1.

2 Molecular Biology
2.1 Molecules to metabolism
Molecular biology:
● Reductionist approach in coming to conclusions. Can’t explain everything

by breaking down complex systems into small parts and studying them individually.
Need to study emergent properties as well, which only occur when the organisms
are studied as a whole.

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Synthesis of Urea:

o ●  Ammonia + Carbon Dioxide => Ammonium Carbonate => urea + water

o ●  Synthesised in the liver due to excess amino acids (deamination).
o ●  Excreted in urine.

Vitalism:

● Origin of all life comes due to a “vital principle”, which is different to life

being composed purely of chemical + physical forces. Production of Urea by

Fredrich Wohler in 1828, disproved this theory. First organic compound, which was
synthesised artificially; hence without a vital principle.

Carbon Compounds:
● Carbon atoms can form 4 covalent bonds. These can be single or double

bonds.
● Can form chains/rings of any length.

Classifying Carbon atoms:

o ●  Carbohydrates: Carbon, Hydrogen, Oxygen. H:O => 2:1

o ●  Amino acids: Carbon, Hydrogen, Oxygen, Nitrogen, 2 Amino acids also

contain sulphur.

o ●  Lipids: Insoluble in water. Triglycerides are fats if solid at room

temperature and oils if liquid. Also contain Carbon Hydrogen and Oxygen.

o ●  Nucleic Acids: Chains of nucleotides. Carbon, Hydrogen, Oxygen, Nitrogen

 and Phosphate. Form DNA and RNA.

Drawing molecules:

o ●  Amine group: NH2

o ●  Carboxyl group: COOH
o ●  Methyl group: CH3
o ●  Hydroxyl group: OH
o ●  Ribose: C5H10O5. OH groups on Carbons 1, 2 and 3. Point up, down, down

respectively.

o ●  Glucose: C6H12O6. OH groups on Carbons 1, 2, 3, 4. Point down, down, up,

down respectively (alpha). On beta glucose, found in cellulose, OH group on

carbon 1 points up.

o ●  Saturated fatty acids: Carbon atoms form an un-branched chain of about

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14-20 atoms, no double bonds.

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o ●  Amino Acids: Contain Amine group; Carboxyl group; Hydrogen atom; and
R variable group.
 o ●  Lipids contain less oxygen than carbohydrates. Proteins usually contain
sulphur. Carbohydrates have a H:O ratio of 2:1.

Metabolism:

o ●  Web of all enzyme catalysed reactions in a cell or organism. Most

reactions are enzyme catalysed and generally occur in cell cytoplasm.

o ●  Anabolism: Synthesis of complex molecules from simpler ones. Monomers

=> Macromolecules by condensation reactions. Photosynthesis is an

anabolic process.

o ●  Catabolism: Breakdown of complex molecules into simpler ones including

the hydrolysis of macromolecules into monomers. Digestion, respiration and

decomposition are catabolic processes.

2.2 Water
Hydrogen bonding in water:

o ●  Water molecules are polar and hydrogen bonds form between them.
o ●  Bonds between hydrogen and oxygen involve the unequal sharing of

electrons because oxygen nuclei are more attracted to electrons than

hydrogen nuclei. Hence hydrogen atoms are partially positive and oxygen
atoms are partially negative, forming two poles.

o ●  Adjacent water molecules are therefore attracted to one another

(hydrogen to oxygen) forming hydrogen bonds.
o ●  In general a hydrogen bond forms when a hydrogen atom in one polar
molecule is attracted to a partially negative atom of another polar covalent
molecule.

Water properties:

o ●  Cohesive properties: the binding together of two-like molecules. Water to

water. Hydrogen bonds enable this binding. Used in capillary action.

o ●  Adhesive properties: Hydrogen bonds between water and other polar

molecules. Useful in leaves where water adheres to cellulose molecules in
 cell walls. Maintains dampness for diffusion of CO2.

o ●  Thermal properties: High specific heat capacity; restricts temperature of

water in varying environment. This is due to water requiring large amounts

of energy to change by 1 C̊ . Allows for stability of water, but also means it is a
large store for heat energy, hence serving as a coolant.

