Biological Molecules

Monomers and Polymers

 Organic compound- mostly made up of
carbon (+ oxygen, hydrogen and
nitrogen)

Polymers- 
 Can be homogeneous or heterogeneous
( made up of the same monomers or
made up of varying monomers e.g.
sucrose= glucose+fructose

Monomer- Examples include: monosaccharides, amino acids and nucleotides

Biological Monomer Polymer
molecule

Protein Amino Acids Polypeptide

Lipid Fatty Acid, Lipid

Glycerol 

Nucleic acids Nucleotide Nucleic

Acid

Repeating smaller units which produce polymers

Condensation reaction-
 Monomers join to make polymers
 REMOVES WATER which forms a covalent bond (so loss of 2xH and 1xO)

Hydrolysis reaction- 
 Addition of a water molecule ( so gives 2xH and 1xO)

Carbohydrates

 Simple sugars: monosaccharide, disaccharides

When x= y it's simple so Cx(H20)y 
 They join to make polymers called complex carbohydrates 
When x does not = y it's simple so Cx(H20)y 

Monosaccharide are organic: C, H,O (E.g. glucose, fructose and galactose)

5= pentose (Ribose, deoxyribose) , 6= hexose (glucose and fructose)  3= triose
Glucose-
 Used in respiration 
 Optical isomers: similar chemical formulas but different structural due to variation in atom
arrangement.
Examples of monosaccharides:
 Formula of a monosaccharide : (CH₂O)n - where n is between 3 and 7

Fructose sweeter- 4 ring carbon - more compact- fits better in taste bud- greater sense of taste

Disaccharides:
 Can Be homogenous or heterogeneous 
 Made via condensation reaction forming a covalent bond called a glycosidic bond

Maltose: 2 alpha glucose                                                                     Disaccharides formation

Formation of polysaccharides:
 Condensation of many glucose units 
 Glycosidic bonds and loss of water

Amylose- Alpha glucose

Polysaccharides 

Starch- 
 Store excess glucose IN PLANTS
 Insoluble so prevents osmotic effects of swelling or bursting cells
 Amylose: compact storage- unrbances - coiled helical structure so cylindrical (highly
branched per 20 sub units)
 Amylopectin: fast breakdown: it is a long chain with branches extending outwards:
glycosidic bonds are much more readily available to enzymes to break down branches to

release glucose for respiration

Explain how the properties of starch are related to its role in living organisms 
 role - storage;
 properties - insoluble;
 explanation - therefore stays inside cell/membrane;
 properties - large molecule/coiled/branched;
 explanation - lots of glucose/carbohydrate molecules in small space/stays inside cell;
 properties - osmotically inactive;
 explanation - does not cause the cell to absorb water;

Glycogen- 
 Key energy store for ANIMAL
 Made of alpha glucose
 Store in liver or muscle cells
 Glucose used in respiration to obtain energy 
 Adapted to storage and fast breakdown 
 More branches so easily broken down, glycosidic bonds are much more readily available to
enzymes to break down branches to release glucose for respiration
Cellulose- 
 Cell walls
 B- glucose: glycosidic bonds -- for microfibers -- makes cell walls strong 
Adaption:
Made up of β-glucose
 So form long straight, unbranched chains that run parallel to each other and are cross
linked by hydrogen bonds
 Adds collective strength
              Grouped to form microfibrils
 Which in turn are grouped to form fibres
 Provides more strength
 Water permeable as small gaps 
 Insoluble- osmotically inert
Describe the structure of a cellulose molecule and explain how cellulose is adapted for its
function in cells.
1. Made from β-glucose;
2. Joined by condensation/removing molecule of water/glycosidic bond;
3. 1: 4 link specified or described;
4. “Flipping over” of alternate molecules;
5. Hydrogen bonds linking chains/long straight chains;
6. Cellulose makes cell walls strong/cellulose fibres are strong;
7. Can resist turgor pressure/osmotic pressure/pulling forces;
8. Bond difficult to break;
9. resists digestion/action of microorganisms/enzymes;

Glycogen vs amylopectin
 Both made of branches but Glycogen has more branches

Two ways in which the structure of cellulose is different from the structure of starch. 
Starch
1. (1,4 and) 1,6 bonds/contains 1,6 bonds /branching 
2. All glucoses/ monomers same way up 
3. Helix/coiled/compact 
4. Alpha glucose 
5. No (micro/macro) fibrils/fibres 

Cellulose 
1. 1,4 bonds / no 1,6 bonds / unbranched / straight; 
2. Alternate glucoses/monomers upside down; 
3. Straight; 
4. Beta glucose; 
5. Micro/macro fibrils/fibres; 

Explain how cellulose gives cotton its strength.

