EDEXCEL: AS BIOLOGY

REVISION NOTES: UNIT 1

Specification
Topic 1: Lifestyle, health and risk

1. Demonstrate knowledge and understanding of the practical and investigative skills

identified in numbers 4 and 5 in the table of How Science Works on page 12 of this
specification.

2. Explain the importance of water as a solvent in transport, including its dipole nature.

3. Distinguish between monosaccharides, disaccharides and polysaccharides (glycogen

and starch – amylose and amylopectin) and relate their structures to their roles in
providing and storing energy (β-glucose and cellulose are not required in this topic).

4. Describe how monosaccharides join to form disaccharides (sucrose, lactose and

maltose) and polysaccharides (glycogen and amylose) through condensation reactions
forming glycosidic bonds, and how these can be split through hydrolysis reactions.

5. Describe the synthesis of a triglyceride by the formation of ester bonds during

condensation reactions between glycerol and three fatty acids and recognise
differences between saturated and unsaturated lipids.

6. Explain why many animals have a heart and circulation (mass transport to overcome
limitations of diffusion in meeting the requirements of organisms).

7. Describe the cardiac cycle (atrial systole, ventricular systole and diastole) and relate
the structure and operation of the mammalian heart to its function, including the
major blood vessels.

8. Explain how the structures of blood vessels (capillaries, arteries and veins) relate to
their functions.

9. Describe how the effect of caffeine on heart rate in Daphnia can be investigated
practically, and discuss whether there are ethical issues in the use of
invertebrates.

10. Describe the blood clotting process (thromboplastin release, conversion of

prothrombin to thrombin and fibrinogen to fibrin) and its role in cardiovascular
disease (CVD).

11. Explain the course of events that leads to atherosclerosis (endothelial damage,
inflammatory response, plaque formation, raised blood pressure).

12. Describe the factors that increase the risk of CVD (genetic, diet, age, gender, high
blood pressure, smoking and inactivity).

13. Describe the benefits and risks of treatments for CVD (antihypertensives, plant
statins, anticoagulants and platelet inhibitory drugs).
14. Analyse and interpret data on the possible significance for health of blood cholesterol
levels and levels of high-density lipoproteins (HDLs) and low-density lipoproteins
(LDLs). Describe the evidence for a causal relationship between blood cholesterol
levels (total cholesterol and LDL cholesterol) and CVD.

15. Discuss how people use scientific knowledge about the effects of diet (including
obesity indicators), exercise and smoking to reduce their risk of coronary heart
disease.

16. Describe how to investigate the vitamin C content of food and drink.

17. Analyse data on energy budgets and diet so as to be able to discuss the consequences
of energy imbalance, including weight loss, weight gain, and development of obesity.

18. Analyse and interpret quantitative data on illness and mortality rates to determine
health risks (including distinguishing between correlation and causation and
recognising conflicting evidence).

19. Evaluate design of studies used to determine health risk factors (including sample
selection and sample size used to collect data that is both valid and reliable).

20. Explain why people’s perceptions of risks are often different from the actual risks
(including underestimating and overestimating the risks due to diet and other lifestyle
factors in the development of heart disease).
Topic 2: Genes and health

1. Demonstrate knowledge and understanding of the practical and investigative skills

identified in numbers 4 and 5 in the table of How Science Works on page 12 of this
specification

2. Explain how models such as the fluid mosaic model of cell membranes are
interpretations of data used to develop scientific explanations of the structure and
properties of cell membranes

3. Explain what is meant by osmosis in terms of the movement of free water molecules
through a partially permeable membrane (consideration of water potential is not
required).

4. Explain what is meant by passive transport (diffusion, facilitated diffusion), active

transport (including the role of ATP), endocytosis and exocytosis and describe the
involvement of carrier and channel proteins in membrane transport.

5. Describe how membrane structure can be investigated practically, e.g. by the

effect of alcohol concentration or temperature on membrane permeability.

6. Describe the properties of gas exchange surfaces in living organisms (large surface
area to volume ratio, thickness of surface, difference in concentration) and explain
how the structure of the mammalian lung is adapted for rapid gaseous exchange.

7. Describe the basic structure of an amino acid (structures of specific amino acids are
not required) and the formation of polypeptides and proteins (as amino acid
monomers linked by peptide bonds in condensation reactions) and explain the
significance of a protein’s primary structure in determining its three-dimensional
structure and properties (globular and fibrous proteins and types of bonds involved in
three-dimensional structure).

8. Explain the mechanism of action and specificity of enzymes in terms of their three-
dimensional structure and explain that enzymes are biological catalysts that reduce
activation energy, catalysing a wide range of intracellular and extracellular reactions.

9. Describe how enzyme concentrations can affect the rates of reactions and how
this can be investigated practically by measuring the initial rate of reaction.

10. Describe the basic structure of mononucleotides (as a deoxyribose or ribose linked to
a phosphate and a base, i.e. thymine, uracil, cytosine, adenine or guanine) and the
structures of DNA and RNA (as polynucleotides composed of mononucleotides
linked through condensation reactions) and describe how complementary base pairing
and the hydrogen bonding between two complementary strands are involved in the
formation of the DNA double helix.

11. Describe DNA replication (including the role of DNA polymerase), and explain how
Meselson and Stahl’s classic experiment provided new data that supported the
accepted theory of replication of DNA and refuted competing theories.
12. Explain the nature of the genetic code (triplet code only; non‑overlapping and
degenerate not required at IAS).

13. Describe a gene as being a sequence of bases on a DNA molecule coding for a
sequence of amino acids in a polypeptide chain.

14. Outline the process of protein synthesis, including the role of transcription,
translation, messenger RNA, transfer RNA and the template (antisense) DNA strand
(details of the mechanism of protein synthesis on ribosomes are not required at IAS).

15. Explain how errors in DNA replication can give rise to mutations and explain how
cystic fibrosis results from one of a number of possible gene mutations.

16. Explain the terms gene, allele, genotype, phenotype, recessive, dominant, homozygote
and heterozygote, and explain monohybrid inheritance, including the interpretation of
genetic pedigree diagrams, in the context of traits such as cystic fibrosis, albinism,
thalassaemia, garden pea height and seed morphology.