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o ●  Solvent properties: Polar nature of water means that it forms shells

around other polar molecules. As a result solutes to clump together. Both
positive and negative ions dissolve.
 o ●  Hydrophilic and Hydrophobic properties: All chemical substances that
dissolve in water are hydrophilic. Substances that water adheres to are also
hydrophilic. Substances that are insoluble are hydrophobic: uncharged and
non-polar particles, like lipids. When hydrophobic substances enter water,
hydrogen bonds form between water molecules but not between water and
hydrophobic substances. This is because hydrophobic substances are non-
polar and are therefore immune to hydrogen bonds. Instead hydrophobic
interactions occur, as the substances are more attracted to themselves than
they are to water, and so they end up clumping together.
o ●  Water vs. Methane: Both small molecules linked by single covalent bonds
and have similar masses. However methane is nonpolar and doesn’t form
hydrogen bonds. Water has a higher specific heat capacity, latent heat of
vaporisation and thus a higher boiling point. Methane is liquid over a range
of 22 C
̊ whereas water is liquid over a range of 100 C̊ .
o ●  Sweat as a coolant: Heat needed for the evaporation of water in sweat is
taken from the tissues of the skin, reducing their temperature. Solutes are left
on the skin. Hypothalamus controls sweat secretion. Adrenaline can cause
the body to sweat even when cold because it anticipates a period of intense
activity.

Transport in blood plasma: Blood transports a variety of substances.

o ●  Sodium Chloride: Dissolves in water to form Na+ and Cl-.

o ●  Amino Acids: Both negative and positive charges. Solubility depends on R

group. All amino acids, however, are soluble enough to dissolve in blood

plasma.

o ●  Glucose: Freely soluble because it is polar.

o ●  Oxygen: Non-polar molecule. Dissolves due to its small size but saturates

blood at low levels. Higher temperature blood plasma results in lower

bandwidth of absorption. Hence Haemoglobin, an oxygen carrier, is present
in red blood cells.

o ●  Fatty molecules: Entire nonpolar and large. Completely insoluble. Carried

in micelles, which are lipoprotein complexes. Phospholipids act as a vesicle,
with hydrophobic fatty tails on the insides, facing the fatty molecule. Single
layer of phospholipid.
o ●  Cholesterol: Mainly hydrophobic: Insoluble in water. Transported in
lipoprotein complexes. Positioned within the phospholipid monolayers with
the hydrophilic part facing outwards with the phosphate heads.

2.3 Carbohydrates and Lipids:

Carbohydrates: Monosaccharide monomers are linked together by condensation
reactions to form disaccharides and polysaccharide polymers.

● Monosaccharides: Glucose, fructose, galactose and ribose. Single sugar units.

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o ●  Disaccharides: Two monosaccharides linked together. Maltose: glucose +

glucose. Sucrose: glucose + fructose. Lactose: glucose + galactose.
o ●  Polysaccharides: Starch and Glycogen are examples.
o ●  Monosaccharides combine in a condensation reaction. Loss of OH group
 from one molecules and hydrogen from another. OH and H form H2O. This
anabolic process requires energy. Link between two monosaccharides is
called a glycosidic bond.

Polysaccharides: Cellulose and starch in plants. Glycogen in humans.

o ●  OH groups on Carbon 1, 4 and 6 are used to make links. OH on Carbon 6 is

usually for side branches.

o ●  In alpha glucose the OH points downwards and in beta, it points upwards.
o ●  Cellulose: Linking beta glucose in a 1-4 structure makes cellulose. OH

groups point in opposite directions therefore each glucose molecule is

positioned 180 ̊to the previous one. Hence the beta glucose molecules
alternate ‘up and down’. This results in a straight chain. Un-branched chains
allow them to form bundles, connected by hydrogen bonds and created
cellulose micro-fibrils. These give cellulose its high tensile strength. Used in
cell walls.

o ●  Starch: Made by linking alpha-glucose molecules. Made by 1-4 glycosidic

bonds. All –OH molecules point downwards, hence all molecules have a
similar orientation, which results in a curved structure. This forms two types:
amylose and amylopectin. Due to insolubility of both molecules, despite them
being hydrophilic, they are used as a storage molecule as they do not cause
an influx of water into cells.
o ●  Glycogen: Similar to amylopectin in structure; but has more branching.
The molecule is more compact. Stored in the liver and some muscles. Stores
energy in the form of glucose because large stores of dissolved glucose would
cause osmotic problems. Easy to add/remove glucose molecules on either
branched/unbranched sides of glycogen/starch.
Amylose Amylopectin
Branched Unbranched
Alpha helix Globular
Hydrophilic but insoluble due to
Hydrophilic but insoluble due to size
size
Has some 1-6 linkages in addition to 1- 4
Has only 1-4 linkages
linkages

Lipids:

o ●  Triglycerides are formed by condensation from three fatty acids and a

glycerol.

o ●  All lipids are insoluble.

o ●  Triglycerides are the fat in adipose cells and oils in sunflower seeds.
o ●  Fats are liquid at body temperature (37 ̊C) but solid at room temperature

(20 ̊C).

o ●  Oils are always liquid.

