- 1 ' ] head
charged

~ ;[i ] :::::terol
~
Fig. 3. shows a how phospholipids spontaneously fonn stable bilayers and R 2
micelles in an aqueous medium E i!'j 'i°': stiffened
Phospholipids tend to form stable bilayers in an aqueous medium. They may also
C

1
_ ,?1 region
form micelles.(Fig.3) H (r''%
;-;, ·0,
] more fl,~
region
Phospholipids in the membrane are held together by weak hydrophobic 0~ -~t;,
interactions and van der Waals forces.
Since these interactions are weak, phospholipids and some proteins are able to drift
'"""" 0
Fig. 5. Arrangement of cholesterol within the phospholipid layer
laterally within the plane of the membrane thereby contributing to the fluidity of the
Cholesterol has a characteristic four-ring structure and is largely hydrophobic. (Fig. 5)
membrane. (Fig.4.) ~ ~ 01,..,\ ~ At'e- ~
Like phospholipids, it is amphipathic, having a hydrophilic hydroxyl (-OH) group and
[ .,, V1'6<W<WI~ i')\"1'\l>niii{,; the hydrophobic ring structure.
Last updated by: Mr Low Chor Meng, Mr ArlffChan, Mrs Yeo Yew Tin ~ ~\\ \Jl\"Wlll~ }' l-'1UY\-f\114Y
Ulst updated by: Mr Low Chor Meng. Mr Ariff Chan, Mrs Yeo Yewlln 4
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Raffles Institution H2 Biology {Students) 2018-2019
Raffles Institution , _, , , , , , H2 Biology (Students) ~l,j 2018-2019
The hydroxyl group of cholesterol aligns with the phosphate heads of the phospholipids
while the remaining portion of it is tucked into the hydrophobic core of the membrane.
a) lntegralftntrinsic proteins ~1:)h'ltm1~l'lV
Integral proteins, when folded, have exposed hydrophobic and hydrophilic regions,
Cholesterorui;i,i;gi;i,at¥s)l)e'ril'.braneJIUiclify -: , and are thus@mpfopathic.\
Prevents the membrane from being overfy fluid at (warmer temperatures)\ as Hydrophilic regions of a protein will consist mostly of amino acids with polar or
cholesterol restricts phospholipld movement through its mteraci1oriS Wlllt tli~ charged(acidic/basic) R groups while the hydrophobic regions wi!l consist mostly
phospholipids.(Fig. 6.} ~ cl~¥~v ~ of amino acids with non-Polar R groups.
The fused-ring structure of cholesterol is rigid, and it stabilizes the lipid fayer through ~.\~tels Integral proteins are inserted into the membranes such that their
van der Waals interactions. (especially at the regions of the hydrocarbon chains (~ Hydrophobic regions lie in the hydrophobic core of the phospholipid bilayer
closest to the charged head) (ii) Hydrophilic parts are exposed to the aqueous medium on both or either side of
Prevents the membrane being overly firm at\lower temperatures(as cholesterol the membrane
prevents the close packing of phosphohp1ds and hence hinders the
solidification/crystallization of the bilayer. 2 types of integral proteins:
(i) Unilateral proteins - reach partway across membrane
(ii) Transmembrane proteins ~ completely span across the thickness of the
c) Cholesterol reduces membrane
fluidity at moderate membrane
temperatures by reducing
phospho!ipid movement but at b) Peripheral/extrinsiC proteins
- ires it hinders Peripheral proteins are not embedded in the lipid bilayer but !oo~ttached to the
,y disrupting the
:ng of
surface of membrane or to integral proteins through wea~ic and hydrogen
~ (;V
." lipids bonds.

(c) Cholesterol within the animal eel! membrane ,._ ~ Both integral and peripheral proteins may be _a~~ to the fibres of the
extracellular matrix on the exterior side of plasm~~;ane. (Fig.8.)
Fig. 6. Effect of cholesterol on the phospholipidJl~r
, 1/l The extracellular matrix is the substance in whi~0mal tissue cells are embedded
Q Why is membrane fluidity important? R} and consists of protein and polysaccharides. ~
~ 1'11M~ ~ ~'- i,,,wll<P>1'l1tt\j <>f- 1110 ~ a e , ~•oi ~\1$ ltt-olbil>tij ill On the cytoplasmic side of the plasma ~ n e , they may be held by filaments
Wi\ffi, o, Ill \,6\11\~ •:[!:i of cytoskeleton. ~ f2
- J', ~1'1l ~~~ t,,- 11'[~tl'""1!\'1'">itt1""-""'~:::l,,-an~ l'\1rltiWS -l<l-'t'<U1ro ~""' o{-
The cytoskeleton is a network ~• ·f
~ubules, microfilaments, and intermediate