17. Explain how the expression of a gene mutation in people with cystic fibrosis impairs
the functioning of the gaseous exchange, digestive and reproductive systems.

18. Describe the principles of gene therapy and distinguish between somatic and germ
line therapy.

19. Explain the uses of genetic screening: identification of carriers, preimplantation

genetic diagnosis and prenatal testing (amniocentesis and chorionic villus sampling)
and discuss the implications of prenatal genetic screening.

20. Identify and discuss the social and ethical issues related to genetic screening from a
range of ethical viewpoints.
Metabolism
Metabolism is a term to describe all reaction which is taking place within a cell and is
separated into two types which are
• anabolic - compounds being built up
• catabolic - compounds being broken down

Water
The water molecule is a molecule which is made up from 2 hydrogen atoms and 1 oxygen
atoms (H2O). It is bounded by 2 covalent bonds and has is polar. The reason why water
molecules are important for living organisms are because:
1. They are important solvents since they are polar
2. Important coolants for excessive metabolic reactions
3. Important for insulation since they have high specific heat capacities, minimise
temperature fluctuations in living things
4. It is a very good mechanism for transport since they are highly cohesive
5. Important reagents for chemical reactions (such as hydrolysis and photosynthesis)

Carbohydrates
Separated into 3 types which are monosaccharides, disaccharides and polysaccharides

Monosaccharides
• there are three main types of monosaccharides which you have to know in this level which
are
1. Pentoses - Such as ribose (with formula C5H10O5) and fructose
2. Hexose - Such as alpha and beta glucoses
•All members of monosaccharides are reducing since they have the aldehyde groups,
therefore they will cause a brick red precipitate to form when tested with Benedict’s solution

Disaccharides
• You would need to know 3 types of disaccharides in this level which is
1. Lactose - Formed between glucose and galactose and is bounded by 1,4-glycosidic
bonds (found in milk)
2. Maltose - Formed by 2 molecules of glucose and is bounded by 1,4-glycosidic bonds
(found in starch after being hydrolysed)
3. Sucrose – Formed by a molecule of glucose and a molecule of fructose bounded by
1,2-glycosidic bonds (Found in most plant since it is used to transport sugary
compounds)
• The formation of bonds between 2 monosaccharides is called condensation and the Commented [JC1]: a chemical reaction where 2 molecules
breakage of these bonds are called hydrolysis. Hydrolysis of these bonds can be brought are joined together by a covalent bond to make a larger,
more complex, molecule, with the loss of a small molecule.
about by adding dilute HCl.
• Both lactose and maltose are reducing but sucrose is not a reducing sugar. Therefore,
disaccharides can or cannot be reducing.

Disaccharides are not always reducing sugars.

Polysaccharides
• There are three types of polysaccharides that we need to know at this level which are

1. Starch
• A polymer of alpha glucose and is bounded by 30% amylose (1,4-glycosidic bonds, straight
chained) and 70% amylopectin (both 1,4 and 1,6-glycosidic bonds, branched)
• It is used as a food storage for plants and is built from the amyloplasts in the cytoplasm of
plant cells.
•Starch is an important storage molecule since it is compact, insoluble in water, inert to
chemical reactions and is easily hydrolysed when required.

2. Glycogen
• A polymer of alpha glucose with 1,4-glycosidic bonds but even more 1,6-glycosidic bonds
compared to starch since it is even more branched.
• It is used as an energy store in animals and is also found in bacteria
• Glycogen is an important storage molecule since it is compact, insoluble in water, inert to
chemical reactions and is easily hydrolysed when required.

3. Cellulose
• A polymer of beta glucose and is by only 1,4-glycosidic bonds. Therefore, it is not branched
but arranged in a matrix which is bounded by hydrogen bonds
• It is the constituent of cell walls and can be hydrolysed by ruminant animals by the action of
cellulase enzymes.

All polysaccharides are non-reducing sugars.

Lipids
• Lipids are basically fats and oil that contain elements of carbon, hydrogen and oxygen

Triglyceride
•An example of a lipid would be the triglyceride which is formed by glycerol and fatty acids. Commented [JC2]: • There are two types of fatty acids
The bond formed is catalysed by the process of condensation between the –OH groups of the which are unsaturated and saturated fatty acids.
• An example of a saturated fatty acid would be stearic acid
glycerol and the fatty acids. The bonds formed between them are the ester bonds. Since and unsaturated would be the oleic acid.
triglyceride itself is an ester. • The difference between saturated and unsaturated fatty
• The usages of triglycerides are important energy stores, compact, insoluble in water, acids are the double bonds and the amount of hydrogen
present at where saturated acids have more hydrogen and no
releases energy twice the amount of carbohydrates, and provides buoyancy for aquatic double bond present.
animals. • The usages of fatty acids include the formation of
triglycerides and is also required for the formation of
phospholipids.
Phospholipids
•Formed between fatty acids, glycerol and a phosphate group.
•The head is hydrophilic (soluble in water) but the tail is hydrophobic (insoluble in water).
•Therefore, phospholipids are used as the main constituents of cell membranes
Protein
Primary structure
• It is the number, type and sequence of amino acids which makes up a polypeptide chain
Each amino acid is bonded to another acid by peptide bonds by the process of condensation.
Amino acid is amphoteric since it has a zwitterion shape.

Secondary structure
• It is the shape of molecule formed when polypeptide chains are either coiled by hydrogen
bonds into a spiral spring, the alpha helix or linked to form beta pleated sheets Commented [JC3]: • The alpha helix coils the polypeptide
•Insoluble in water. chains and are help in place by hydrogen bonds. An example
of this would be keratin.
Commented [JC4]: • The beta pleated sheets are formed by
Tertiary structure hydrogen bonds taking place between the CO and NH
• It is the folding of a polypeptide to form a globular shape. groups. It is very strong but supple. An example would be
collagen since it is fibrous.
• R groups of these proteins are bounded by ionic bonds, disulphide bridges and hydrogen
bonds.
• An example would be enzymes.