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Triglycerides:

o ●  3 fatty acids + glycerol => triglyceride + 3H2O.

o ●  Fatty acids form ester bonds with glycerol, which are generally formed
 when an acid reacts with the OH group in alcohol. Energy from triglyceride
can be released from aerobic cell respiration.

Energy storage:

o ●  Lipids are more suitable for long-term energy storage than

carbohydrates.

o ●  Adipose tissue is located directly beneath the skin and round some organs

including the kidneys.

o ●  Amount of energy released in cell respiration per gram of lipids is double

that of carbohydrates. Therefore it adds half the body mass as

carbohydrates.

o ●  Fats store as pure droplets whereas glucose stores with two grams of

water (per gram of glucose).

o ●  Effectively lipids are 6 times more efficient in energy storage than

carbohydrates.

o ●  Lipids are insulators as they are poor conductors of heat. This is why

adipose tissue is subcutaneous.

o ●  They can also act as shock absorbers because they are liquid at body

temperature.

o ●  However fat cannot be rapidly used and therefore can only be used in

aerobic respiration.

Body Mass Index (BMI):

o ●  BMI = Mass (kg)/(Height (m))2.

o ●  Units are in kg/m2
o ●  Causes of being overweight/underweight vary..
o ●  Obesity and anorexia nervosa are both eating disorders, which amount to
 unhealthy body composition.

o ●  Can use a nomogram to calculate BMI (its a cross of 2 scales).

Fatty Acids:

o ●  Can be mono/polyunsaturated or saturated.

o ●  Most fatty acids have 14-20 carbon atoms.
o ●  Carbon atoms with a double bond can only link to two hydrogen atoms.
o ●  Fatty acids without any double bonds are saturated and those with

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double bonds are mono/poly unsaturated, depending on the number of

double bonds present. ● Unsaturated fatty acids:

o Can be ‘cis’ or ‘trans’ isomers.

o Fatty acids are cis if the hydrogen atoms are on the same side of

the double bond. If they are on opposite sides they are trans.
o In cid fatty acids there is a kink at the double bond, which causes the fatty acid to
bend. This contributes to cis’s ability to pack tightly in regular arrays; far more
efficiently stored than saturated

fatty acids. Tight packing also lowers their melting point.

o Trans-fatty acids have no kinks because they have been artificially

hydrogenated in a factory.

Health risks:

o ●  Main concerns is CHD (Coronary Heart Disorder) .

o ●  Coronary arteries getting partially blocked resulting in clotting and
 damage. Positive correlation between saturated fats and CHD.

o ●  Cis monosaturated fatty acids are claimed to be good fats.

o ●  Trans fats are the biggest contributors to heart disease.

2.4 Proteins
Amino acids and polypeptides:

o ●  Amino acids are linked together by condensation to form polypeptides.

The linking together occurs on ribosomes during translation.

o ●  Dipeptides: Two amino acids.

o ●  Polypeptide: 20 or more amino acids.
o ●  Oligopeptide: between 2 and 20 amino acids.

Diversity of amino acids:

o ●  20 different amino acids in polypeptides.

o ●  By changing an amino acid, you essentially get an entirely different

protein. In collagen, the change of one amino acid from proline to

hydroproline, results in a stronger structure.

o ●  20n , where n is the number of amino acids in the chain.

o ●  Three bases of DNA code for one amino acid. These ‘codons’ are triplet

bases.
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Proteins and polypeptides:

o ●  Protein may consist of two single polypeptides or more than one

polypeptide linked together.

o ●  Lysozyme: 1 polypeptide.
o ●  Integrin: 2 polypeptides.
o ●  Collagen: 3 polypeptides.
o ●  Haemoglobin: 4 polypeptides.

