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A Sam Ellis Academy Document

AQA A-LEVEL biology | 3.1 - Biological Molecules

Written by Hilary Meng & edited by Sam Ellis

in 2022
There are no copyright restrictions, you can distribute this document
freely.

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3.1 - Biological Molecules

Monomers and Polymers
There’s a few words we need to get to grips with, if you’re doing A-Level
Chemistry you’ll be happy with this already. If you’re not, don’t stress
this is easy.
• Monomers: smaller ‘units’ that larger molecules are made.
• E.g. monosaccharides, amino acids, or nucleotides.
• The ‘units’ are the single molecules that join up over and over
again

• Polymers: molecules made from a large numbers of monomers joined

together.
• E.g. starch, protein, and DNA.
• The polymers are the whole chain of hundreds, thousands, or
even hundreds of thousands of monomers

• Condensation reaction: a reaction joining 2 molecules together with

a chemical bond involving the elimination of a molecule of water.

• Hydrolysis reaction: A reaction that breaks a chemical bond between

2 molecules using a water molecule.

Carbohydrates
Monosaccharides
Monosaccharides: the monomers from which larger carbohydrates are made.
• E.g. glucose.
• glucose has 2 isomers: α-glucose and β-glucose.
- Isomers: a compound with the same chemical formulae but a different
structural arrangement.
• α-glucose and β-glucose have -H and -OH groups attached differently
to C1.

• The human body can only use α-glucose.

• This is because many chemical reactions in our bodies controlled by
enzymes.
• This is important because only one isomer of a given chemical “fits”
into the specific active site of the enzyme needed for it to react.
• In out bodies, the reactions involving glucose are catalysed by an
enzyme that only fits α-glucose into its active site.
• That’s why only one α-glucose takes part in these reactions.

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Disaccharides
Disaccharides: when 2 monosaccharides (monomers) combine through a
condensation reaction forming a single molecule (joined by a glycosidic
bond)
• Glycosidic bond: a chemical (covalent) bond formed as a result of
condensation between 2 monosaccharides.
• They often occur as the intermediate either in the breaking down or
building up of polysaccharides.
• E.g. in the alimentary canal:
POLYSACCHARIDE → DISACCHARIDE → MONOSACCHARIDE

• The 3 most commonly occurring disaccharides are maltose, sucrose and

lactose.

α-glucose + α-glucose → maltose (found in germinating seeds)

hydrolysed by maltase

α-glucose + β-galactose → lactose (found in milk)

hydrolysed by lactase

α-glucose + β-fructose → sucrose (found in sugar cane)

hydrolysed by sucrase

Maltose

α-glucose + α-glucose ⇌ maltose (+ water)

➔ NOTE: this is a condensation reaction, this means it’s reversible by

a hydrolysis reaction.

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Polysaccharides
Starch
• Starch is a Polymer of α-glucose, formed by condensation.
• It’s used for energy storage in plants
• The rate in which energy needs to be released is much slower in plants
than, for example, animals because they're stationary
• This means that branching in the polymer (Polysaccharide) is less
frequent.
• Starch is made up of 2 types of polysaccharides: amylose + amylopectin.

1) Amylose (15-30%)
• Molecules joined by α 1-4 glycosidic bonds.
• Long, unbranched polymer chain.
• α-helical structure (‘α’ as it twists clockwise)
• This makes it compact.

STORAGE FEATURES PRESENT:

• Very compact
• Insoluble so does not diffuse out of cells easily or have any effect on
pressure and therefore osmosis (osmotically inert)
• But, because it’s linear (the polymer is without branches) it will be
hydrolysed slowly.

AMYLOSE IS BROKEN DOWN BY AMYLASE (A HYDROLASE) HERE:

a. The mouth by salivary amylase, where pH is 6.5-7
b. The duodenum by pancreatic amylase, where due to bile salts pH
is 7-8

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2) Amylopectin (70-85%)
Long chains of α 1-4 glycosidic bonds, but every 20th glucose molecule is
a branch point, which is achieved using an α 1-6 glycosidic bond.