Quaternary structure
• A complex protein molecule which has more than one polypeptide chains bounded to it.
•An example would be haemoglobin.

Explain how the primary structure of protein will determine its 3-dimensional structure
1. primary structure is the sequence of amino acids
2. primary structure determines positioning and types of bonds
3. between R-groups
4. affects the folding/ secondary structure/tertiary structure

Lipoproteins
Cholesterol is a soluble lipid made in the body and is transported by proteins in soluble
complexes called lipoproteins consisting of proteins and lipids. There are two types of
lipoproteins:

High-density lipoprotein
‘good’ cholesterol
• Formed from unsaturated fats, protein and cholesterol and transports cholesterol from body
tissues to the liver where it is broken down
• reduces the cholesterol levels and reduce the risk of atherosclerosis.

Low-density lipoprotein
‘bad’ cholesterol
• Formed from saturated fats, protein and cholesterol and transports cholesterol from the liver
to the blood, thus causing the cholesterol level to increase, hence why it is linked to
atherosclerosis.

There is a correlation between high levels of saturated fats and high blood cholesterol as
saturated fats are one of the components of low-density lipoproteins. However, the link
between cholesterol and cardiovascular diseases is causal because cholesterol is involved in
plaque formation.
Enzymes
• Enzymes are basically tertiary proteins which have an active site which binds onto a
substrate. The reaction causes bonds to be formed and broken much easier. This is because
enzymes act as organic catalysts which reduces the activation energy needed for a reaction
to go forward.
• When the enzyme and substrate form a complex, the structure of the enzyme is distorted.
so that the active site of the enzyme fits around the substrate. This is called the induced fit
hypothesis. Initial rate of reaction can be measured by calculating the gradient of a
concentration-time graph.

1. Globular proteins
2. Primary structure → secondary structure
3. Hydrophobic (inside) & Hydrophilic group (outside)
4. H bonds, ionic bonds, covalent bonds and polar interactions hold the R side chains
5. Each enzyme has a very specific, individual active site shape. Very few amino acids
form the actual active site. Specific - catalyse the reactions also specific. Commented [JC5]:
Commented [JC6]: 1.Enough substrate to saturate the
• The process is summarized as below: enzymes
Enzyme + Substrate  enzyme-substrate complex  enzyme + products 2.Substrate is not a limiting factor
3.As reaction proceeds, substrate decreases, the rate of
reaction also decreases a lot.
Factors affecting rate of enzyme reaction 4.Substrate concentration should be kept constant.
5.The highest reaction rate gives the maximum possible
1. Temperature reaction rate for an enzyme under a particular situation.
a. The increase in temperature would increase the total kinetic energy of the
substrate and enzyme, thus the rate of collision increases and the rate of
reaction increases. The opposite is shown if the temperature is reduced
2. pH
a. The decrease in pH would lead to excess H+ ions which will ionize the side
groups in the enzyme’s amino acids residue. This would lead to a change in its
molecular structure and cause the enzyme’s active site to be not
complementary to the substrate anymore. Thus, lower the pH, the more
ionization and a less rate of reaction.
3. Enzyme and Substrate concentration
a. The increase of any of the substrate or concentration would lead to a higher
rate of collision and thus increases the rate or reaction
4. Inhibitors
a. There are two types of inhibitors which are reversible inhibitors and non-
reversible inhibitors:
b. An irreversible inhibitor are inhibitors which has a shape which is
complementary to the active site of an enzyme and therefore competes with
the substrate for a reaction to proceed. This decreases the rate of reaction
c. A non-competitive inhibitor is inhibitor, this is usually heavy metals which
binds on to the enzyme and causes the enzyme to change its shape and loses
its catalytic abilities. Therefore, the rate of reaction is reduced
Usages of enzymes

Cellulase
• Catalyses the breakage of cellulose into beta glucose
• Uses include the production of single cell protein and saccharification (sweetening)

Amylases
• Catalyses the hydrolysis of glycosidic bonds in starch into alpha glucose
• Uses includes the clarification of fruit juices and sweetening of fruit juices.

Protease
• Catalyses the breakage of protein into amino acids
• Used for the clarification of beer, biological detergents and the tenderisation of meat.

Lactase
• Catalyses the breakage of lactose into glucose and galactose
• Uses includes sweetening, production of lactose free milk and the production of
immobilized enzymes

Lipase
• Catalyses the breakage of lipids into glycerol and fatty acids
• Uses includes the enhancement of cheese ripening and biological detergents.

2014 Jun Explain why a gene mutation can result in an enzyme that is unable to break down
lipids.
1. There is a change in sequence of a gene.
2. Change in amino acids, change in primary structure of the enzyme.
3. Different R groups lead to different types / position of bonding
4. Change in folding different 3D structure
5. Change in shape / properties of active site
6. Substrate cannot fit in the enzyme’s active site.

Experimental tests
• Bear in mind that most of the unit 1 tests has at least 1 biological test question which can
yield up to 5 points and these tests should not be neglected.

Benedict test
• Test to confirm reducing properties of sugars.
• Add a few drops of benedict solution into the sugar and boil. If it shows a brick red
precipitate, a reducing sugar is present. Since Cu2+ is reduced to Cu+ which shows are brick
red precipitate Cu2O

Biuret test
• Test to confirm the presence of protein.
• Add an equal amount of protein and biuret reagent. A purple-violet colour would confirm
the presence of proteins. This can be used as a qualitative test since the colour gets more
intense as the protein content increases.
Emulsion test
• To test the for the presence of lipid
• the test substance is mixed with 2 cm3 of ethanol, an equal volume of distilled water is
added, a milky-white emulsion forms if the test substance contains lipids.

Sudan III test

• To test the for the presence of fat
• Add equal amount of Sudan III and fat contents together. A suspension of red liquid and
white precipitate on the top would confirm that there is fat present.