¾W, VVJ1,\'ll\,r/lP/le \111\!kl, ll'"O ~re, ~ ·:;:• CAttj 'I<+ "'1'\\ ceJM&\( ~ct<,\i\dR.
filaments that branch throughou ytoplasm and serve a variety of mechanical
and transport functions in the ce
Attachment of proteins ~cytoskeleton and extracellular matrix of the cell
3. Proteins -~•
-·--·" membrane helps to mai~il'i cell shape and fix the location for some membrane
Memorane proteins a e t ~ most of the membrane's specific functions. proteins. ,Cj
Plasma membrane -~ihn~embranes of the various organelles have unique collections
of proteins. (Fig:Z{Q""'""'
These proteins~•be classified into a) integral/intrinsic proteins and;
r.;
Ymnsmembrene
b) peripheral/extrinsic proteins Extracellular matrix
pnitelnsl Peripheral
membrene ~~Vl
protein
"'1n euoo,n, ~'o(r
,.-} uJl\!\oj\13' "'-l"(1t1I ...,l>f
i fllo,pbollolO ~•,.- f.-t;,\'< ➔ ~VO!'l">1'1V
:, blleyer
·~ l vice.,"""").
http://usars.rcn.r;omljkimbeJl.ma. Phospholipid bilayer
uttraneVBiologyPages!CICel/Ma

Cytoplasm
Cl'lCl1'~SIC~
en.,;Mel'Wl~
Fig.7. shows the different types of proteins found in membranes
Fig.8. Extracellular matrix on the extracellular side of membrane and
the cytoskeleton on the cytoplasmic side of the membrane

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Raffles Institution H2 Biology (Students) 2018-2019
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Q. Phospholipids move quickly along the membrane's plane, averaging 2µm per second.
{i) Membrane proteins generally drift more slowly than the phospholipids (ii) and in some Glycoprotein Cell Receptors
cases, they may even be immobilised. Can you account for the observations? Surfa,o• COlbebydr31os on ~el~ urva ai pdnt= ofa:tachmallt .;,- · /.
rorcthr~,infil~b.morio.vl=.•.i<inS,,lloml""a~ l . .
l)l"""'\mtne ~ . fe},\o\ ~ .,,~~V ➔ 'i"'f\wArru:') •"dmanyetl,a.rmQJi.cll]o:,.. , J

8ACT.eRlUM ~

;\ ~ ~ )W\eMI - ~ 'oe.,~VlCN\om\ "fu m,v '1t1o\v\tr ldil ih,1 VIRUS

. ~ f - ~'-
• ..:·e;;;:..,~~. \?f'.¾-,,;,;;
: CELL __,_, __ ,;
~e,"11,, <Yl ~M•~~ w -!ViW V,,:tt,,,,WI\U\~e-,>\P\tVlK o,J ille,,n,q-m\e,

4)1G1ycoproteins and Glycolipid~- (Carbohydrate components)

ch;·-~~cteristics
~-
Fig.9. Receptors are attachment points for various molecules and cells
Carbohydrates in membranes tend to be covalently bonded to either lipids or
proteins fanning glycolipids or glycoproteins respectively. et embedded in the plasma membrane?
Are usually branched!oligosaccharides) <IS-~~~ <:'
Vary from species to species, between individuals of .the~ species and even
Fig.10. Endomembra2·tem
v
Showing how protein factured in
among the different cell types in the same individual. 1
.,,~ li.... the rough endopiaffli:1' ticulum
- e.g. Four human blood groups designated A, 8, A~~ 0 reflect the variation in eventually end UP.'ftrrtb""'edded in the
the oligosaccharides on the surface of the red bl~~II membrane. membrane o~fed .

the carbohydrates of glycoproteins and glycoripfe's~e always found projecting out of !,\l?j
the cell fnto the extracellular matrix (i.e~the
{~ytoso/ic side of plasma membrane)

~ Jl)u,wr,,, ,., ~ I
:$'qj
Functions
1.-:eee:H;.;eellrecognition,, ~~
•
~4-«~ L~ . ,.!Ji
~
Pi~
• Membrane carbohydrates, bee of their diversity, are good cell markers that
differentiate one cell type ~ nother. G!ycoprote1ns and gfycolipids are very
important for cell-cell rec~ti~n.
cP
Cel!Mcel! recognition = j;,b~lity of a cell to determine if other cells it enco_unters are
alike or different fro~~-
Celkell recognitjpO crucial in the functioning of an organism. It is the basis for;
(i) Sorting out a@~al embryo's cells into tissues and organs. (£if1'1ftWJ)
(ii) Rejection o~reign cells by the immune system.
1. Synthesis of membrane proteins and lipids occur in the membrane of the
2.:-··ce11:re~ptors,•
endoplasmic reticulum. The proteins are embedded in the membrane as a result. The
As receptors for hormones in cell-signalling process of glycosylation adds carbohydrates to the proteins making them
As receptors for viruses, bacteria and toxins, providing a point of attachment so that glycoproteins. (Fig.10.)
pathogens and toxins can gain entry into the cell. Panthogens have exploited the
presence of cell receptors for their own purposes.(Fig.9.) ( Vl'YL1S k,fy\J\ 1'o re.cep¼·s) 2. Inside the Golgi apparatus, the glycoproteins undergo further carbohydrate
modification, and lipids acquire carbohydrates, becoming glycolipids.
Receptors for white blood cell recognition - when under attack, cells will express some
g!ycoproteins that are presented on the cell surface, so that they are recognised as 3. The membrane glycoproteins and glyco!ipids, are transported in vesicles to the
infected by white blood cells. The immune system will usually respond by destroying plasma membrane.
the infected cell thus preventing further spread of infection to other cells.
4. The vesides fuse with the membrane, and glycoproteins and glycoliplds are
presented on the outside of the plasma membrane.