STORAGE FEATURES PRESENT:

• Easily hydrolysed - branching ∴ more ends to which enzymes can combine
so there could be simultaneous hydrolysis.
• Insoluble so it doesn’t diffuse out of cells easily or have any effect
on pressure or therefore osmosis (osmotically inert).
• However, due to branching, it is not as compact.

AMYLOPECTIN IS BROKEN DOWN BY AMYLASE IN THE SAME PLACES AS AMYLOSE.

Glycogen
• Polymer of α-glucose, formed by condensation (again!)
• Used for energy storage in animals
• The rate at which energy needs to be released (by respiration)
is high in animals as they're motile organisms
• This explains why branching is more frequent.
• Soluble in water.

- It has long chains of α 1-4 glycosidic bonds, but every 12th glucose
molecule is a branch point,
- This is achieved using an α 1-6 glycosidic bond.
- This forms an α-helix polymer.

FOLLOWING STORAGE FEATURES:

• Compact, as α 1-4 sections are shorter and there’s more α 1-6 sections.
• Easily hydrolysed - branching means there’s more “ends” that enzymes
can combine with.
• The multiple ends allows simultaneous hydrolysis to occur.

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Cellulose
• Polymer of β-glucose, formed by condensation.
• It’s found in plant cell walls
• This makes it a structural carbohydrate
• Because of its function, after it’s made, it doesn’t need to be broken
down.
• That’s why there’s no branching present

- It has long chains of β 1-4 glycosidic bonds

- Here: every other glucose molecule rotates 180° to give a straight,
rigid molecule
- This is unlike α bonds that are flexible

FOLLOWING STRUCTURAL FEATURES:

● Strong - hundreds of these chains lie side by side, linking
together by many H-bonds (although each individual H-bond is
relativity weak, a load of them together lead to strong binding
between the molecules) forming microfibrils.
● H-bonds are known as ‘cross-links’
● This gives the cell high tensile strength, to endure high osmotic
pressures without lysis.
● This also provides mechanical support.
● Insoluble so therefore osmotically inert.
● Water permeable, this because there’s reasonably sized gaps.

CELLULOSE CANNOT BE BROKEN DOWN (METABOLISED) BY ANIMALS, THEY DON’T HAVE

CELLULASE.
ONLY BACTERIA HAVE CELLULASE, AND EVEN THEN METABOLISM IS SLOW.

More on the next page

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Tests for Reducing / Non-reducing Sugars (Benedict’s Test)

• Benedict’s reagent is composed of copper(II) sulphate in alkaline
solution.
• It’s what we use to distinguish between Reducing and Non-reducing
Sugars
➜ All monosaccharides are reducing sugars
➜ This means they’re all capable of reducing copper(II) sulphate to
insoluble copper(I) oxide,
➜ copper(I) oxide is a brick red precipitate in alkaline conditions.

- Most disaccharides are also reducing sugars.

- However some disaccharides are non-reducing sugars e.g. sucrose.

• When monosaccharides combine to form disaccharides, reducing ability is

often retained.
• sometimes, though, reducing part of the molecule is hidden in the bond
(e.g. α 1-2 glycosidic bond for sucrose)
• therefore reducing ability is lost, making the new molecule a non-
reducing sugar.
• In sucrose, glucose C1 and fructose C2 does have reducing power as long
as it’s not involved in a glycosidic bond.
• This means the Benedict’s test is not appropriate without hydrolysis.

Test for Reducing Sugars

1. Take 2cm3 of Benedict’s solution
2. test solution in a test tube; mix the solutions thoroughly.
3. Place the test tube in a 90°C water bath
4. leave for 5 mins, shaking occasionally.
a. +ve result = clear blue to green ➜ red ppt. (nearer red
greater conc. of reducing sugar)
b. -ve result = remains clear blue.

Controls: experiment in which verify an experiments functionality (in

this case, food test)
CONTROLS: Known +ve: green ➜ red ppt. (e.g. glucose)
Known -ve: to remain clear blue (e.g. sucrose)

• Cu2+ combines with sulphate ions to make a blue solution.

• Therefore the more Cu2+ the bluer the solution, and the fewer the
glucose molecules within the solution.
• Cu+ combines with other reagents within the Benedict’s solution to form
insoluble, red, copper oxide.
• The more Cu+ the paler the solution, and the more glucose molecules w/
in the solution.