Need for heart and circulatory system

In order to survive, animals require essential substances (e.g. oxygen, carbon dioxide) to
enter and leave the body in sufficient quantities and be transported around the body. The
needs of small organisms use open circulation:
1. Large surface area: volume ratio
2. All cells are very close to the heart
3. Diffusion
4. Low metabolism
5. Movement of blood is fast enough

However, as the size of the organism increases:

• Surface area to volume ratio decreases
• Diffusion distance increases, not enough
• Mass flow of glucose and amino acid Commented [JC7]: A system of transport that uses a fluid,
• High metabolic rate which is moved by a pressure gradient. Substances to be
transported are suspended or dissolved in the fluid and all
move in one direction.
Diffusion becomes insufficient. As a result of that, larger organisms have a mass
transport system, consisting of heart and circulation, which moves the substances
around the body and allows exchange of substances to take place.

Features of a mass transport system:

• Vessels
• Directional
• Transport medium
• Maintenance of speed

Double circulation allows effective gas exchange

1. One side of the heart pumps blood to the lungs, the other pumps blood to rest of body
2. Oxygenated and deoxygenated blood is separated.
3. Steep concentration gradient is maintained in lungs/alveoli and tissue
4. Lower pressure in the pulmonary side, protects alveoli capillary network
5. Higher pressure in systemic circuit allows rapid supply of oxygen to body cells

Heart and Cardiac Cycle

• Four chambers - right and left atria, right and left ventricles

Commented [JC8]:
• Four main blood vessels - pulmonary vein (from lungs to left atrium), aorta (from left
ventricle to body), vena cava (from body to right ventricle), pulmonary artery (from right
atrium to lungs)
• Atrioventricular valves - mitral or tricuspid/bicuspid - separate atria from ventricles
• Semilunar valves - pulmonary/aortic – separate arteries from ventricles
• Tendinous chords/valve tendons – prevent atrioventricular valves turning inside out due to
pressure
• Septum - muscle and connective tissue - prevents oxygenated/deoxygenated blood mixing
• Coronary artery - wrapped around the heart to supply blood to cardiac muscle
• Cardiac muscle - thicker on the LHS because higher pressure is needed to pump blood
further

There are 3 stages of the cardiac cycle:

1. Atrial systole – during atrial systole the atria contract. This forces the
atrioventricular valves open and blood flows into the ventricles.
2. Ventricular systole – contraction of the ventricles causes the atrioventricular valves
to close and semilunar valves to open, thus allowing blood to leave the left ventricle
through the aorta and right ventricle through the pulmonary artery.
3. Cardiac diastole – atria and ventricles relax and pressure inside the heart chambers
decrease. The causing semilunar valves in the aorta and pulmonary arteries close,
preventing backflow of blood.

Electrical Activity of Heart

Commented [JC9]:
• Myogenic, Intrinsic rhythmicity

SAN  Atrial systole  AVN Bundle of His  Purknye fibre  Ventricular systole

1. SAN (sinoatrial node) sets up wave of electrical excitation (depolarisation) which causes
atrial systole.
2. Excitation spreads to Atrioventricular node. Commented [JC10]: There is a slight delay before the AVN
3. Wave of depolarisation passes into the bundle of His. reacts, to make sure the ventricles contract after the atria
have emptied.
4. Bundle of His carries the excitation down along Purknye tissue.
5. As the depolarisation spreads down, it sets off ventricular systole, starts at the bottom,
squeeze blood out of the heart.

2019 Jan (2, 3), 2018 Jun (3), 2018 Jan (1)

Blood Vessels Commented [JC11]: Type of tissues:

1.Endothelium: reduce friction
Arteries 2.Smooth muscle: contracts
3.Elastic tissue: to stretch and recoil (elastic recoil)
• Carry oxygenated blood to the body tissues (other than the pulmonary artery)
• Have a small lumen to maintain high blood pressure
• Endothelium (folded membrane, allow expansion, protects against damage, and provides a
smooth surface so
there is less resistance to blood flow)
• Thick layer of smooth muscle (contract and relax to dilate and constrict blood vessels)
• Elastic fibres (stretch and recoil)
• Collagen fibres (for strength and support, maintain pressure)
Veins
• Carry deoxygenated blood to the lungs (except the pulmonary vein)
• Large lumen
• Endothelium
• Thinner layer of muscle and elastic fibres
• Collagen fibres
• Valves (to prevent backflow)

Capillaries
• Lumen
• Endothelium (to maintain short diffusion distance and fit between cells)
2018 Oct (6c)

Blood Clotting
Thrombosis also known as blood clotting prevents blood loss when a blood vessel is
damaged, it also prevents the entry of disease-causing microorganisms and provides a
framework for repair.

A series of reactions which lead to clot formation:

• When a blood vessel is damaged, platelets attach to exposed collagen fibres
• A protein called thromboplastin is released from platelets and this protein triggers the
conversion of inactive prothrombin which is a protein into active thrombin which is an
Commented [JC12]:
enzyme. In order for the conversion to occur calcium ions and vitamin K must be present
• Thrombin catalyses the conversion of soluble fibrinogen into insoluble fibrin Commented [JC13]: Both are globular protein
• Fibrin forms a network of fibres (mesh) in which platelets, red blood cells and debris are Soluble fibrinogen – hydrophilic group outside
trapped to form a blood clot Insoluble fibrin – hydrophobic group outside

2018 Jun (8) Fibrinogen  fibrin

1. Protease breaks bonds in fibrinogen to produce fibrin
2. Fibrin is hydrophobic
3. Causing fibrin to stick together, forming a mesh

Atherosclerosis
Atherosclerosis is the hardening of arteries caused by the build-up of fibrous plaque called an
atheroma. Atheroma formation is the cause of many cardiovascular diseases and occurs as
following:
1. Damage to the endothelial lining of the artery, for instance by high cholesterol
levels, smoking or high blood pressure
2. This causes the inflammatory response. The white blood cells arrive at the site, the
cells accumulate low density lipoprotein (bad cholesterol). This forms the atheroma
3. Fibrous tissues and Calcium salts are also laid with the atheroma, results to hardened
plaque

• The build-up of fibrous plaque leads to narrowing of the artery and restricts blood flow thus
increasing the blood pressure which in turn damages the endothelial lining and the process is
repeated
Impact
1. Narrowing of lumen
2. Loss of elasticity
3. Raise blood pressure
4. Blood clot (thrombus) may form within vessel
5. Embolus is a blood clot that has broken away from a clot, may sweep into smaller
artery, causing complete blockage
6. Self-perpetuating (positive feedback)

Risk Factors for CVD

Atherosclerosis is multi-factorial and has modifiable and non-modifiable risk factors:
• Genetics (genetic predisposition to high blood pressure etc.)
• Age (arteries become less elastic with age)
• Diet (diet can increase cholesterol)
• Gender (oestrogen makes arteries more elastic)
• High blood pressure (can damage endothelium)
• High cholesterol levels
• Smoking (nicotine narrows arteries)
• Physical inactivity (increases obesity risk)
• Obesity (increases blood pressure etc.)