5. Other transmembrane proteins such as channel proteins and carrier proteins are
embedded ln the same way.

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http:llwww.sju.edutbio/ogy/Ce//sPowerPtlchp11/s/d034.htm

(C) THE FLUID MOSAIC MODEL MembrJne- proteins ofa ltuman and munse

LO:
•. fl"'T~· , ~.
cell were labeled with different green and mou,ocol1

explain the fluid mosaic model in cell membranes. Cells were (osC-0 to form a hybrid cell with
a ~untinnous mernbr..nre.
Proposed by S.J.Singer and G.LNicolson In 1972
1. · "fliJid_t(refto pg 3)
Cell membrane comprises of phospholipids and proteins which are free to move
l fl11oreieo1r,-
Hybrid L'l!II membrane had initinlly distinL1 ::..~:~::
regions of green and red dye. pro101n t1iM•.Omlnutos lirriil • 40 m1fflll0<
laterally within a layer. (_eefl.'M'\~ \ ~ ~ of\orcol\fu;1on of\orcolltl/Olon

phospholipids are able to uflip-flopn from one layer to another but this is a rare nomon ee11
occurrence. !n !i:ss than an hot lhc two colors
intffillixed•
wcr,:

2. Mosaic character of the membrane

2. Mosaic·
random arrangement of the proteins embedded amongst the phpspholipid The freeze-fracture technique confirmed that proteins are embed!4!d in the membrane.
molecules resemble a mosaic pattern _-4,_~;;,,; Using this technique, biologists were able to separate the bilay~(~~n viewed under an
electron microscope, proteins are found to penetrate into th!\.'JY°rophobic core of the
membrane and their random arrangment identified. ,. r ·

•..

Q. Why is it a rare occurrence fo~QWholipids to flip-flop from one layer to another?

l\,e yrol~r \Ill~~ ~~, ½!llV!r ill !"l'i>< i½Y'"oh 1'J\QI \olf~V01"\0 ',le l-OYI,
I{- 1\/1~ ~ - , IN\~l~ ~ntm~r,t\6\e, (~e.'1< 1,H')
~o
Two separate definitive experiments provided evidence for the Fluid Mosaic Model. E face: exterior surface of cell
membrane
1. Fluid character of the membrane
P face: protoplasmic surface of
The fact that proteins drift laterally was established experimentally by fusing a human cell ,...,,,n mru-nhr::o1nP.
and a mouse cell which had differently dyed membrane proteins (Frye and Edidin, 1970).
The mixing of the mouse and human membrane proteins indicate that at least some
membrane proteins move sideways within the plane of plasma membrane.

