SEMESTER 1

CHAPTER
Biological (a) describe the chemical properties (solvent, bond angles and hydrogen bond)
Molecules of water and relate its physiological roles in the organisms;

1.1 Water (b) describe the physical properties (polarity, cohesiveness, density, surface
tension, specific heat capacity, and latent heat of vaporisation) of water and
relate its physiological roles in organisms.

1.2 (a) classify carbohydrates into monosaccharide, disaccharide and polysaccharide

Carbohydrates with respect to their physical and chemical properties;

(b) classify monosaccharide according to the number of carbon atoms and the
functional groups (i) triose e.g. glyceraldehydes, (ii) pentose e.g. ribose and
deoxyribose, (iii) hexose e.g. glucose and fructose,

(c) illustrate the molecular structure of a monosaccharide and differentiate

between the reducing and non-reducing ends;

(d) describe the formation of glycosidic bond in disaccharides (maltose and

sucrose) and polysaccharides (starch, glycogen and cellulose);

(e) relate the structure of disaccharides and polysaccharides to their functions in

living organisms.

1.3 Lipids (a) describe the structures, properties and distribution of triglycerides,
phospholipids (lecithin) and steroid (cholesterol);

(b) state the functions of triglycerides, phospholipids (lecithin) and steroids

(cholesterol);

(c) differentiate between saturated and unsaturated fatty acids.

1.4 Proteins (a) classify amino acids into four main classes based on their side chains: polar,
non-polar, acidic and basic;

(b) describe the structure of an amino acid and the formation of peptide bonds
in polypeptides;

(c) explain the properties of protein (amphoteric, isoelectric point, buffer and
colloid);

(d) differentiate the various levels of organisation of protein structure (primary,

secondary, tertiary and quaternary) and relate the functions of each structure to
the organisation of proteins;

(e) explain the denaturation and renaturation of protein; (f) classify proteins
 according to their structures, compositions (simple and conjugated) and
functions.

1.5 Nucleic (a) describe the structures of nucleotides and the formation of phosphodiester
acids bonds in a polynucleotide;

(b) distinguish between DNA and RNA and the three types of RNAs (mRNA, tRNA
and rRNA);

(c) describe the structure of DNA based on Watson and Crick model.

1.6 Analytical (a) describe the basic principles of paper chromatography in pigment separation,
techniques electrophoresis for protein and nucleic acid separation.

2 Structure of (a) state the cell theory;

Cells and
Organelles (b) compare the structures of prokaryotic and eukaryotic cells;

2.1 Prokaryotic (c) compare typical animal and plant cells as seen under electron microscopes;
and eukaryotic
cells (d) describe the basic principles of light and electron microscopy

2.2 Cellular (a) identify the cellular components of typical plant and animal cells;
components
(b) describe the structures of organelles and state their functions;

(c) explain the basic principles of differential centrifugation used to fractionate

cellular components (g and S values).

2.3 Specialised (a) outline the structures, functions and distributions of unspecialised cells
cells found in plants (meristematic cells);

(b) describe the structures, functions and distributions of specialised plant cells
found in epidermal, ground and vascular tissue;

(c) describe the structures, functions and distributions of specialised animal cells
found in connective, nervous, muscular and epithelial tissues, including the
formation of endocrine and exocrine glands.

3 Membrane (a) describe the structure of a membrane based on Singer-Nicolson fluid mosaic
Structure and model;
Transport
(b) explain the roles of each component of the membrane.
3.1 Fluid
mosaic model

3.2 Movement (a) explain the processes of passive and active transports, endocytosis and
of substance exocytosis;
across
membrane (b) explain the concepts of water potential, solute potential and pressure
potential;

(c) calculate the water potential of a plant cell in a solution.

Enzymes (a) explain that enzyme is a globular protein which catalyses a metabolic
reaction;
4.1 Catalysis
and activation (b) explain the mode of action of enzymes at active site involving enzyme-
energy substrate complex and lowering of the activation energy and enzyme specificity

4.2 (a) illustrate enzyme specificity using induced fit (Koshland) and lock and key
Mechanism of (Fischer) models;
action and
kinetics (b) explain the time course of an enzyme-catalysed reaction by measuring the
rate of formation of product(s) or rate of disappearance of substrate(s) as the
rate of reaction;

(c) deduce the Michaelis-Menten constant (Km) from the Michaelis-Menten and
Lineweaver-Burk plots;

(d) explain the significance of Km and Vmax;

(e) explain the effects of temperature, pH, enzyme concentration and substrate
concentration on the rate of an enzyme-catalysed reaction.

4.3 Cofactors (a) explain the roles of cofactors (ion activators, coenzymes and prosthetic
groups) in an enzymatic reaction;

(b) explain the importance of vitamins and minerals as precursors of

coenzymes/cofactors.

4.4 Inhibitors (a) explain the effects of competitive and non-competitive inhibitions on the rate
of enzyme activity of reversible inhibition;

(b) relate the Lineweaver-Burk plot to the effect of inhibition on Km and Vmax
values.

4.5 (a) describe enzyme classification according to International Union of

Classification Biochemistry (IUB) e.g. oxidoreductase, transferase, hydrolase, lyase, isomerase
of enzymes and ligase.

4.6 Enzyme (a) explain the importance and the main techniques of enzyme immobilisation
technology namely adsorption, entrapment and covalent coupling;

(b) explain the application of enzyme immobilisation in the development of

biosensors.

5 Cellular (a) outline the importance of energy and respiration in living organisms;
Respiration
 (b) describe the structure of the energy carriers such as ATP, NADH and FADH2.
5.1 The need
for energy in
living
5.2 Aerobic (a) describe the various stages of aerobic respiration and its location in the cells;
respiration
(b) describe glycolysis, and calculate the net energy produced in glycolysis;

(c) describe the various steps involved in the Krebs cycle (including the link
reaction);

(d) explain the formation of NADH, FADH2, GTP and ATP during the Krebs cycle;

(e) describe oxidative phosphorylation and chemiosmosis in the electron

transport system;

(f) explain the role of NADH, FADH2 and ATP synthase in the electron transport
chain;

(g) calculate and explain the net energy produced in aerobic respiration per
molecule of glucose in liver and muscle cells;

(h) describe the effects of cyanide and carbon monoxide on respiration;

(i) explain how lipid and protein act as alternative energy sources.

5.3 Anaerobic (a) explain the anaerobic respiration in yeast and muscle cells;
respiration
(b) describe the applications of anaerobic respiration in food industries (bread,
tapai and yogurt).

6 (a) classify autotroph into photoautotroph and chemoautotroph;

Photosynthesis
(b) describe photosynthetic pigments;
6.1 Autotroph
(c) explain the absorption spectrum and action spectrum of photosynthetic
pigments.

6.2 Light- (a) explain photoactivation of chlorophyll a resulting in photolysis of water;

dependent
reactions (b) explain the cyclic and non-cyclic photophosphorylation including electron
transport system resulting in the production of ATP and NADPH.

6.3 Light- (a) describe Calvin cycle;

independent
reactions (b) explain photorespiration;

(c) describe the anatomical structure of C4 leaf (Krantz anatomy) in comparison

 to C3 leaf;

(d) explain carbon dioxide fixation in C4 plants and Crassulacean Acid

Metabolism (CAM) plants;

(e) differentiate the metabolism of C3, C4 and CAM plants.

6.4 Limiting (a) explain limiting factors of photosynthesis (light intensity, carbon dioxide
factors concentration and temperature);
(b) relate the roles of C3, C4 and CAM plants on the increasing carbon dioxide
emission and global warming.