Emily Summers

AS Unit F212: Molecules, biodiversity, food and health

Module 1 - Biological molecules

Biological molecules
Describe how hydrogen bonding occurs between water molecules, and relate this and other properties of water to the roles of water
in living organisms.

Describe, with the aid of diagrams, the structure of an amino acid.

Structure of an Amino Acid

All amino acids have the same

general structure, a carboxyl group,
an amino group attached to a carbon
atom (-NH2) but the R group is
variable, and that is the only
difference between amino acids.

Structure of Glycine

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Describe, with the aid of diagrams, the formation and breakage of peptide bonds in the synthesis and hydrolysis of dipeptides and
polypeptides.

Condensation reactions make

peptide bonds between amino acids.
A molecule of water is released.

It’s reversible, and by adding a water

molecule you can break the peptide
bonds. This is called hydrolysis.

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Explain, with the aid of diagrams, the term primary structure.

Explain, with the aid of diagrams, the term secondary structure with reference to hydrogen bonding.

Explain, with the aid of diagrams, the term tertiary structure, with reference to hydrophobic and hydrophilic interactions, disulphide
bonds and ionic interactions

Ionic Interactions weak attractions between oppositely charged parts the molecule

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Disulfide Bonds  Two molecules of an amino acid close together, the sulphur atoms in
them bond together forming this bond. (E.g. Cysteine)

Hydrophobic Water repelling groups near together in a protein they clump.

Hydrophilic Water attracting groups are likely to be pushed outside, affecting the
protein’s final structure.

Explain, with the aid of diagrams, the term quaternary structure, with reference to the structure of haemoglobin.

The quaternary structure tends to be determined by

the tertiary, when it involves multiple polypeptides.
E.g. Haemoglobin has a quaternary structure, it has 4
polypeptide chains.

Describe, with the aid of diagrams, the structure of a collagen molecule

Collagen is a strong protein that is fibrous. It is a

supportive tissue in animals; it is made of three
polypeptide chains that are very tightly coiled into a
triple helix, interlinked by covalent bonds. Minerals
are able to bind to this helix to increase rigidity.

 Tendons are made up mostly of collagen

 Walls of arteries contain collagen to prevent
bursting from high pressure blood in them
 Cosmetic treatment for lips for a fuller appearance
Compare the structure and function of haemoglobin (as an example of a globular protein) and collagen (as an example of a fibrous
protein).

Haemoglobin Collagen
Globular protein Fibrous Protein
Large variety of amino acids in it’s primary 35% of primary structure is glycine
structure
Has a prosthetic group- haem Doesn’t contain a prosthetic group
Mostly wound into alpha helix structures Mostly left handed helix structures

Describe, with the aid of diagrams, the molecular structure of alpha-glucose as an example of a monosaccharide carbohydrate.

Monosaccharide carbohydrate, a hexose

sugar because it has six carbon atoms in
every molecule. The structure determines
its solubility so it can be easily
transported. It’s a source of energy for
4 animals and plants. Its chemical bonds
have lots of energy in them.
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State the structural difference between alpha- and beta-glucose.

Describe, with the aid of diagrams, the formation and breakage of glycosidic bonds in the synthesis and hydrolysis of a disaccharide
(maltose) and a polysaccharide (amylose).

Condensation- H2O removed!

Hydrolysis- H2O breaks glycosidic

bond.

Compare and contrast the structure and functions of starch (amylose) and cellulose.

Starch Cellulose
Large molecules of many alpha glucose Large molecules of many beta glucose
molecules joined with condensation molecules joined with condensation
reactions, insoluble in water and form reactions, they are insoluble in water and
granules also strong
For energy storage in plants Structural found in plants where it forms
cell walls

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Describe, with the aid of diagrams, the structure of glycogen.

Excess glucose is stored as glycogen

in animals.

The 1-4 and 1-6 glycosidic bonds

cause branching!

Meaning that the glucose can be

quickly released- good for animals!

Explain how the structures of glucose, starch (amylose), and glycogen and cellulose molecules relate to their functions in living
organisms.