 (long) straight/unbranched chains;
 (idea of more than 1) chains lie side by side / form (micro)fibrils;
 idea of H bonds holding chains together;

Explain how a change in the primary structure of a globular protein may result in a different
three-dimensional structure.
 sequence of amino acids changes;
 tertiary structure changes/folds in a different way;
  bonds form in different places;

Reducing sugars- 
 Acts as reducing agent → donates electrons 
 Most disaccharides e.g sucrose

Test: Benedict's test  

1. Add benedict’s reagent (blue) to food sample.
2. Heat in a boiling water bath.
3. Positive = green / yellow / orange / red precipitate (reducing sugar present).
 If negative result (Benedict's reagent doesn’t change colour) to Benedict’s
test for reducing sugars, perform this test to see if non- reducing sugars are
present instead...
Benedict’s test for non-reducing sugars:
Add an equal volume of sample and dilute hydrochloric acid to hydrolyse the sugar.
1. Heat in a boiling water bath.
2. Neutralise with sodium bicarbonate.
3. Carry out normal benedict’s test.
4. Non-reducing sugar present = green / yellow / orange / red precipitate.

DETERMINING GLUCOSE CONCENTRATION

1. Produce a dilution series of glucose solutions of known concentrations.
2. Perform a Benedict’s test on each sample (use same amount of solution for each test) and
remove any precipitate (e.g. by centrifuging).
3. Using a colorimeter, measure the absorbance of each sample to establish a calibration curve.
4. Repeat with unknown sample and compare the absorbance to the calibration curve to
determine glucose concentration.

Test for Starch- 

1. Add iodine dissolved in potassium iodide solution and shake/stir.
2. Blue-black colour = starch present.

Disadvantages of Beneditcs- 
 Not sensitive at low concentrations as it falls out of the sensitive range of the calibration
curve
 Does Not distinguish between non reducing  sugars- not specific

How to take away these disadvantages- 

 Enzyme will give bon sensitivity and specificity 

Lipids
Organic molecule (lots of H andO )
 Contain fatty acids which contain hydrocarbon chains
Glycerol- 
 Alcohol because of it presne of OH groups in its structure 

Fatty acids-
 Contain carboxyl group and fatty acid

chain 
 Insoluble in water
 R groups can be saturated or unsaturated 

Saturated- no double bonds between adjacent atoms

Unsaturated- double bond is present between adjacent carbon atoms - more bends- less compact-
lower bp

Reaction for Triglycerides:

ESTER Bond between an OH from the glycerol and the H from the fatty acids 

Triglycerides- 

 Energy store
 Store twice as much energy than carbohydrates
Phospholipids
Phospholipids are apathetic
 Have a hydrophobic tail and a
hydrophilic head
 Its polar
Forms
 In cell membranes
 Phospholipid bilayer
 Cells have an aqueous solution outside (extracellular fluid)  and inside (cytoplasm) so the
hydrophilic heads will face the extracellular fluid and cytoplasm and hydrophobic tails will
face inwards so a bilayer is formed.
Why does the sample when testing for lipids turn cloudy?
 The cloudy colour is due to any lipid in the sample being finely dispersed in the water to form
an emulsion. Light passing through this emulsions is refracted as it passes from oil droplets to
water droplets, making it appear cloudy

Test for lipids

Proteins- 
 20 amino acids- different R groups( know as a side chain )
 Peptide bonds- water is released
  The polypeptide chain means its final structure is tertiary structure
 3D shape
 Zwitterion- amino acid at neutral charge
 Amino acids can act as a buffer → cooh
accepts  H- Becomes uncharged→ Amino
group gives an H and becomes charged→
proton donor

Protein test-
 Using the Biuret test:
1. Place the test sample in a test
tube and add an equal
volume of NaOH at room
temperature
2. Add a few drops of very
dilute copper (II) sulphate
solution and mix gently