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Limitations of the Benedict’s Test
● Benedict’s does not distinguish between reducing sugars - not
specific.
● Not sensitive at low conc. as it falls out of the sensitive range
of the calibration curve.
Enzymes in a test will give you both sensitivity + specificity.

Test for Non-reducing Sugars

1. Carry out the test for reducing sugars - should test -ve.
2. With a fresh sugar sample (equal vol. e.g. 2cm3) add 1cm3 of dilute
HCl acid to hydrolyse any glycosidic bonds present.
a. Mix it.
3. Place the test tube in a 90°C water bath
4. leave for 5mins.
5. Add sodium hydrogen carbonate solution until the solution is
neutral or slightly alkali (use pH paper to test this and until it
stops fizzing).
6. This needs to be done to neutralise the acid as the reducing sugar
test doesn’t work in an acidic environment.
7. Carry out the test for reducing sugars again - should test +ve.

Testing for Starch (Iodine Test)

1. Place 2 drops of the test solution on a spotting tile / in a test
tube.
2. Add a drop of iodine solution.
3. Look at the results
a. +ve result: brown to blue-black
b. -ve result: remains brown.

CONTROLS: Known +ve that would blue-black (e.g. amylose and amylopectin)
Known -ve that would remain brown (e.g. glucose)

Lipids
• Used as an energy store, thermal insulator, buoyancy agent, and
protection of vital organs.
• Triglycerides & phospholipids are 2 groups of lipids. The different
properties of the two are related to difference in structures.
• Triglycerides and phospholipids are not polymers
• They are not a long molecule of repeating sections.

Triglycerides = 1 glycerol and 3 fatty acid chains

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Glycerol
• Glycerol is an alcohol containing 3 -OH groups.
• The 3 -OH groups allow glycerol molecules to join with 3 F.A.s
• This produce a triglyceride.

Fatty Acid
• A fatty acid (F.A) is an organic (carboxylic) acid
• They can be saturated or unsaturated.

- The basic F.A. formula is “R.COOH”,

- R represents a hydrocarbon chain, in this case a long one.
- Unsaturated F.A.s contain one or more C=C, this means they could bond
to more H atoms.
- Saturated F.A.s contain no C=C so can’t bond to any more H.

• It is the nature of the F.A.s which determines the characteristics

of any particular lipid.

• If you do A-Level Chemistry, here’s that info but quickly:

A. saturated = no double bonds
B. Unsaturated = Containing double bonds
- These acids are called fatty simply because of the LONG R group.

Condensation Reactions with lipids

• Triglycerides are formed by the condensation of 1 molecule of glycerol
and 3 F.A. molecules
• The bond formed between the glycerol and the carboxyl group located in
the F.A. is called an ester bond / ester linkage.
➡Formation of ester bond is also called esterification.

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Phospholipids
• The structure of phospholipids is similar to triglycerides
• The only difference is that one F.A. chain is substituted with a
phosphate-containing group.
• ‘Head’ is made of glycerol and phosphate
• phosphate group means ‘head’ is hydrophilic (attracted to water)
• the 'tail’ of F.A. chains is hydrophobic (repelled by water)

Testing for Lipids (The Emulsion Test)

1. Add 4cm3 of ethanol to test solution and shake.
2. Pour solution into a 2nd test tube of 2cm3 boiled water.
3. Results
A. +ve result: cloudy white emulsion formed.
B. -ve result: remains colourless.
➡ This is due to lipids’ solubility in ethanol and
insolubility in water.

Proteins - General Properties

• Monomers = amino acids
• Polymer = polypeptide (protein)

Amino Acids
General structure of an amino acid involves one ‘central’ C atom (α-
carbon) with bonds to 4 groups:
• Hydrogen atom
• Amino group (which is basic)
• Carboxyl group (which is acidic)
• Variable R-group (The carbon-containing chain)

• They are called amino acids because they’ve got amino (NH2) and
carboxylic acid (COOH) groups.
• Amino acids differ only in their R groups -
• In nature there’s 20 different R-groups therefore 20 different
amino acids.