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[I§): FUNCTIONS OF MEMBRANES 4. lncrease·surface area-for chemical reactions
- e.g. Highly folded cristae of mitochondria increases the surface area to hold more
LO: electron transport chains and ATP synthase complexes. (to be covered in greater
(k) outline the functions of membranes at the surface of cells and membranes detail under 'Photosynthesis' & 'Cellular Respiration')
within the cell. 5. cell-cell recognition-and adhesion
1. \~1:t:guJ_a~rm~m,er,it,:c,f~_ub,slcll,}C~_ ac,ro~::tbe-'rii8iribrane- _., ~ I nrtGVeJment of-81.!Wtancu Membrane glycoproteins and glycolipids are involved in cell-cell recognition .
. Being seie~tiv~ly p~~e-able, the membrane only allows some molecules to cross .J; Such glycoproteins and glycolipids are also responsible for the unique surface
the membrane directly without assistance. (/tVYl\1D!Y-t~'M'lt M topography present on the surface of cells. The ability of drugs, chemical
As such, movement of most substances across membrane can be regulated to ~l~tf/;yJ messengers and viruses to dock: onto such molecules has far-reaching implications
create an environment within the cell/organe!le (or part of) that is different from the in medicine and drug therapy. Ref to pg 7.
external one. (Adhesion) Membrane protein of adjacent cells may hook together to form various
NonMpolar l uncharged molecules are able to dissolve and diffuse through the kinds of junctions such as tight junctions or gap junctions
hydrophobic core of the phospholipid bilayer. 6. Sigil-al transductiOn
The same hydrophobic core however, repels charged and most polar molecules Some transmembrane proteins serve as cell surface receptors to transfer
such as ions, amino acids, organic acids and simple sugaJ&,,. They must be infonnation from the environment into the cell when specific molec~ (ligands) bind
transported across the membrane by transpart proteins. '<> i""- ~b~ ~
a M e.g. glucagon (honnone) bind to the glucagon receptor_ membrane which r,~
2. · "Corilpartm·entarisitiOri ~G triggers a cascade of chemical reactions leading to th;:,_~olysis of glycogen to
glucose ~ ¾-
(The ability to control the movement of substanc~
~oss the membrane makes
compartmentalisation possible). It allows X0= (Glucagon is a peptide hormone and cannot~e cell because of its large
size. The binding of glucagon to its recepto igger a cascade of signaling
(a) Formation of unique environment for h i gs~ l~lised
y activities activities within the cell to eventually activate~- nzyme that hydrolyse glycogen).
M e.g. lysosomes maintain an acidic en · :nt that allows its enzymes to work at
e,;u
(E) HOW AND WHY DIFFERENT SUBSTANCW(lVE ACROSS MEMBRANES I
its optimal pH. ~~
'\...:'
(If the lysosome were to b~rs~ hydrolytic enzymes would not work in the
neutral environment of the ~Y-
LO, ~~• •
(I) Explain how and why different ~ nces move across membranes through
U simple diffusion, osmosis, facm
exocytosis ,"¾.. ,.
diffusion, active transport. endocytosis and
(b). Accumulation of charge~ "'and formation of chemical gradients across
membranes ~Tl)"' 0"'
Movement of substances~ membranes is vital for the cell:
- e.g. accumulatidll't).; high concentration of Na .. ions outside the axons and high
concentra~i!l\._~"Zr~side the axons generates the resting potential in preparation 1. To obtain nutrien~energy and raw matenals
for an actl?~ential
2. To excr:ie~ubstances
e.g. ac~ulation W ions in the intermembranal space in the mitochondria and " re1il:W,i\'!i,
3. To sec;~te U~ul substances c.e •T eM'ttf ~ 1 lrLO')'\.'¼O\-if$1 ttc.)
within the thylakoid space in chloroplasts establishes a proton gradient for
chemiosmosis and fonnation of ATP (to be covered in greater detail under 4. To generate the ionic gradients essential for nervous, muscular activity and ATP
'Photosynthesis' & 'Cellular Respiration') production.
(c) Storage offood source 5. To maintain a suitable pH and ionic concentration within the cell for enzyme activity
e.g. starch are stored in specialized membraneMbound organelles called
amy!oplasts in plant cells. Five ways in which substances move across a membrane ~ ,,,e)
1. Simple diffusion
°'""'""'"e.! me, P~1'f_ pe,,-mewo _
3. --Loc·attSa'tiOriot·pro-~ins_,of a, relatecJ_,~_~i;tcti_Ori:ai·Ong a membrane 2. Facilitated diffusion W,Wi!r\'il' i1J)'L'I< "1tE- o f - - ~
Jt allows functionally-related proteins to be grouped together so that sequential 3. Osmosis cf-nwte.O··tlerr-- -l-\'tlfttC M ~ ~ ot Ce,(l
biochemical processes are facilitated.
4. Active Transport Ji
e.g. enzymes and proteins are grouped into photosystems If and! on thylak:oid m<t,"'
5. Bulk: Transport (endocytosis & exocytosis)
membrane of chloroplast; electrons from PS II are shuttled to PS I during IJ ~~ "IY\\J'O'- ilf-h\?llll
photophosphorylation. (to be covered in greater detail under 'Photosynthesis')
ll) ~ ~ll'WfW
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The 5 ways can be classified into active or passive processes. e. s·unaCe- area· of Cell membrane
(a) PASStVfrP~OCESSES: simp!e diffusion, facilitated diffusion and osmosis t surface area, t rate of diffusion
During simple diffusion, facilitated diffusion and osmosis, substances are transported e.g. microvilli of cells lining intestines increase the surface area for absorption of
down their concentration gradient
nutrients
These processes do not require energy in the form of ATP {adenosine
triphosphate).
f. Distance l ~£>itww6-
\~~)~
If
,,, i'lor ~ foW,1 cl- ~ci11'<'.....,""""+-- t distance, ,l. rate of diffusion
··· ... ........ . (eA,o!i) ,C i'l<O"fJ,!n) Therefore diffusion is only effective over very short distances 1_ !J
(b);,ACTIVE PROCESSES,:: active transport and bulk transport
During active transport, polar molecules and ions are transported across a
l•\~~1~01).,,, r>iv<>1ve.>~,.,,..,,,.,,,nb trnr.,,O\'f "'7\~ws-<,c;,,,11,.i~~
membrane, through protein pumps, against their concentration gradient. This 2. Facilitated Diffusion (Substances Involved: polar molecules & ions) ct;vnW~ffiM.
requires energy in the form of ATP and is an active process.
Facilitated diffusion is similar to simple diffusion
During bulk transport, large molecules are transported in and out of the cell via
in that it is a passive process where substances
vesicles. The concentration gradient is irrelevant The process requires energy in the
move down the concentration gradient with
form of ATP and is an active process. It is not considered active transport.
no usage of ATP.
1. Simpl_e.DJff_usion_ ✓ (Substances involved: non~polar molecules & pqja[water molecules) BUT
Simple diffusion is the movement of non-polar molecules~small polar water Transport proteins are needed as ions or polar
molecules directly through the membrane, down its ,,c~entration gradient, molecules cannot diffuse through hydrophobic
without the assistance of any transport proteins. "~V
It does not require ATP. v~ core of plasma membrane.
Two types of transport proteins
Diffusion of the particles will continue unti! ~~icles are evenly distributed (Fig.12)
such that there is no net movement of~les in any direction. (Dynamic {i) channel proteins and;
Equilibrium) ~(}
Each type of molecule moves down i~~ concentration gradient, independent of
(ii) carrier proteins 'S.,~ C""1orptgt,,lo
e--Sol•IO-
Fig.12. Transport proteins
other concentration gradients. \'{.U - Each transport protein is specific for a,~!ar (ti)