Protein conformations:

● Amino acid sequence determines the 3D shape of the polypeptide.

Fibrous Globular
Elongated, with a repeating Intricate shape with parts that are helical or sheet-
structure like.
Polypeptide folds up as amino acids are added on.
Have bonds between the R groups of the amino acids.
No folding up, amino acid
prevents it. Hydrophobic groups on the inside and hydrophilic
groups on the outside.

Denaturation of protein:
 o ●  Heat/pH extremes (causes).
o ●  Bonds in 3D structure of protein are susceptible to breakage.
o ●  This breakage in bonds results in denaturation.
o ●  Denatured protein does not normally return back to its former structure.

Soluble proteins become insoluble and form a precipitate because

hydrophobic groups become exposed to water.

o ●  Heat breaks intermolecular bonds or interactions.

o ●  pH changes affect charge on the R groups, breaking ionic bonds with the

protein or causing new ones to form.

Protein functions:

o ●  Catalysis.
o ●  Muscle contractions.
o ●  Cytoskeletons.
o ●  Tensile strengthening.
o ●  Blood clotting.
o ●  Transport of nutrients and gases.
o ●  Cell adhesion.
o ●  Membrane transport.
o ●  Hormones and receptors.
o ●  DNA packing.
o ●  Immunity.

Examples of proteins:
● Rubisco: Ribulose phosphate carboxylase. Catalyses the reactions for

carbon fixation.

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o ●  Insulin: Signal to cells to absorb glucose. Reduces blood glucose. Shape and
chemical properties correspond to binding site on the receptor. Secreted by
beta cells in pancreas.
o ●  Immunoglobulin: Antibody. Binding sites for bacterial antigens has a
different binding cite – specific immunity.
o ●  Collagen: Rope-like protein made of three polypeptides wound together.
They are located in the skin, blood vessel walls to prevent tearing and allow
for tensile strength.
o ●  Rhodopsin: Pigments of rhodopsin, membrane proteins of rod cells in the
retina are light sensitive molecules surrounded by an opsin polypeptide.
 Changes in shape when it absorbs light, triggers opsin and abuses the rod cell
to send an impulse to the brain.
o ●  Spider silk: Polypeptide forms parallel arrays very resistant to breaking.

Proteomes:

● All of the proteins produced by a cell, tissue or organism. Genome of an

organised is fixed but a proteome is not because different cells make different
proteins. Proteomes reveal what is happening in a cell at the time, not what could
happen. Proteomes differ due to differences in amino acid sequences.

2.5 Enzymes:
Active site and enzymes:

o ●  Enzymes have active sites to which specific substrates bind.

o ●  Enzymes are globular proteins that work as catalysts.
o ●  Enzyme substrate specificity: one enzyme can facilitate one particular

substrate only.

o ●  Shape and chemical properties of active site and substrates match each

other.

o ●  Enzyme catalysts require molecular motion and the collision of substrates

with the active site.

o Substrate binds to enzyme.

o Substrate changes in chemical structure. o Products separate from active site.

● Collision: when enzyme and substrate come together. Collisions occur because of
random movements and are successful when the substrate and active site are
correctly lined up to each other.

Factors affecting enzyme activity

Temperature: Higher kinetic energy leads to greater rate of collision and an

increased chance of a successful collision as the energy could exceed the activation
energy needed for the reaction to proceed. However, bonds in enzyme vibrate more
and change of breakage increases. Breaking of bonds changes shape of active site
and this is called denaturation. As temperature increases and more enzymes
denature, the rate of collision decreases.

pH: Enzymes have an optimum pH for functionality. Change in pH, or deviation from
the optimum pH, results in reduced rate of reaction. When

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the H+ ion concentration is higher/lower than the optimum, enzymes activity is

hindered and the structure of the enzyme is altered – another example of
denaturation. Not all enzymes have the same optimum pH.

● Substrate concentration: Increased substrate concentration would mean more

frequent collisions between enzyme and substrate. After binding substrate to active
site it is unavailable to other substrates until the products have been created and
released. As substrate concentration rises, active sites are increasingly occupied at a
given moment; hence the rate of reaction will stagnate.