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Peptides and Proteins

● (Functional) proteins: one or more polypeptide chains folded into a
complex 3D shape.
● Dipeptide: 2 amino acids joined by a peptide bond. H-N-C=O
○ Peptide bond: a bond formed by the condensation of 2 amino
acids between the carboxyl group of one amino acid and the
amino group of another.
● Polypeptide: Many amino acids joined by peptide bonds (formed by
many condensation reactions).

Condensation Reaction

peptide bond

Protein Structure
Primary structure: the sequence of amino acids in a polypeptide. (unique
to each gene!)

Secondary structure:
• the shape the polypeptide chain folds into, such as an α-helix or a β-
pleated sheet
• (both can occur in one polypeptide chain)
• α-helix and a β-pleated sheets are held together by H-bonds between the
carboxyl groups and amino groups in the polypeptide backbone
• Its folding is dictated by the shape of the R-group and the enzyme
folding the protein up.(R-group itself is not involved in it)
• α-helix: the polypeptide is wound together to form a helix.
• It is held by H-bonds running parallel with the long helical axis.
• Lots of H-bonds so very stable and strong structure.
• β-pleated sheet: the polypeptide chain zigzags back and forth forming
a sheet of antiparallel strands
• held by H-bonds.
• Strength achieved through layering and bonds between layers
• This means, compared to an α-helix, it has a weak structure.
• Other examples of secondary structure include β-bend and triple helix
(collagen only).

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Tertiary structure:
• further folding of the secondary structure which gives the protein the
characteristic complex, 3D shape that is closely related to its
function.
• This is dependent on primary structure for the side chain bonds (i.e.
R-group) which hold the tertiary structure together.
• 4 types of bonds involved:

○ Hydrophobic / hydrophilic interactions:

• some amino acids may be hydrophobic
while others are hydrophilic.
• In a water based env., a globular
protein will orientate itself such
that its hydrophobic parts are
towards its centre + its
hydrophilic parts are towards its
edges.
○ Hydrogen bonds:
• weak: Between uncharged R-
groups.
○ Ionic bonds:
• fairly strong. Between R-groups
with +ve or -ve (opposite)
charges,
○ Disulfide bridges:
• very strong; Covalent bonds
between 2 sulfur containing
amino acids.

There are 2 types of tertiary structure to learn:

1)FIBROUS PROTEINS:
• look like rope, typically long, thin, and insoluble
• often have structural functions
• e.g. collagen (in bone), keratin (in hair) + actin (in muscle)
• Expect regular repeats in the primary structure to ‘twist’ at
regular intervals.
2) GLOBULAR PROTEINS:
• more spherical in shape. They are soluble and have biochemical
functions
• e.g. enzymes, membrane proteins, receptors etc.
• Expect no regular repeating pattern in primary structure.
Quaternary structure:
how different polypeptide chains are arranged in the protein ➜ only
found in proteins containing more than one polypeptide chain.
• E.g. haemoglobin
○ It has a globular quaternary structure.
○ It becomes a biologically active upon the establishment of its
quaternary structure.
○ It is also a conjugated protein - this means that it’s
attached to a prosthetic group.
• E.g. collagen
○ It has a fibrous quaternary structure.
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Testing for Proteins (Biuret Test)

1. Add 1cm3 biuret reagent (composed of copper(II) sulphate and
potassium hydroxide) to test solution
2. Results:
A. +ve result = clear blue ➜ lilac-purple.
B. -ve result = remains clear blue.

Proteins - Enzymes
• Enzymes are globular proteins; they’re biological catalysts.
• For a reaction to occur, the substrate must collide with the enzyme and
form an enzyme substrate complex.
- Enzymes are biological catalysts; a key feature of a catalyst is that
it remains unchanged before and after a reaction occurs. This is true
for enzymes.

• Enzyme-substrate complex: the enzyme and substrate bonded together.

• Once enzyme-substrate complex forms the reaction will happen more
easily.
• In chemistry a catalyst is defined as a substance that lowers the
activation energy of a reaction by providing an alternative reaction
pathway.
• That is true of enzymes too
• Activation energy: the energy required for a reaction to start.