solute ; sW>\'<' N''

- e.g. 02 diffuses from the lung~\he blood while at the same time CO 2 diffuses
Q
in the opposite direction. {i) ·Channel·Protein ---l-l1dtl'tlPYI~
"''~ ~ _6. .rpe.aflv
~"tµMe-4
Factors a~~~~~!µ~~e _rat~ of si~~~sion ~ ul.1Pit1fv' Transmembrane protein G
a. ,·Molecular SIZO • 0"' i.. ~J-tltru!i<f \"1"1h qr It provides a hydrophi~ic~ ..through which only a particular ion or polar/charged
molecule can diffuse re~h~oughfrom one side of the membrane to the other.
- The smaller th~cle, the faster it will diffuse. (Less drag) ffi olllR/ rt..1-i~ctwrttVVl
e.g. water channel ~ins (aquaporins) found in the cells lining collecting ducts in
b. So10bitttjflifl~i11_@1ayer ~~~ kidney ➔ Allow ~Q-;olecu!es to flow very quickly from one side of the membrane
- Since t~fri)rnbrane is essentially non-polar, non-polar substances move Jtiy~f1V!,rloi~ to the other st~"\vater intake can be greater than if it is by simple diffusion.
throug~ membrane faster compared to polar substances. 1• " ,A,..P,. Some channe1{iroteins may be gated. Gated channels can close to prevent access
c. ·corn::entration.gradienb "l~h"'•=• C>JAMt to the hydrophilic pore but will open with the arrival of a chemical or electrical
stimulus.
The steeper the concentration gradient, the faster the rate of diffusion.
(ii) Carrier' Pl"Otein
d. Kinetic energ9"of molecules1
Usually a transmembrane protein
t temperature, t kinetic energy of molecules, therefore t rate of diffusion of
these molecules Exists in two alternate conformations. (Fig.13)
t temperature ➔ phospholipids gain kinetic energy and membrane becomes The hydrophilic interior of the carrier protein contains a binding site (not 'active site')
highly fluid ➔ formation of more transient pores ➔ t rate of diffusion for its solute and is exposed to one side of the membrane.

Too high temperatures however affects the integrity of the membrane and results a conformation change in the protein occurs when the solute binds to its binding site
In the loss of selectivity. --- solute is now exposed to the other side of the membrane where it is released
direction of flow depends on the relative concentrations of the solutes across the
membrane (bidirectional)

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transport proteins can take up the polar molecules/Jons from either side of the
membrane as they diffuse from a region of high concentration to low concentration Q. Draw in the graph below the@1mpie d1ffus1on\of a small non~polar molecule across a
membrane.
transport depends on chance collision between transport protein and solutes.
t number of carriers will result int rate of facilitated diffusion Rate of uptake/I
moldm-3S·1
Higher t :; : Lower concentration
f ti - ~-hhii-Oih1tlilM
-concentration
Q o,- ••• :z: ••• ~
Oilfusion through
tfte!lpidlaf!!r ~ f
~ f v-• ►o -"'1Cll«ttmt1!'n ~n~,a,n-;,
o ,;:i,
:J
o
J!;
0
~
"'.
~
t5
l.ipid-aoll.lblem-olecu!e-s
$U<;hMOiMdCO;i
dlfft.1$(1 ~I~ thl(IV!lh
the plasma ,ra1mbfaM.
-l'lo- cl-- <ttlntfw+ ~ws r
,,
c
o
~~---
Q,~
6j·,,·: .
Oill'u$ioei-lhrough
·•o ern,mnel~
CHANNEL PROTEIN
Has a hydrophilic pore through which
Concentration difference across the membrane/mol dm-a

Q. Draw in the graph below the jfac1htated diffusion\ of a hydrophilic molecule across a
Q. C ~ lUQlecrlles. diffuse: --+ a specific. solute (or "~ter
Serna polar 11ml i::t13rged
"'" for membrane. Assume the concentration on the other side of the membrane is kept low.
0 Q R (, ttmn,gh protein <:hunn& aquaponn) can pass
fJ
Q'., 0
O
i::
~
§
Q
that $p,.1nlho:1
mecnbrnne.Waler .,r..,,
~ ==--"'""" r,>tt
0

0
.,. . ~_
•'Ii--~~•··
0
QI

-:;; ··
i;:;

t
fa a fype&l example.