Thus, risk of CVD can be reduced by stopping smoking, regular exercise, reducing
consumption of alcohol, dietary changes and maintaining healthy bodyweight.
Atherosclerosis can cause angina, stroke, myocardial infarction and aneurism.

Treatments for CVD

Drug Treatment Mode of action Risk/ side effects
Diuretics Increase volume of urine, Nausea, muscle cramp,
thus lowers blood pressure dizziness
and volume
Beta blockers Make heart contraction less Increase risk of diabetes
frequent and less powerful
by blocking response of
heart to hormones
ACE inhibitors reduce blood pressure by Dizziness, cough, heart
blocking production on arrhythmia, impaired kidney
angiotensin converting function
enzyme which causes
arterial constriction
Statins lower levels of cholesterol in Nausea, inflammation,
blood by blocking enzyme diarrhoea and constipation
which produces cholesterol
in liver Some stop healthy diet
Anticoagulants reduce risk of clot formation Uncontrolled bleeding
e.g. warfarin (dosage must be carefully
controlled)
 Platelet inhibitory drugs make platelets less sticky, Irritates stomach lining,
e.g. aspirin thus reduce risk of blood cause stomach bleeding
clots and atheroma
formation
Antihypertensives

Energy Balance
Energy balance is the balance of calories consumed through eating and drinking, compared to
calories burned through physical activity. Therefore, if a greater number of calories is burned
through physical activity than is consumed it leads to weight loss. If fewer calories are
burned than consumed it leads to weight gain. The ways of determining whether an
individual is overweight, underweight or healthy weight include:

• BMI is the body mass index which can be calculated by dividing the body mass in
kilograms by height in metres squared. The value obtained is then compared to a chart, for
instance a value below 20 indicates that the individual is underweight.
• Waist-to-hip ratio can be used to determine how likely a person is to get heart disease based
on the distribution of fat in the body.

Aggregations of cells
An overview of a multicellular organism, where cells make up the entire body. This is as
follows:
Cells  Tissues  Organs  individuals
There are distinct differences between an animal cell and a plant cell. Among the many, they
are:
1. Vacuoles which are found to be much larger in plant cells
2. Chloroplasts which are found more abundantly in plant cells
3. Cell walls are usually present in plant cells

Cell membrane
• The membrane functions as a passage of control for the substances into and out of the cells.
The membrane is not only present on the surface of the membrane but also at the membrane
of organelles (mitochondrion, Golgi apparatus, chloroplast, etc.)
• It follows the fluid mosaic model at where fluid represents the phospholipid molecules
having a fluid arrangement and mosaic represents the random arrangement of proteins,
which moves above the phospholipid bilayer.
• The model shows phospholipids pointing head up. This is because the head section of the
phospholipids is hydrophilic (soluble in water) where else the tail is hydrophobic (insoluble Commented [JC14]:
in water)
• Thus, having to know that, the bilayer only allows non-polar molecules to diffuse through a
concentration gradient. Molecules which are sufficiently small (such as water, oxygen and
carbon dioxide diffuses through the membrane freely regardless of being polar or not. Polar
molecules are only allowed to enter if they are incorporated into a carrier protein at where it
is actively transported into the cell or undergo facilitated diffusion (diffusion using a protein
molecule).
• Glycolipids are also present on the cell surface membrane since it allows cell recognition
and also to promote an immune response; as receptor sites for chemical signals; binding cells
to form tissue Commented [JC15]:
• Carbohydrates and cholesterol functions to reduce the fluidity of the membrane and
maintain its stability to ensure that no leaking occurs (water and ions cannot pass through
easily)
•Proteins which are present can either be intrinsic or extrinsic and is important in maintaining
the stability of the membrane.

How is a phospholipid bilayer formed?

1. Fatty acid chains on phospholipid are hydrophobic
2. And group together
3. Phosphate groups on phospholipid are hydrophilic
4. And associate with water
5. Two monolayers form a bilayer

What is a fluid mosaic model?

1. Phospholipids can move in plasma membrane
2. Proteins randomly inserted in plasma membrane

Transfer across cell membranes

Diffusion
• There are 2 types of diffusion which are facilitated diffusion and simple diffusion.
1. Simple diffusion involves the transfer of molecules across a membrane or barrier
following a concentration gradient.
2. Facilitated diffusion involves the transfer of molecules across a barrier or membrane
following a concentration gradient with the help of a channel protein/ protein
carrier. This is because as the molecules bind on the protein, it changes shape in a
way that it allows the molecule to be detached form the protein and get released into
the cytoplasm of the cell or vice versa. Commented [JC16]:

Osmosis
• It is the process whereby water moved down a water potential across a partially permeable
membrane.

Active transport
• It is a process whereby molecules are moved across a membrane or barrier against the
concentration gradient with the help of a protein carrier and a molecule of ATP.
• The molecules bind on to the protein and ATP releases a phosphate group to the protein
which alters the protein shape for it to release its contents against the concentration gradient.