• Denaturation: a permanent change to the shape of an enzyme’s active

site
• This means it’s no longer able to combine with its complementary
substrates to form an enzyme-substrate complex.
○ This occurs as a result of breaking the bonds that maintains its
tertiary structure.
○ It happens when pH / Temperature / other physical conditions change
from those typical for the enzymes environment

Enzyme Models
Lock and Key Model
• Enzymes are highly specific.
• for the enzyme to be useful the substrate must be COMPLEMENTARY to the
active site.
• This is explained using the ‘Lock and Key Hypothesis’
• It says:
A. the active site of enzyme = rigid lock;
B. substrate = key which fits exactly into the lock.

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Induced Fit Model

● An enzyme’s active site is not perfectly matched to the substrate
before the two bind to form the enzyme-substrate complex.
● A change in the shape of the enzyme is induced when enzyme-
substrate complex is formed in order to enfold the substrate.
● ∴ enzyme takes up its most effective catalytic shape after binding
w/ the substrate (i.e. active site before = partially
complementary; after = fully complementary).
● The distorted enzyme in turn distorts the substrate, straining the
bonds. This puts stress on the bonds, thus lowering the activation
energy as it is less stable.
● The reaction occurs + products = formed ➜ enzyme-product complex.
● Product ≠ complementary ∴ no longer binds to active site + moves
away.
! The enzyme returns to its normal shape + available for next
reaction.

Factors that Affect Rate of Enzyme Reactions

• The following affect the EFFECTIVE COLLISION RATE between enzymes and
substrates; these affect the probability of forming enzyme-substrate
complexes:
➔ Temperature
➔ Substrate concentration
➔ Enzyme concentration

• The following affect the SHAPE OF THE ACTIVE SITE.

• This is what changes the probability of forming enzyme-substrate
complexes as the active site is no longer complementary to the
substrate:
➔ High temp. - breaks the hydrogen bonds as they are weak.
➔ pH - breaks the ionic bonds.
➔ Inhibitors - either blocks or changes active site so enzyme-
substrate complex can’t be formed.

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There are two major processes affecting the action of the enzyme:

Temperature

1. As temp. Increases, KE of enzyme and substrate increase

● ↑ effective collision rate between enzyme and substrate
● ↑ probability of forming enzyme-substrate complexes
● ↑ the rate of reaction. UNTIL OPTIMUM TEMP. IS REACHED
2. As temp. increases, the increased KE may affect the overall
stability of the enzyme.
● At high temp, the enzyme has such high impact collisions due
to high KE that it causes the enzyme’s H-bonds to break…
● so changing the shape of the active site. This means the
active site no longer complementary to the substrate
● so even if the enzyme and substrate collide, they will not
form enzyme substrate complexes.
● The Enzyme is permanently DENATURED.

Temperatures below/equal to optimum temperature:

Rate of reaction limited by KE of molecules: it limits number of
effective collisions between enzyme and substrate.

Temperatures above optimum temperature:

Rate of reaction limited by stability of enzymes.
At these high temp.s the enzyme has such high KE, H-bonds within the
molecule break, causing a permanent change in shape of the active site -
denaturation (making the enzyme loose its active site)

Substrate Concentration

① increased substrate conc. increase collision rate, so number of

enzyme-substrate complexes, so increases rate of reaction.
② All active sites are full, so any further increase in substrate conc.
will not increase the rate of reaction until another
variable (e.g. enzyme conc.) is changed.

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Enzyme Concentration
• Increased enzyme conc. = increased number of active sites
• This increases the probability of an enzyme colliding with a substrate
to form an enzyme-substrate complex
• This increases the rate of reaction.

pH
• Enzymes are very sensitive to changes in pH; they are usually active
across a narrow pH range.
• Changes in pH alter ionic bonds holding enzymes in their tertiary
structure (changing the shape of the active site)
• Changes in pH will only affect basic and acidic R-groups.
• If goes slightly acidic, acidic R-groups will accept protons making
them neutral and decrease the number of ionic bonds.
• If goes slightly basic, basic R-groups will donate protons making
them neutral, decreasing the number of ionic bonds.
• SO: change in tertiary structure due to change in number of ionic
bonds (which help form active site).