Immobilised enzyme:

o ●  Widely used in industry. Enzymes are immobilised by attaching them to

other substances or into aggregations to restrict movement. Enzymes can

be attached to a glass surface, trapped in alginate gel or bonded together.

o ●  Advantages:

o Easily separated from products of reaction, preventing contamination of products.

o Recycling of enzymes: more cost efficient.

o Increases durability of enzymes to temperature/pH change
o Higher enzyme concentration can be used for increased reaction

rate.
● Lactose free milk: Lactose is broken down into glucose and galactose with

the help of lactase, an enzyme.

o After extracting the lactase from yeast it is used commercially.
o Lactose intolerant individuals benefit off this.
o Galactose + glucose is sweeter so less sugar needs to be used.
o Glucose + galactose are more soluble and hence give a smoother
texture in icecream.
o Bacteria ferment glucose + galactose faster, so it is easily digested.

2.6 Structure of RNA and DNA:

Nucleic acids and nucleotides:

o ●  Nucleic acids, DNA and RNA, are polymers of nucleotides.

o ●  Linking together nucleotides forms nucleic acids.
o ●  They consist of three parts:

o A sugar: Ribose/deoxyribose. Both are five carbon atoms (pentose).

o Phosphate group: Acidic, negatively charged part of the nucleic acid.

o Nitrogenous base: Made of nitrogen. Either two/one rings of atoms in its structure
(purine (AG)/pyrimidine (CT)).

o Base and phosphate are linked to the sugar by covalent bonds.

o Covalent bonds are also formed between the phosphate of one

nucleotide and the sugar of the next - phosphate with no3 Carbon. o Creates a
backbone of alternating sugar and phosphate groups.
o Base sequence can vary, and this is how information is stored,

through sequencing of 4 bases.

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Differences between DNA and RNA:

Structure of DNA:

o ●  Double helix.
o ●  Made of two antiparallel strands of nucleotides linked by hydrogen

bonding between complementary base pairs.

o ●  Each strand consists of a chain of nucleotides linked by covalent bonds.

o ●  Antiparallel strands: One strand runs in the opposite direction to the

other.

o ●  Two strands are wound together to form a double helix and are held
 together by hydrogen bonds between the nitrogenous bases. 2 hydrogen

bonds between A and T, 3 hydrogen bonds between C and G.

o ●  Complementary base pairing: Adenine with Thymine (Uracil in RNA) and

Cytosine with Guanine.

2.7 Transcription, Translation and Replication:

Semi-conservative replication of DNA:

o ●  New strands of DNA are formed upon the template strand.

o ●  The original strand divides.
o ●  The free nucleotides are added upon the template strand.
o ●  As a result, two new strands are formed, both having 50% pre-existing

DNA.

o ●  Base sequence of the template strand determines the base sequences on

new strand, due to complementary base pairing.

o ●  A hydrogen bond would not form with a non-complementary nucleotide.

DNA Helicase:

o ●  Unwinds the double helix and separates the two strands by breaking the

hydrogen bonds. Groups of enzymes that use energy from ATP are

required to break the Hydrogen bonds.

o ●  Globular (6) polypeptides arrange around a string of DNA.

o ●  Causes unwinding of the DNA, which separates the strands.

DNA polymerase III:

o ●  Links nucleotides together to form a new strand, using pre-existing strand

as a template.

o ●  Each of the two strands after helicase splits the DNA molecule, are used as

templates.
DNA RNA
Deoxyribose - 2nd Carbon has no hydroxyl
Ribose
group
Two polymers of nucleotides (double One polymer of nucleotide (single
stranded) stranded)
Thymine Uracil

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o ●  DNA polymerase moves from the 5’ to 3’ direction, adding a nucleotide at a

time.
o ●  Nucleotides must be complementary to the base position on the template
strand.
o ●  Hydrogen bonds are formed between nucleotides.
o ●  After hydrogen bonds, DNA polymerase links the nucleotide to the

existing end of a new strand. This is done by making covalent bonds between
the phosphate groups of the new nucleotide on the new strand the sugar
group of the existing nucleotide on the new strand.

o ●  Very high degree of fidelity is maintained.

Polymerase chain reaction (PCR):

o ●  Use of Taq DNA polymerase to produce multiple copies of a specific DNA

sequence.

o ●  Very small quantity of DNA is needed at the start.

o ●  Three stages:

o DNA molecule is heated to 95 ̊C for 15 seconds to break the hydrogen bonds

between the two strands and separate the strands.

o DNA molecule is then cooled to 54 ̊C for 25 seconds during which multiple DNA
primase enzymes bind RNA primers bind on the parent strands. This stops them
from re-annealing with each other and also provides a starting point for replication.

o Reaction mixture then heated to 72oC, the temperature at which Taq DNA
polymerase works and adds complementary nucleotides to template strands.