Bulk transport
 Move large quantities of materials in and out.
 Endocytosis Commented [JC17]:

 Exocytosis
 Membranes can easily fuse, separate and pinch off forming vesicles.
 ATP
 pinocytosis: liquid materials

Commented [JC18]:
Gas Exchange
The rate of gas exchange by diffusion becomes more rapid as:
• Surface area of the surface increases
• Diffusion distance decreases
• Diffusion gradient becomes more steep

Fick’s Law is used to determine the rate of diffusion and it state that the larger the surface
area, difference in concentration and shorter the diffusion distance the quicker the rate.
Commented [JC19]:

In mammals, lungs are adapted for rapid gas exchange in the following ways:
• They have a large surface area due to the presence of many alveoli which increase
the surface area
• Good supply of circulating blood to the lungs which carries carbon dioxide to the
lungs and oxygen away from them ensure that the concentration gradient is steep –
high concentration of oxygen and low concentration of carbon dioxide is maintained
by breathing
• They have a short diffusion distance as the alveoli are just one cell thick thus
reducing the diffusion distance

Nucleic acids
• A nucleotide is made up of a pentose sugar, and organic nitrogenous base and a
phosphoric acid
• It is formed between the condensation of a nucleotide and a phosphate molecule
• Bonds which link a phosphate group to another phosphate group in a nucleotide is called the
phosphodiester bond and the bond which links the phosphate and the nucleotide is the
phospho-ester bonds.
• There are 2 types of ribonucleotides which are RNA (the one containing ribonucleotides)
and DNA (the one containing the deoxyribonucleotides) Commented [JC20]:
• There are two types of purines (Adenine, Guanine) and three types of pyrimidines (Uracil, Commented [JC21]: Only in RNA
thymine and cytosine)

Mononucleotides
DNA
• Bases:
- Purine (two nitrogen-containing rings): adenine, guanine
- Pyrimidine (one nitrogen-containing rings): cytosine, thymine
• Pairing:
- A-T - C-G
• Sugar: deoxyribose (hydroxyl group replaced by hydrogen on Carbon-2)
• Bonding:
- Phosphodiester bonds between phosphate group and Carbon-5
- Hydrogen bonds between the bases
- Hydrogen bonds holding the structure together
• Structure: double-stranded, alpha double helix with a sugar-phosphate backbone on each
strand
Commented [JC22]:
mRNA
• Bases:
 - Purine: adenine, guanine
- Pyrimidine: cytosine, uracil
• Pairing:
- A-U - C-G
• Sugar: ribose
• Bonding: same as DNA
• Structure: single-stranded, not usually folded, carries codons which attach to tRNA via
hydrogen bonds

tRNA
• Bases, pairing, sugar, bonding: same as mRNA
• Structure: single-stranded, folded into a specific pattern held together by hydrogen bonds,
carries anticodons which attach to mRNA via hydrogen bonds.

DNA replication
• Replication of DNA is semi-conservative, which means that the original DNA strand is Commented [JC23]: Each new daughter DNA
reused to form new double stranded DNA. molecules contain 1 strand from the original DNA
Half of the original DNA molecule is conserved

Meselson – Stahl Experiment

1. Originally grew DNA in a culture containing 15-N for several generations, so all the
bases contained this isotope.
2. They then grew the DNA in a culture of 14-N for one generation. After this
generation, the DNA contained one strand containing 15-N and one strand containing
14-N.
3. After another generation, half of the DNA molecules were the same as in previous
generation, and the other half contained entirely 14-N (where the 14-N strand from
generation one had been used as a template).

Process of DNA replication

1. DNA helicase unwinds the double stranded DNA by breaking the hydrogen bonds
between complementary bases
2. One of the strands is used as the template and complementary base pairing occurs
between the template strand and free nucleotides. (A-T, C-G)
3. Adjacent nucleotides are joined by phosphodiester bonds formed in condensation Commented [JC24]:
reactions, catalysed by DNA polymerase.
• In the end, there will be two identical strains of DNA formed as a result.
• This is important in cell divisions of mitosis and meiosis

Genetic Code
• The order of bases on DNA is called the genetic code, which consists of triplets of bases.
Each triplet of bases codes for a particular amino acid and is known as a codon. The amino
acids are then joined together by peptide bonds and form a polypeptide chain.
• Therefore, a gene is a sequence of bases on a DNA molecule coding for a sequence of
amino acids in a polypeptide chain. However, not all of the genome codes for proteins – the
non-coding sections of DNA are called introns and the coding regions are called exons.
(RNA splicing)

Commented [JC25]:
Features of the genetic code:
• The genetic code is non-overlapping, meaning that each triplet is only read once and
triplets do not share any bases.
• The genetic code is degenerate, meaning that more than one triplet codes for the
same amino acids. Only 20 amino acids are needed in protein synthesis, so more codons than
amino acids.
• The genetic codes contain start and stop codons which either start or stop protein
synthesis.

Protein synthesis
• This process involves the synthesis of protein molecules by using genes found in the DNA
• The process of transcription and translation is assisted by RNA (tRNA, mRNA and rRNA).
They differ in three ways, which are
1. It is single stranded
2. It contains a pentose instead of a deoxyribose
3. The base thymine is replaced by uracil

Transcription: Synthesis of mRNA

• DNA unwinds and hydrogen bonds between base pairs split to separate the two strands.
One is used as template (antisense strand).
• Ribonucleotides are paired with their complement on the template strand: U with A, then
RNA polymerase join them together, forming a strand.
• mRNA formed, leaves the nucleus through pores in the nuclear membrane and pass to
ribosomes in cytoplasm.

Amino acid activation

• The amino acids are activated for protein synthesis by combining with tRNA.
• Forming amino acyl-tRNA.
• tRNA translates a three-base sequence (anticodon) into an amino acid sequence.

Translation
• Ribosome moves along mRNA strand to ‘read’ information of the codons.
• mRNA carries genetic message in the same base sequence language as the DNA
• Each codon of mRNA attracts tRNA with complementary anticodon and specific amino
acid
• Peptide bonds formed between adjacent amino acids. At completion of translation, a
polypeptide chain formed and released from ribosome
• tRNA returns to cytoplasm. Free tRNA molecules are available to bind with their specific
amino acid again

DNA mutation
Mutations are permanent changes in the DNA of an organism. Gene mutations are changes in
the arrangement of bases by:
• Substitution (change in one base)
• Addition (adding another base in)
• Deletion (taking a base out)
This change to the base sequence results in a change to the mRNA, tRNA and therefore to
the primary structure of the protein.