Inhibitors
Inhibitors: substances which can interfere with enzymes, reducing or even
completely destroying their action.
● There are 2 types: competitive inhibitors + non-competitive
inhibitors.

Competitive Inhibitor
• Competitive inhibitors have shapes resembling the enzyme’s normal
substrate
• They competes with the normal substrate to occupy the active site.
• If an inhibitor occupies an active site, enzyme-inhibitor complex
formed, preventing enzyme-substrate complex from forming.

Effect of competition inhibitor depends on:

• Substrate conc. ➜ more substrate conc. means more
substrate entering active site. This lowers the blocking
inhibitor probability therefore decreases the effect of
competitive inhibitor.
• How tightly the enzyme binds to the inhibitor and to
substrate.
• Inhibitor conc. ➜ higher inhibitor conc. decreases
substrate entering active site probability as ↑ inhibitor
blocking active site probability.

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Non-competitive Inhibitor
• The effect of non-competitive inhibitors is independent of
substrate conc.
• Non-competitive inhibitor does not attach to the active site, but
binds with enzyme on its allosteric binding site.
• Once attached, a non-competitive inhibitor causes active site to
change shape, preventing normal substrate from binding.
• Not all non-competitive inhibitors are bad.
• The end-product of a reaction can act as a non-competitive
inhibitor, controlling a series of enzyme catalysed reactions
• This is known as end-product inhibition.

Differentiating: Competitive and Non-competitive Inhibitors

• Based on what we just learned, the 2 types of inhibitors can be

distinguished experimentally by carrying out a substrate conc. and rate
of reaction experiment in the presence and absence of inhibitor.
• If the inhibition is reduced at high substrate concentration then the
inhibitor is competitive.
• Probability of non-comp. inhibitor forming enzyme-inhibitor complex
not affected by substrate conc. as binds to allosteric binding site
instead.
■ Ratio of inhibitor conc. to enzyme conc. will deduce how
much lower new Vmax is.

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Nucleic Acids and DNA

Structure of DNA and RNA
• DNA and RNA are both types of nucleic acids.
• They are important information-carrying molecules
• In all living cells:
● DNA (deoxyribonucleic acid) hold genetic info.
● RNA (ribonucleic acid) transfers genetic info. from DNA to the
ribosomes.
○ Ribosomes are formed from RNA and proteins.

Nucleotide Structure
• Both DNA and RNA are polymers made from nucleotides (monomers).
• Each nucleotide is formed from a pentose, a nitrogen-containing organic
base, and a phosphate group:
● The components of a DNA nucleotide are deoxyribose, a phosphate
group, and one of organic bases
○ adenine, A
○ cytosine, C
○ guanine, G
○ or thymine. T
! The components of an RNA nucleotide are ribose, a phosphate group,
and one of the organic bases adenine, cytosine, guanine or uracil.

Polynucleotide Structure
• Many nucleotides join together to form polynucleotide strands.
• The nucleotides bond by condensation reactions which form
phosphodiester bonds between ribose sugars and phosphate groups.
• The chain of phosphate and sugars = sugar-phosphate backbone.

• A DNA molecule is a double helix with 2 polynucleotide chains held

together by H-bonds between complementary base pairs:
• A=T = 2 H-bonds (always equal amounts of A + T)
• C☰G 3 H-bonds (always equal amounts of C + G)
• The 2 polynucleotide strands are anti-parallel.
• The sugar-phosphate backbone protects the genetic info.
• An RNA molecule is a single polynucleotide strand which is relatively
short compared to most DNA polynucleotides.

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DNA as the Carrier of the Genetic Code
The relative simplicity of DNA led many scientists to doubt that it
carried the genetic code. Some argued that genetic info. must be carried
by proteins - which are much more chemically varied.