▪ Taq DNA polymerase is extracted from bacteria, Thermusaquaticus, and can

withstand very high temperatures. It is used because it will not denature at 95 ̊C.
Reaction mixture is heated to 72 ̊C for 80 seconds, during which 1,000 nucleotides
are added per minute.
Transcription:

o ●  Synthesis of mRNA from the DNA base sequence using RNA polymerase.
o ●  Proteins are what determine observable characteristics in an organism.
o ●  Transcription occurs along the antisense strand. RNA polymerase binds

to it at the start of a gene and then moves along to separate the two DNA
strands. Concurrently it pairs RNA nucleotides with complementary bases.

o ●  Uracil replaces thymine and is complementary to Adenine.

o ●  RNA polymerase forms covalent bonds between RNA nucleotides and then
separates from the DNA. Transcription stops at the end of the gene,

the enzyme is then released and the mRNA molecule as well.

Ribosomes:

o ●  Synthesis of polypeptides on ribosomes: ribosomes consist of a small and

a large subunit. Have binding sites for each molecule that partakes in the

process.

o ●  Large subunit makes peptide bonds between amino acids to link the,

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together into a polypeptide.

Messenger RNA and genetic code:

o ●  mRNA determines all sequences of polypeptides according to genetic

code.

o ●  Length of mRNA is usually 2000 nucleotides.

o ●  Only certain genes will be transcribed, depending on which protein is

required to be made.

o ●  Cells that need or secret large amounts of a particular polypeptide will

contain large amounts of the specific mRNA needed to create it.

Codons:
 o ●  Genetic code converts base sequence on mRNA into amino acid sequence.
o ●  Sequence of three bases is called a codon. 64 possible codons.
o ●  Genetic code is degenerate - many codons specify the same amino acid.
o ●  Each amino acid is carried by a transfer RNA. Contains a 3 base anti-

codon complementary to the mRNA codon for that particular amino acid.

Codons and anticodons:

o ●  Translation depends on complementary base pairing between mRNA

codons and tRNA anticodons.

o ●  Ribosomes act as the binding site for both mRNA and tRNA. They catalyse

assembly of polypeptide.

o ●  Translation follows the following process:

o mRNA binds to small subunit.

o tRNA binds to ribosome. Has anti codon complementary to first

mRNA codon.
o 2nd tRNA binds. Maximum of two tRNA can be bound to a ribosome

at one time.
o Amino acids from first tRNA goes to second tRNA and joins by a

peptide bond. 2nd tRNA carries dipeptide.

o Ribosome moves along mRNA and tRNA is removed leaving one

space for new tRNA molecule.

o Similar process continues until a stop codon is reached.
o Polypeptide is released and ribosome complex breaks down.

Human insulin production:

o ●  Occurs in bacteria and is a manifestation of how universal the genetic

code is; allowing gene transfer between species.

o ●  Human insulin is produced synthetically using E. coli bacteria.

o ●  Gene that codes for insulin production is transferred to bacteria.
o ●  Transcription and translation then occur to produce harvestable
 quantities of bacteria.

o ●  Earlier bovine insulin was used. Despite slight genetic difference they still

bound to insulin receptors properly.

2.8 Cell Respiration:

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Cell respiration:

o ●  Controlled release of energy from organic compounds to produce ATP.

o ●  ATP from cell respiration is immediately available as a source of energy in

the cell.

o ●  The 3 main ATP-requiring activities are:

o Synthesising large molecules: DNA, RNA proteins.

o Pumping molecules/ions across membranes: active transport. o Moving things
around in a cell/ muscle contraction.

● ATP is used by splitting ATP into ADP + P. This is an exothermic reaction and
releases energy. This energy is used by cells and then converted into heat energy,
which is not reusable/recyclable. As a result all energy is eventually lost to the
environment, thus creating a continuous need to obtain energy through ingestion
and then respiration.