Roles of protein- 
 Enzyme-3D tertiary structured globular proteins (metabolic reactions) that act as catalysts to
alter the rate of a chemical reaction without undergoing permanent changes themselves/ They
lower the activation energy of the reaction it catalyses and finds an alternate reaction
pathway/In this way, enzymes allow reactions to take place at a lower temperature than
normal, enabling some metabolic processes to occur rapidly at the human body temperature
 Antibody
 Transport proteins
 Structure: keratin hair, collagen in cartilage

Peptide bond-
From the condensation of amino acids with the removal of a water molecule
 The water is made by combining an --OH from the carboxyl group of one amino acid with an
--H from the amino group of another
 The two amino acids then become linked by a peptide bond between the carbon atom of one
amino acid and the nitrogen atom of the other
Because it determines the protein's ultimate shape and hence its function
 A change in just a single amino acid in the sequence can lead to a change in the shape of the
protein, which is very specific to its function, and so it may cause the protein to function less
well or differently

What determines the arrangement of the active site?

 The hydrogen and ionic bonds between --NH2 and --COOH groups of the polypeptides that
make up the enzyme

Describe the structure of an amino acid molecule and explain how amino acids link together. 
1. Amino acid based on carbon with four groups attached;
2. Amino/ NH2 and carboxyl / COOH;
3. R-group/ side chain + hydrogen;
4. R-group differs from one amino acid to another;
 5. Amino acids joined by condensation;
6. Bond formed between NH2 and COOH;
7. Involves removal of molecule of water;
8. H from NH2 and OH from COOH;

Explain how the structure of fibrous proteins is related to their functions.

 Long chains of aa;
 Folding of chain into a coil / folds / helix / pleated sheet;
 Association of several polypeptide chains together;
 Formation of fibres / sheets explained; 2
 H bonds / Disulphide bonding (In context);
 Fibres provide strength (and flexibility);
 Sheets provide flexibility;
 Example e.g. keratin in hair, collagen in bone; (MUST be in context)
 Insoluble because external R-groups are non-polar;

Structure:

Structure: Description Bonds- 

- 

Primary -

Secondary -

Tertiary -

Quaternary -

Two types of proteins-  Effects of events on protein structure:

Change Impact Bond broken

Temperature

PH
DNA and RNA
 DNA: Stores genetic information 
 RNA: Passing genetic information from DNA to ribosomes ( by mRNA) 
 Polymers made up of nucleotides * they are nucleic acid

Ribosomes made up of 

 rRNA+ Proteins which help ribosomes make new proteins (protein synthesis)

Types of bases- 
 Purines- A, G
 Pyrimidines: T, C U

2 phosphodiester bonds made when a nucleotide joins 

 Form between the phosphate group of one nucleotide
 And pentose sugar of second one
 Sugar-phosphate backbone

DNA- 
  Made of complementary polynucleotide chain
 Antiparallel
 H bonds between competitors,entry bases
 Twist to form helix 
 -T C-G

DNA structure→ 

DNA replication→ 
1. strands separate / H-bonds break;
2. DNA helicase (involved);
3. Both strands / each strand act(s) as (a) template(s);
4. (Free) nucleotides attach;
5. Complementary / specific base pairing / AT and GC;
6. DNA polymerase joins nucleotides (on new strand);
7. H-bonds reform;
8. Semi-conservative replication / new DNA molecules contain one old strand and one
new strand;

Nelson and Stahl’s Experiment→ 

ATP- 
 Adenosine Triphosphate 
 Made in mitochondria
 Unique- 3 phosphate groups 
 Energy between phosphate groups 
Made in PS and Resp
Phosphate- 

 Added to another to make it more reactive

 Used in phosphorylation
Water- 

Give two properties of water that are important in biology. Explain the importance of each property
you identify.
1.     Any two pairs from:
1.     Polar (molecules);
2.     Dissolves charged particles/acts as a (universal) solvent;
2.     A metabolite;
3.     Involved in metabolic/cell reaction/condensation/hydrolysis;
4.     Water molecules stick together/cohesion between water molecules;
5.     6. Provides surface tension/prevents columns of water breaking;
6.      High (specific) heat capacity;
7.      Reduces fluctuations in temperature (of water bodies);
8.      High (latent) heat of evaporation;
9.     Evaporation of small amount of water cools organisms;
 
Explain why this column of water does not brea
1.     water being pulled up through its narrow xylem vessels. Water molecules are polar;
2.     Form hydrogen bonds between water molecules;
3.     Cohesion prevents breakage;
 
Explain one other effect on the plant caused by the evaporation of water from its leaves.
 