Cystic Fibrosis Commented [JC26]: Normal

(recessive genetic disorder)
For example, cystic fibrosis is a genetic disorder caused by a mutation of a single gene
which codes for the CFTR protein

CFTR is a channel protein which transports chloride ions out and into the mucus. This
channel protein makes the mucus watery as it causes water to move into mucus by osmosis.
Therefore, a mutation in this gene makes the mucus very thick, as a mutant CTFR protein is
less efficient at transporting chloride ions. Sticky and thick mucus causes many problems in
gas exchange, reproduction and digestion. CF

Respiratory system:
• Build-up of mucus in lungs trap bacteria, thus increasing the risk of infection.
• Build-up of mucus in airways decreases the number of alveoli involved exposed to fresh air,
therefore reducing the surface area for gas exchange.
• Lungs damage by coughing are more prone to bacterial infection, phagocytes cannot
destroy bacteria

Reproductive system:
• Cervical mucus prevents sperm from reaching egg.
Commented [JC27]: Cystic Fibrosis Transmembrane
• In men, sperm duct is blocked with mucus, meaning sperm produced cannot leave the Regulatory
testes.

Digestive system:
• The pancreatic duct which connect pancreas to the small intestine can become blocked with
mucus, so the digestive enzymes do not reach the small intestine. As a result, food is not
properly digested, so fewer nutrients are absorbed.
• The mucus lining in the duodenum is very thick, thus reducing the absorption of nutrients.
• Mucus can cause cysts to form in the pancreas and damage the insulin producing cells, thus
leading to diabetes.

2018 Oct (7a) Explain how a mutation in the CFTR gene affects movement of water through
the cell membrane.
1. mutation changes the sequence of amino acids in the CFTR protein
2. leads to a non-functional CFTR protein/ chloride channel
3. chloride ions do not move out of / move into the cell
4. water does not move out of / moves into the cell

2019 Jan (5), 2018 May (6)

Genetics
Keyword:
• Gene - a piece of DNA which has a specific sequence of bases. Each gene codes for a
specific protein.
• Allele - one of the different forms of a particular gene.
• Genotype - all the alleles of an organism.
• Phenotype - the set of observable characteristics of an individual resulting from
the interaction of its genotype with the environment.
• Recessive – an allele that produces a feature if two copies are present.
• Dominant – an allele that produces a feature even if only one copy of the allele is
present.
• Incomplete dominance - a form of intermediate inheritance in which one allele for a
specific trait is not completely expressed over its paired allele. This results in a third
phenotype in which the expressed physical trait is a combination of the dominant
and recessive phenotypes.
• Homozygote - an individual having two identical alleles of a particular
gene.
• Heterozygote - an individual having two different alleles of a particular
gene.

Monohybrid inheritance
is the inheritance of just one characteristic. The image presents a pedigree diagram of
monohybrid cross.

Gene therapy
Insertion of a normal allele of a gene into cells to replace a faulty allele that causes an
inherited disorder.
Commented [JC28]:
Germ line therapy
• affecting gamete-producing cells, can pass genes to next generations.

Somatic therapy Commented [JC29]: Genetic Engineering

• affecting body cells
1. Identify the gene
2. Make copies of normal allele and insert into a vector e.g. liposome / virus
3. Use the vector to insert the allele into the target body cells.

• Problems with current gene therapy

- Only about 25% of normal Chloride transport function is restored.
- Effect is temporary for the epithelial cells are constantly replaced.
- Using virus
- Inefficient delivery

Explain how gene therapy could enable cells lining the lung to function normally in CF
patients. [4]
1. Vector carrying the fundamental gene code for CFTR protein.
2. Arrive to the epithelial lining
3. Gene is expressed. CFTR protein are formed on the cell membrane
4. Allow chloride ions to leave the cell and sodium ions diffuse out.
5. Lowers the water potential along the airway
6. Water moves out by osmosis.
7. Mucus is kept runny.
Genetic Screening
The purpose of genetic screening is to determine if the DNA of an individual contains alleles
for genetic disorders.

DNA testing: identifying carriers

Social and Ethical issues

1. Emotional stress
2. False results lead to incorrect information
3. Other abnormalities may be found
4. Can the results be used by employers / life insurance company, lead to genetic
discrimination

PIGD preimplantation genetic diagnosis

• embryos created through IVF are tested for genetic disorders before they are implanted into
the woman’s uterus.

Social and Ethical issues

1. May be used to find out other characteristics, results to designer babies.
2. False results bring about incorrect information.

Pre-natal screening
 Chronic villus sampling – this test is carried out at 8 to 12 weeks of pregnancy. A
sample of embryonic tissue is taken from the placenta and the DNA is analysed. This
form of testing is quicker than amniocentesis
 Amniocentesis – carried out at 14-16 weeks. A sample of amniotic fluid, which
contains foetal cells, is obtained using a needle. The DNA is then analysed. Results
are available after 2-3 weeks, as foetal cells need to be grown in culture first.

Social and ethical issues

1. may result in a miscarriage / spontaneous abortion
2. risk of false positive / negative / inaccurate result
3. healthy fetus may be aborted
4. killing is wrong / unethical
5. who has right to decide if tests should be performed
6. The outcome of testing might lead to an abortion - right to life.
7. The cost of bringing up a baby with a genetic disorder.
8. Emotional and mental issues surrounding the birth a baby with a disorder.