Fal:ll!bted
transport
CARRIER
To~tra
r.o'
~,

El~
~te1n alternates between
Rate of uptakeJI
moldm-as-1
--· .

~G
o'
~limtf!Sl"'t"
l'>v1m ""' /;) wse,)

8 two ations, moving a solute ,:;j

~
~*
0 0 0
~ -r,,,· C8rtilln.me4Elcvle$blnd emembraneastheshapeofthe
0
o . · _. ":'; !~~:;!::::P'!. -+ · changes. The protein~
"! -'-. · · ". 1t1at1ransp,:,11s100 sport the solute in either direction,
v
0
O ~, ?.•. moleclllQe;:ierosstM ~ 1 t thene movementbein.g own e
~..,,, concentration of the solute
~'Ct
c, o
0
~
,
' .,;.
,.,
"\, .. ~ ..
m~btana.Glueoji'
m,,ei.111 llflleis ce s ~ V
-,..Q 1tllsmelhod, ~~ Fig.13. !!A'
Concentration diff~"'\~oss the membranelmol dnr3
o 'I o B.__________;_ - ~-bmb.psu.edu/courseslbisci004alcelfslcellstruc.htm
Q. Explain the shape of the facilitated di~"graph
3. _OslTI0Sis i' (Substances lnvolvect"'gi
(Refer to ~~tes on Wat~~ P~1)
, ~ •~•¥ IY!~~~~/il$1Y10ie#'ire/M"'1l~
• The movement of W\_fujjmolecules from a region of higher water potential ('Pw) to a
>?--w,,,~cw~ 1~ ~ '1- "'tw,m wlin e,,mlff r-otem
region of lower ~~otential through a selectively penneable membrane 'i<'\11'1•rtT"'1 !"'Yb.,,:,;,~ ~\lt/irt\._,.,, MUI-C wl,e,v, 1\1.L i\je, [bl~+e.,

Can be s·~m
i.'Vitrusion whereby_ water molecules diffuse directly across the
\,t;,,cl"4 <l\t'e.! ~@f''i,jim,,,- ~roto,YS are. 1~ ~,e,,
membrane gh the transient pores or facilitated diffusion through the • 1'¼!\t~tell i ~ Di""IM~ 8'titlmt'VYI );/()~1M do a.,,,"fm,v
aquaporin "oteins. ~twv, e;-·

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4. "Active Transport: (Substances Involved: polar or charged molecules & ions)
,jli% pl17C,,Z f ACVV,, itil11Sfi1i'i-
Active transport is the transport of polar molecules or ions across a membrane
against a concentration gradient with the expenditure of ATP.
5. BulkTransp_ort (Substances Involved: macromolecules).

It involves carrier proteins. These carrier proteins may also be referred to as Bulk transport is an active process as ATP is used to mobilize the movement of the
'pumps'. membranes. ~/f-~!'l~t ~ C1f1tlVI ,t.u1}) f',J(2hii/gyj;li"l€/
Movement is of substances is in{one d1recbon) only (unlike facilitated diffusion which lt is not considered active /ansport as it is different from active transport which
can be bidirectional). involves a change in conformation of a carrier protein on the membrane.

An example of a carrier protein that carries out active transport is the sodium- . - ~[;\It fflllllP"'t ➔ CU/J"l))/f W'IC· ,fy(A/i(/e,,if-
potassium pump. (l!)1,wi,r "''"''~~, "1Jt"'1 f""VY\'j') . (a) Endocytosis
uptake of substances into the cell/organelle

-
The pump oscillates between two infolding or extension of the cell surface membrane to form a vesicle, allows the
conformational states in one pumping cell to acquire macromolecules and particulate matter.
cycle.
It trans!ocates 3 Na"' out of the cell for
every 2 ~ pumped into the cell. There are 3 types of endocytosis in animal cells