1.     Cools leaves;
2.     Evaporation uses heat from leaves;
 
Explain the meaning of the terms hydrophilic and hydrophobic.
1.     Hydrophilic – will mix with/dissolve in water;
2.     Hydrophobic – will not mix with/dissolve in water;
 
Give one example of a hydrophilic substance and one example of a
hydrophobic substance.
1.    Hydrophilic – any named ion, any named gas (eg, oxygen, carbon dioxide), amino acid,
glucose, sucrose, etc;
2.    Hydrophobic – eg lipid;
 
Organisms that live on land usually experience greater ranges of environmental  temperature than do
organisms that live in water. Explain why.
1.     Water has higher (specific) heat capacity than air;
2.     So more heat is need to raise the temperature of water (than air);
 
Suggest why water becomes lighter as it expands.
1.     Density = mass ÷ volume;
2.     Ice has same mass of water but greater volume;
 
Suggest why water becomes lighter as it expands.
1.     Ice is colder than water;
2.     (Being lighter than water) ice floats on water;
3.     Reduces freezing of water (below ice);

Scientists looking for extra-terrestrial life are looking for planets with evidence of free water. Explain
why water is considered so important for life to occur.
1.     Life (thought to have) evolved in water;
2.     Water provides support (for bodies of organisms);
3.     Water a major component of cytoplasm;
4.     Water is a universal solvent/metabolic reactions occur in aqueous solution;
5.     Water is a metabolite/a reactant in many cell reactions;
6.     Water stabilises (external) temperature;
7.     Water important in cooling/stabilising internal temperature (of organisms);

Q: What is the advantage of metabolic reactions taking place in solution?

 Increases random movement of molecules and so increases rate of successful collisions
between reactants (link to enzyme action, section 3.1.4.2).

Q: Would you expect the water content of humans to be constant? If not, why not?
 For example, it will depend on how much water drunk recently, how much lost on sweating,
less  water first thing in the morning since water lost overnight in exhaled breath/sweating.

Teacher notes
 by acting as a temperature buffer, the temperature of bodies of water, such as ponds, lakes or
seas, do not vary as much as the air temperatures above them. This idea can be linked to the
effect of temperature on enzyme-controlled reactions and the special significance for
organisms not able to control their own temperature.
   by removing a large amount of heat when evaporating even a small amount of water,
organisms are cooled. (for example, the evaporation of sweat or the evaporation of water
vapour from the tongue of a panting dog).

Inorganic Ions
• Occur in solution in the cytoplasm and body fluids of organisms.
• Some in high concentrations and others in very low concentrations.
• Each type of ion has a specific role, depending on its properties and these roles are relevant in a
range

of topics across the A Level.

PHOSPHATE IONS – PO43-

• Attached to other molecules as a phosphate group.
• Phosphate ions form the phosphate groups of DNA/RNA nucleotides.
• Enables nucleotides to join together – phosphodiester bonds form. 
• Phosphate ions form the phosphate groups of ATP.
• Breaking the bonds between the phosphate groups in ATP releases energy. 
•Phosphates are present in the cell surface membrane

HYDROGEN IONS – H+
• Maintain pH levels in the body.
• Too much H+ = acidic (low pH).
• Too little H+ = alkaline (high pH).
• Affects rate of enzyme controlled reactions as can cause enzymes to denature. 
 Role in stomach - 
 Breakdown of proteins - low ph of gastric juices- pepsin needs acidic
 Acid killing of bacteria- low ph- sterilize food and kill bacteria

IRON IONS – Fe2+

• Component of (haem group of) haemoglobin which is contained in red blood cells.
• Transports oxygen around the body – oxygen temporarily binds to it so it becomes Fe3+.

SODIUM IONS – Na+

• Sodium and potassium irons are very important in the nervous system and communication between
neurons.
•Sodium helps molecules such as glucose and amino acid to cross the cell membrane in the process of
cotransport. Sodium and potassium irons are very important in the nervous system and
communication between neurons.

Sodium helps molecules such as glucose and amino acid to cross the cell membrane in the process of
co-transport.- Co transport of glucose and amino acids across cell membranes. E.g. digestion