2018 Oct (7bii) Why prenatal testing for cystic fibrosis is not offered to all pregnant women.
1. the condition is rare / no family history
2. the test is expensive / unavailable
Core Practical Skills
1. Effect of Caffeine on Heart Rate

Why Daphnia?
- Daphnia are small and show the results of the experiment quickly
- They have simple nervous systems so are less likely to feel pain
- They are abundant so easy to get hold of / No damage to environment when a few are
removed from it
- Transparent so easy to measure heartbeat

Controlled variables
- Temperature
- Volume of solution
- Time of acclimatisation
- Daphnia must be the same age / size
- Daphnia must have the same health
- Counting time

Method
- Independent variable: Caffeine concentration
- Dependent variable: Heart rate of Daphnia
- Place a Daphnia in each of 5 different solutions (4 different concentrations of caffeine
and one with distilled water to act as a control)
- Leave Daphnia for 5 minutes to acclimatise
- Immobilize the Daphnia using a little cotton wool in a cavity slide and observe under
microscope
- Count and record the no. of heartbeats in one minute
- Repeat 5 times at each concentration and allow means to be calculated

Outcome
As caffeine concentration increases, heart rate also increases

Reason
Increasing caffeine concentration causes the electrical activity of the sinoatrial node to
increase, making it depolarize. As it depolarizes, the right and left atria contract and the
impulse travels to the atrioventricular node where, after a delay of about 0.13 seconds, the
impulse continues to travel towards the ventricles. This delay ensures that the atria have
finished contracting and ventricles are full. The signal then reaches the Purkyne fibres that
conduct the impulses to the apex of the ventricles where contraction begins and travels
upwards towards the atria.

Caffeine also affects the ventricles, leading to an increase in the rate of contraction and
relaxation of each heartbeat. This means that, as well as beating faster, the heart's individual
beats are associated with an increased cardiac output.
 2. Vitamin C Content of Fruit Juice

Controlled variables
- Mass of fruit / age / source / …
- Time for storage
- Method of juice extraction
- Volume / concentration of juice / DCPIP
- Temperature
- Same end point colour

Method
- Independent variable: Fruit juice
- Dependent variable: Volume of juice required to decolourise 1cm3 of DCPIP
- Put 1cm3 of DCPIP solution into a test tube
- Fill a plastic syringe with juice and add drops to the DCPIP until the blue of the DCPIP
is lost. Record the volume of juice added
- Repeat 5 times for each juice to calculate means
- To calculate the actual Vitamin C concentration, the DCPIP solution must be calibrated.
A solution of known Vitamin C concentration is added to 1cm3 of DCPIP until it is
decolourised and the volume recorded.
- Conc. of Vitamin C in juice = (Con. of Vitamin C solution x Volume of Vitamin C
solution needed to decolourise 1cm3 DCPIP) ÷ Volume of fruit juice needed to decolourise
1cm3 DCPIP

Limitations
- Difficulty in controlling temperature
- End point difficult to judge as needs to be just when blue colour disappears especially in
highly coloured juices
- Some loss of solution when transferring from one beaker to another
- Accuracy of measuring equipment

Storing fruit at low temperatures slows down decay

- Low temperature reduces / prevents growth of microorganisms
- Low temperature reduces activity of enzymes
- Less kinetic energy means fewer collisions / fewer cell divisions

3. Effect of Temperature on Membranes

Factors affecting permeability of the beetroot cell membrane

- Temperature
- Age
- Storage
- Duration
- Prior treatment with solvent
- pH
- Bile salts
Controlled variables
- Source / Species of beetroot
- Age / Size of beetroot
- Volume of water / solution used
- Time left in water or solution
- pH

Method
- Independent variable: Temperature of water
- Dependent variable: % transmission of light through resulting solution
- Using a cork borer and knife, cut 5 pieces of beetroot equal in mass and size
- Rinse the beetroot pieces with water and gently pat them dry with tissue before using
them as, when cutting, pigment is released from broken cells and must be removed before
starting or solutions will be darker than they should
- Place one piece into each of 5 tubes and add 5 1cm3 water to each one
- Place each tube into a water bath of different temperature (e.g. 15, 20, 25, 30, 35)
- Leave for 15 minutes
- Remove beetroot and shake tubes to disperse dye.
- Calibrate the colorimeter using distilled water in a cuvette as a reference / control.
- Take readings of absorbance of the water in the tubes
- Take 5 repeats at each temperature and calculate means

Outcome
As temperature increases, % transmission slightly increases.

Reason
This is due to membrane molecules gaining more heat energy and vibrating more, creating
large gaps in the membrane that enable dye to be released. Proteins in membrane may
become denatured, leaving large pores through which the dye leaks.

Limitations
- Pigment is not equally distributed throughout the beetroot
- Some beetroot may have skin on affecting surface area
- Size of beetroot is difficult to control

4. Effect of Enzyme Concentration on the Rate of Reaction

Controlled variables
- Temperature (use a thermostatically controlled water bath)
- Volume of enzyme
- Volume of substrate
- Concentration of substrate
- pH
Method
- Take 5 test tubes. In 4, place increasing volumes of trypsin solution e.g. (1, 2, 3, 4 cm3)
and make up the volume to 4 cm3 using distilled water. The other test tube should be filled
with 4 cm3 of water to act as a control.
- Add 5 of milk powder (casein solution) as substrate and start the stopwatch
- Measure the cloudiness of the solution over time using a colorimeter (every 30 secs for
10 minutes) against water as a reference / control
- Repeat at least 5 times at each concentration and calculate means

Outcome
· As concentration of enzyme increases, rate of reaction increases up to a point, where all
enzyme has metabolised all substrate immediately

Why do enzymes work better at higher temperatures?

At low temperatures the reaction is slow because the enzyme and substrate molecules don’t
collide very often and move slowly. Increasing temperature increases kinetic energy and so
frequency of collisions. The substrate binds to the enzyme’s active site more often thus
increasing the rate of reaction. After the optimum temperature bonds holding the 3D – shape
of the enzyme together starts breaking so it loses its shape and the enzyme-substrate complex
can no longer form. The enzyme is denatured.

Common Definitions
Gene
Gene mutation
Enzyme
Dominant allele
Recessive allele
Fluid mosaic
Tissue

Common Questions
Double circulation
Artery, Vein Structure
Mammalian lung adaption
Cystic Fibrosis (Prenatal testing)
Cardiac Cycle
Blood clotting
Transcription, translation
DNA Replication
Past Paper
2017 Oct *** (2c scale, 7b family pedigree, 7cii DNA replication)