Anaerobic respiration:

o ●  Gives a small yield of ATP from glucose, which is broken down without

oxygen.

o ●  Required when a short burst of ATP is needed.

o ●  When oxygen supplies are internally low and in oxygen deficient

environments.

o ●  In humans, glucose is converted into lactic acid. However in yeast and

plants it converts to ethanol and carbon dioxide. Both lactate and ethanol are
toxic.
 Use of yeast in baking:

o ●  Release of carbon dioxide due to anaerobic respiration causes lighter

texture in bread.

o ●  Carbon dioxide cannot escape and forms bubbles.

o ●  Ethanol evaporates during baking.
o ●  Bioethanol is produced by Yeast converting sugar into ethanol. Only

sugars, mono/di saccharides can be converted. This is an enzyme- catalysed

reaction. This ethanol is distilled and can be used in vehicles.

Lactate production in humans:

o ●  Used to maximise the power of muscle contractions.

o ●  ATP is created anaerobically when the body requires quick powerful

movements.

o ●  Weight lifters, short distance runners are examples of sportsmen who

anaerobically respire during their events.

o ●  Muscles cannot tolerate lactate past a certain extent. It results in oxygen

debt and so must be broken down.

Aerobic respiration:

 ●  Requires oxygen and produces large yield of ATP from glucose.

Over 30

ATP produced from a single glucose molecule.

 ●  Molecules of ATP per molecule of glucose.

 ●  Glucose + Oxygen => Carbon Dioxide + Water.
 ●  Most of the reactions happen inside the mitochondria.

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2.9 Photosynthesis:
Photosynthesis:
● Production of carbon compounds in cells using light energy.
Photosynthesis is an example of energy conversion. Light energy is converted to
chemical energy in carbon compounds. Produces carbohydrates, proteins and lipids.

Wavelengths of light:

o ●  Visible light has a range of wavelengths with violet the shortest and red

the longest. This is the spectrum of electromagnetic radiation.

o ●  Visible light ranges between 400-700 nm. Sunlight is a mixture of

different wavelengths.

Light absorption by Chlorophyll:

o ●  Absorbs red/blue light. Reflects green light.

o ●  When drawing an action spectrum for photosynthesis or an absorption

spectrum for chlorophyll, the x-axis should be from 400-700 nm.

o ●  For an action spectrum, the y-axis should be ‘relative rate of

photosynthesis’ from 0-100%.

o ●  On an absorption spectrum the y-axis should be ‘% absorption’ from 0-

100%.

Oxygen production in photosynthesis:

o ●  Caused by photolysis of water. Light energy splits molecules of water to

release electrons needed in other stages.

o ●  2H2O => 4e-+4H++O2. Oxygen is therefore a waste product and diffuses

away.

Effects of photosynthesis on Earth:

o ●  Changes to Earth’s atmosphere, oceans and rock deposition due to

photosynthesis.

o ●  Causes rising oxygen concentration in atmosphere, known as the Great

 Oxidation Event.

o Glaciation occurred due to reduction of greenhouse effect – fall in

RIP BIO CLASS OF 2K17

methane and carbon dioxide concentrations.

o Oxidation of iron deposits in the water result in precipitation on

the sea-bed called banded iron formation – iron ores.

Production of Carbohydrates:

o ●  Energy is needed to produce carbohydrates and other carbon compounds

from carbon dioxide.

o ●  Endothermic reaction to make carbohydrates from carbon dioxide. This

energy is derived from light absorption.

o ●  Light energy is therefore converted to chemical energy.

Limiting factors:

o ●  Temperature, light intensity and carbon dioxide concentrations.

o ●  Can limit photosynthesis if below the optimal level.
o ●  Under any combination of limiting factors only one actually limits the rate

of photosynthesis: the one furthest from its optimum.

o ●  In order to test for effects of limiting factors, two will have to be constant

by controlling them. The third would be the independent variable and would
change by stead increments.

3 Genetics
3.1 Genes
What is a gene?

o ●  A gene is a heritable factor that consists of a length of DNA and influences

a specific characteristic.

o ●  Genes consist of a much shorter length of DNA than a chromosome and

each chromosome carries many genes.

Comparing numbers of genes

o ●  E. coli has 3200 genes. Gut bacterium. Prokaryote group.

o ●  T. vaginatis has 60,000 genes. Unicellular parasite. Protoctista group.
o ●  S cerevisiae has 6,000 genes. Unicellular fungus. Fungi group.
o ●  O. sativa has 41,000 genes. Rice. Plant group.
o ●  H. sapiens has 23,000 genes. Humans. Animal group.