~~t7~~: AD'p> ATP powers ~ changes in

(i) Phagocytosis

•
0Cytop1ttmc:Na~blni:r,io- 8 N11,• 1>tnd'"9 sUmuUltm; conformation ..,tw]p.!!_osphory!ating the = "Cell eating~
t11ira0dlum,potnulum pljmp.. pllo:sphcnylotl0fl by AT;>.
transport prot~'b..J-

t Steps
~
~.;:j,
material taken up is in solid (Insoluble) form
e.g. white blood cells engulfing bacteria by
phagocytosis
1. ~~plasmic Na" bind to sodium~
.,.{'\,,.,1p§tassium pump (Na/K) w~°"
~'Binding of Na" stimulates
Process: ~
'S.,,fo. phosphorylation by ATP 1. filaments in the cytoskeleton are r e ~ d to help form pseudopodia (With the
Iii ~ 3. Phosphorylation causes
utilisation of ATP) ~~, -
(J 11:• Is l'OIAood llnd Nr conformational change in protein 2. pseudopodia are the outward sions of the membrane which wraps around
$llcs a~ roca,ptlw flgllln:
ll>l:',,;,ycle,opc:11t$. expelling Na" to the outside and engulf the particle G
4. 2 extracellular K" binds the protein and 3. the ends of the pseudo~~/ extension of cell membrane fuse and a vesicle/
trigger release of phosphate group vacuole containing ~eeitd matter is oinched off and moves into the cytoplasm
5. Protein returns to original conformation
releasing K" inside the cell
:;;::;.
(ii) Pinocytosis ~Q
6. Na" sites become receptive again
="Celldf!~"
material ta'ken up is in liquid (soluble) form
(non~specific transport)

-~·.,·._',
•.·•.~•
0 LoG!I ol tha pl>osphalo () Exlrl'CeHutm- IC' bl'nd& a small area of the plasma membrane ,:-.··
..'; ....·
n,i:t,,m,s 1h11 protDln's le, !ho ~ro1'11n, triggering ', '
o,lg1nal CO~lflrn\aUcn.
invaginates to form tiny vesicles within the cell
n!lMISlt ol the pll<)$ptmto
Fig. 14. g:roup. e.g. human egg cell takes up nutrients from
surrounding follicle cells by pinocytosis.

Q. What happens after a cell engulfs a food particle and forms a food vacuole?
• h I~-€/ ,m\'.<Mm~ ~l'ol~l\'1; l)\,1"fl)11l/i\tlu w,\½ Will/ VC,Wl)"\e- hl/ll>I +\1el
CV\'l<\Wi ~ vv\l\ "l~Y01~'ll!- 1vie1 !'OlimloJ m901u~e, ~ctutii.
• U!!,1'\il yY<Jt>l\lel! ~Ye/ ~-,,.~ ,Vlltl tt}e, Ufl"Pllllr'h
U • ~ ~--owe•~I\ Wtih\'(\ ~½!I VPlUA~e) U,\'\ 16€1 vei"<le, ... i\\Ef"' ~ I
w\€Cl\\,\W, \Al\ n ~ t i ;

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Additional information
(iii) Receptor-mediated endocytosis ~ - - - - - - - - -0 - - - : , - - - - -0O -::---:,------:;::::ie----- Extracellular

_,.,
:;~;
o o o o O;J O'-
O
environment
Specific transport 0

Protein receptors are embedded in membranes that are exposed to the extracellular
fluid I.~:~ ·?-. '~ Cytoplasm

Extracellular substances that bind to the receptors are ca!led ligands

lnvagination of the membrane occurs to form vesicles containing the ligand-receptor
complexes which are then transported within the ceJVorganelle
The receptor proteins are usually clustered in regions of the membrane cal!ed coated
~-~- ~~rtveslcie moves
& plasma membrane
Vesicle and cell
membrane fuse
Contents of vesicle
released outside of cen

pits (a fuzzy layer of protein on the cytoplasmic side in electron micrograph below) (b} Exocytosis