DNA + RNA Comparison: Structure

DNA RNA

Shape Double-stranded - a double Single-stranded

helix held together by H-
bonds.
Pentose Deoxyribose sugar Ribose sugar
sugar

Bases A T C G A U C G

Size Long Relatively short

DNA Replication
• The method of DNA replication is known as semi-conservative replication
• It’s called “semi-conservative” as half of the strands in each new DNA
molecule are from the original DNA molecule
• This ensures genetic continuity between generations of cells

Process of Semi-conservative Replication

1. Enzyme DNA helicase unwinds the DNA double helix and, using ATP,
breaks the H-bonds between the complementary bases in the
polynucleotide strands.
- Two single strands formed
2. Each original single strand acts as a template for the new strand.
- Free-floating DNA nucleotides are attracted to the exposed bases
on the template strands by complementary base pairing (H-bonds
formed between: A=T + C☰G)
3. Condensation reactions join the adjacent nucleotides of the new
strand together with covalent (phosphodiester) bonds.
- These are catalysed by the enzyme DNA polymerase.
- New sugar-phosphate backbone formed.
4. This process occurs to both exposed strands, resulting in 2
daughter DNA strands.

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Meselson and Stahl’s Experiment

1. A sample of bacteria was grown for many generations in a medium
containing 15N, a heavy isotope of Nitrogen.
2. A control culture of bacteria was grown for many generations in a
medium containing 14N, the more common isotope of N.
3. As the bacteria reproduced, they took Nitrogen from the medium to
help make more nucleotides for new DNA
a. Eventually Nitrogen became part of the bacteria’s DNA.
4. The bacteria grown in 15N environments were transferred to a 14N
medium and left for periods of time that corresponded to the
generation time of bacteria.
5. Samples of bacteria were taken at intervals to analyse the parental
1st gen. and 2nd gen. DNA.
6. Composition of DNA were analysed using density gradient
centrifugation.
7. After samples are spun at high speed in a centrifuge, DNA is
separated according to its density.
8. This is where it gets interesting:

… HEAVY DNA (which contained 15N) forms a band lower in the tube.
… LIGHT DNA (which contained 14N) forms a band higher in the tube.
… HYBRID DNA (containing 15N + 14N) would settle out in between
HEAVY and LIGHT DNA, (forming a band in between)

This meant that If DNA replication was:

1. Conservative
1. 1st gen. and 2nd gen. = heavy DNA band (from original DNA) and
light DNA band (from new DNA) formed.
2. Semi-conservative
1. 1st gen: only hybrid DNA band formed, as one heavy DNA (original)
strand and. one light DNA (new) strand in each daughter DNA
molecule.
2. 2nd gen: hybrid DNA band and light DNA band formed.
3. Dispersive
1. 1st gen. and 2nd gen: only hybrid DNA band formed, as one heavy DNA
(original) strand and one light DNA (new) strand in each daughter
DNA molecule.

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RESULTS: DNA replicated semi-conservatively!

● Parental generation: all DNA had a density of heavy DNA.

○ So, bottom of tube therefore only heavy DNA present.
● 1st generation: all DNA had a density midway between that of heavy
DNA + light DNA
○ So equal amounts of each => hybrid DNA.
● 2nd generation: 2 sorts of DNA detected:
○ one was light DNA; the other containing equal amounts of 14N
and 15N = hybrid DNA
- (i.e. like DNA in 1st gen.).

Throughout the investigation, DNA from the control produced only light
bands, indicating it contained only 14N.

And they say science isn’t interesting hey!!!

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ATP
A single molecule of ATP (adenosine triphosphate) = a nucleotide
derivative (a phosphorylated nucleotide)
It's formed from a molecule of ribose, a molecule of adenine, and 3
phosphate groups.

Hydrolysis of ATP
• The energy in ATP is stored in high energy bonds between phosphate
groups.
• Energy is released via hydrolysis reactions where ATP is broken down
into ADP (adenosine diphosphate) and Pi (inorganic phosphate).
• The reaction is catalysed by ATP hydrolase.
• The hydrolysis of ATP can be coupled to energy-requiring reactions
within the cell.
• The Pi released during hydrolysis of ATP can be used to
phosphorylate other compounds, often making them more reactive.

Resynthesis of ATP
• ATP is resynthesised by the condensation reaction of ADP and Pi.
• This reaction is catalysed by ATP synthase during photosynthesis, or
during respiration.