Coat proteins e.g. clathrin, probably helped to deepen the pit to form vesicles
Q. What is ATP used for in bulk transport?
Helps cell to acquire large quantities of specific substances even though they may not
be in very high concentration in the extracellular fluid. • li'f\e.m,,, ii,vnir"II> 1o 1,1«,\ ~ reatra11<1)el'il<e.&1t1'-t)<t/e,-to111 1'1tt1Y1€<'/
"'1ltf<l'flil:ittk&
• a-, {1S i<) l'llJMl> ~'1'1 ~bn:!fie.\t t\"'W,,J
i1'Jv"1~ iD fum i\1t,, Ye,\'j;\i:J
e.g. Iron transported in the blood is f\V\,\ rvrwe, ill1" vf8role& ,('.
complexed to a protein called transferrin.
Cells have receptors for transferrin
• ftTf ~ ~\d'll VEJlUtlEiitt'r-fl'Ji!J MVNoi\\vitfm-J or M~&ttm ltf-AJ,"11!8')1'1i!lmne,
(complexed with iron) on their surface.
"SJ"'
When these receptors encounter a
mo!ecule oftransferrin, they bind tightly to I(F) Links . '!:;::."' I
it. The complex oftransferrin and its
receptor is then engulfed by endocytosis.
The topic of cell membranes is relevant to the following top#';,;A level Biology syllabus
Ultimately, the Iron is released into the
cytosol.
. K -----
Torie Comments .(\.-
Microscope image of cell
undergoing endocytos!s.
Cell structure Membranous organelles ~~~"roclude nucleus, endoplasmic reticulum,
A. The cell membrane begins
to sink in. I golqi annaratus & lvsoso .
B.The membrane is attempting
to envelop the material. Cell signalling Receptors on cell m~\';anes are important for ligand recognition and
C.The material has been bind[na so that si,..r,BJ an be transduced into the cell.
captured inside of a capsule
of eel! membrane. Enveloped Mode of en~ry~fi~st cell and release.
D.Endocytosis is complete. viruses
Photosynthesis To~:_,~~fendent reactions of photosynthesis occur on the thylakoid
me me of the chlororlast
(b)Exocytosis fl): Res'"'iration n~ve nhosohonilation occurs on the inner mitochondrial membrane.
Exocytosis ⇒ Sec&fon of macromolecules (waste materials, undigested remains or useful u
products) by the fusion of vesicles with the plasma membrane.
Key words include:
Process: active transport hydrophol)ic core (of phospholipid bilayer)
A transport vesicle budded from the Golgi apparatus moves to the cell surface I carrier proteins phagocytosis
plasma membrane.
channel proteins phospholipid bilayer
Where the membrane of the vesicle fuses with the eel! surface membrane to release endocytosis pinocytosls
contents of the vesicle to the extracellular environment
exocytosis plasma membrane / cell surface membrane
Often used for the export of manufactured products
facilitated diffusion pseudopodia
e.g. Insulin is manufactured in the pancreas and secreted directly into blood by
fl.uid mosaic model water potential
exocytosis.
hydrocarbon tail
e.g. AcetylchoHne in synaptic vesicles is released by exocytosis into the synaptic cleft
so that the neurotransmitter can bind to the receptor site on the post-synaptic hydrophilic pore {of channel protein)
membrane.

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CORE IDEA
(2) Genetics and Inheritance

MITOSIS & MEIOSIS

Content
• Replication and division of nuclei and cells
• Understanding of chromosome number and variation
• Effect of meiosis on chromosome number and variation

Learning Outcomes
2 (I) Explain what is meant by the terms gene mutation and chromoSOn;J~ aberration.
For gene mutation, knowledge of how substitution, addition an(;j''t\leifetion could change
the amino acid sequence (e.g. frameshift) is required. ..·. ()"'• •
- to be covered in DNA & Genomics. • "'(f ··
,{~>::, .
For chromosomal aberration, knowledge of numeric,@h,/~,g,. aneuploidy, as in the case of
trisomy 21, i.e. Down syndrome) and structural (~.g'.{franslocation, duplication, inversion,
deletion) aberration is required. §Z:. {i"
i;f
J~~->
/0:\

(n) Describe the events that occur during the Q1i(9tic cell cycle and the main stages of
mitosis (including the behaviour of chrgmqibrfles, nuclear envelope, cell membrane and
\ . ' ' 1/> tj y>
centrioles). \"~•·'
'"'
·•.~ \''
(o) Explain the significance of the m}tdtic'c~II cycle (including growth, repair and asexual
reproduction) and the need toJeiaulate it tiahtlv. (Knowledge that dysregulation of
checkpoints of cell divisio(i;;,a1:fresult in uncontrolled cell division and cancer is
required, but detail of th1.,P1eit:hanism is not required.)

(s) Describe the event~ft\¥f>~;cur during the meiotic cell cycle and the main stages of
meiosis (including'lf'\l'i'behaviour of chromosomes, nuclear envelope, cell membrane
and centriole~}l~~a'mes of the main stages are expected, but not the sub-divisions of
prophase.) r{(I
~c--,/?
(t) Explain the significance of the meiotic cell cycle (including how meiosis and random
fertilisation can lead to variation).

References
• Campbell, N.A. and Reece, J.B. (2014). Biology, 10th edition. Pearson.
• Jones & Jones. (1997). Advanced Biology.
• Hoh Yin Kiong (2003). Longman A-Level Course in Biology, Vol. 1. Longman
• Green, Stout and Soper (1990). Biological Sciences, Vol 1. Cambridge
• Raven, Johnson, Loses, Mason & Singer (2008). Biology, 8th edition. McGraw-Hill.

* This handout is the effort of several Biology teachers at RI. It has been and will
continue to be updated.
•• Any information given in a double-lined box is for your information only.

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Table of Contents

(A) Cell division ............................................................. 3

(B) Chromosome structure ............................................................. 3
(C) Diploid and haploid ............................................................. 5
(D) Homologous chromosomes ............................................................. 7
(E) Factors affecting cell ............................................................. 9
division
(F) The cell cycle ............................................................. 10
(G) Inter phase ............................................................. 11
(H) Mitosis ............................................................. 11
(I) Cytokinesis ............................................................. 16
(J) Significance of mitosis ............................................................. 18
(K) Uncontrolled cell division ............................................................. 20
(L) Meiosis ............................................................. 21
(M) Significance of meiosis 29
(N) Differences between mitosis 32
and meiosis
(0) Mutations - Chromosomal 34
mutations
(P) Glossary 41
(Q) Links 41

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