Water
A molecule of H2O consists of one atom of O + 2 atoms
of H covalently bonded together (which means they
share electrons).
● Because the electrons shared by hydrogen are
pulled towards the oxygen atom, O = 𝛿- (slightly
negative)
● This, as a result, makes H 𝛿+ (slightly positive)
● This, by definition, makes H2O a polar molecule; water has
permanent partial charges.

Hydrogen Bonding in water

• H-bonds are forces between a 𝛿+ H and 𝛿- O in 2 molecules of H2O.
• Relative to a typical chemical bond (Ionic, Covalent, Metallic) H-bonds
are weak
• H-bonds form because 𝛿- O atoms of H2O attract the 𝛿+ H atoms of other
H2O.
• Hydrogen bonding gives water some of its useful properties.

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Properties of Water

Important Metabolite
➔ H2O is a metabolite in many reactions (including condensation and
hydrolysis reactions)
● A hydrolysis reaction requires a molecule of H2O to break a bond.
● A condensation reaction releases a molecule of H2O as a bond is
formed.

Important Solvent
➔ H2O is an important solvent in which metabolic reactions occur.
➔ A lot of important substances in biological reactions are ionic (made
of +ve and -ve charged ions)
● H2O is polar so the 𝛿+ “H” will be attracted to negative ions in
these substances.
○ The 𝛿- O will be attracted to positive ions.
● This means “layers” of H2O will form around ions
○ That is what dissolution actually is
● This means living organisms can take up useful substances dissolved
in H2O
○ these dissolved substances can be transported around the
organism’s body.

High Specific Heat Capacity

➔ Specific heat capacity: the energy needed to raise the temp. of 1g of
substance by 1°C.
➔ H2O has a relatively high specific heat capacity due to H-bonds, soit
buffers changes in temp.
● When H2O is heated, lots of energy is taken in to break H-bonds
○ This means less heat energy is available to increase the temp.
of the H2O
○ This means it takes lots of energy to heat water relative to
other substances
○ This, in turn, means high specific heat capacity.
● This is useful for organisms: it means H2O doesn’t experience rapid
temp. changes.
○ So, it's a good habitat (as temp. likely to be more stable
than on land)
○ H2O inside organisms also maintain a very stable temperature.
- helps maintain a constant internal body temp.

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Large Latent Heat of Vaporisation
➔ Latent heat: the heat energy that is needed to change a substance from
one state to another.
➔ H2O has a relatively large latent heat of vaporisation, providing a
cooling effect with little evaporation.
● H2O vaporises when H-bonds holding H2O molecules together are
broken.
○ It takes a lot of energy to break H-bonds
○ This means it requires a lot of energy for H2O to evaporate.
○ This, in turn, means H2O has a high latent heat of
vaporisation.
● This is useful for living organisms; it means they can use H2O loss
through evaporation to cool down without losing too much H2O.
○ When water evaporates, it carries away heat energy from a
surface, which cools down the surface and helps decrease the
temperature

Strong Cohesion
➔ There’s strong cohesion between H2O molecules (In english, they tend
to stick to each other) because H2O is polar.
● Strong cohesion helps H2O flow; it’s, therefore, good for
transporting substances.
○ It also supports columns of water in the tube-like transport
cells of plants (i.e. xylem).
● Strong cohesion means H2O has a high surface tension when it comes
into contact with the air.

Inorganic Ions
• An Inorganic Ion is an Ion that doesn’t contain Carbon.
• Inorganic ions exist in solution in cytoplasm and body fluids of
organisms.
• some in high concentration, others in low concentration.

Each type of ion has a specific role, depending on its properties:

● Hydrogen ions (H+) determine pH: acidic environments have lots of
free H+ ions.
○ More H+ = lower pH.
● Iron ions (try saying that 5 times) (Fe3+/Fe2+) form part of
haemoglobin.
○ They form the prosthetic group (haem) which allows haemoglobin
to fulfil its role in oxygen transportation.
○ When oxygen is bound, Fe2+ temporarily becomes Fe3+ until
oxygen is released.
● Sodium ions (Na+) are involved in the co-transport of glucose and
amino acids across membranes.
● Phosphate ions (PO43-) when attached to another molecule, is called
a phosphate group.
○ They are major components of DNA, RNA, and ATP.

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