Carbohydrate Example Characteristics Function in

Organisms
Monosaccharide Glucose (6 Carbon Small, soluble, sweet, Energy via respiration
monomers sugar) crystalline
Deoxyribose (5 Part of DNA
Carbon sugar) information molecule
Disaccharide dimers Maltose (2 glucoses) Small, soluble, sweet Sugar obtained when
& crystalline starch is broken down
in hydrolysis, can be
split to glucose for
more respiration
Polysaccharide Starch & glycogen Large molecules, Energy store in plants
polymers many alpha glucose as cellulose and
molecules joined by glycogen in animals
condensation. and fungi
Insoluble in H2O and
form granules
Cellulose Large molecules of Structural in plants for
many beta glucose cell walls.
molecules joined by
condensation.
Insoluble in H2O and
are strong.

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Compare, with the aid of diagrams, the structure of a triglyceride and a phospholipid.

Phospholipid

Phospholipids are similar to

triglycerides except that one of
Triglyceride
the fatty acid molecules is
replaced by a phosphate group.

Fatty acid tails are hydrophobic

Phosphate group is hydrophilic

and faces outwards. Good in the
bilayer for cell membranes so
water soluble substances find it
hard to get through.

Explain how the structures of triglyceride, phospholipid and cholesterol molecules relate to their functions in living organisms.

Triglyceride molecules are used as energy storage molecules. This is good because the
hydrocarbon tails of the fatty acids have lots of chemical energy that is released when
broken down, so lipids contain double the energy carbohydrates do.

They are insoluble because of their hydrophobic so they do not interfere with the water
potential in cells that would cause water to enter cells by osmosis so they could
swell/burst.

Phospholipid molecules have a hydrophilic head and a hydrophobic tail. The head faces
outwards and the tail faces inwards in the phospholipid bilayer on cell surface
membranes, making it difficult for water soluble substances like Na+ ions and glucose to
pass through.

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Cholesterol is a lipid found in cell membranes for mechanical stability, and is used to
make steroids. It has a hydrocarbon ring structure attached to a hydrocarbon tail. The
hydrocarbon ring has a polar hydroxyl group attached to it which makes it soluble.

Describe how to carry out chemical tests to identify the presence of the following molecules: protein (biuret test), reducing and non-
reducing sugars (Benedict’s test), starch (iodine solution), and lipids (emulsion test).

Biuret’s Test

Add Benedict’s solution to the substance and heat to 80 degrees Celsius in a water
bath. If the solution changes colour from blue to green-brick red then it is a reducing
sugar. (Monosaccharide and disaccharide)

Non reducing sugars do not react with Benedict’s solution so there would be no colour
change E.g. Sucrose, formed by a condensation reaction between glucose and
fructose. The formation of this bond is different to reducing sugars, so it must be boiled
with hydrochloric acid, to hydrolyse/split the sucrose molecules to give glucose and
fructose monosaccharides. Then add an alkali to a cool solution to neutralise it, e.g.
NaCO3 solution. Then do the reducing sugar test and you should get a positive result.

Starch

Add iodine in a potassium iodide solution to the sample, and if there is starch the
sample solution will change from yellow/brown to a dark blue/black. Negative results
present no colour change.

Lipids

Mix the sample with ethanol, dissolving lipids present. Pour the solution into water in a
separate test tube. If there is a lipid there will be a cloudy white milky emulsion near the
top of the water.

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Protein

Add biuret reagent to a sample. The reagent contains sodium hydroxide and copper
sulphate, reacting with the peptide bonds in protein turning the solution to a purple
colour if there is protein, and staying blue if there is no protein.

Describe how the concentration of glucose in a solution may be determined using colorimetry.

A colourimeter measures the absorbance of light of a solution; the more concentrated

the colour the higher the absorbance is.

 Make up several glucose solutions of known, different solutions

 Do a Benedict’s test on each solution, same amount in each case make sure
there is excess reagent
 Remove precipitate (Centrifuge/ leave for a day)
 Use colourimeter to measure absorbance of Benedict’s solution remaining in
each tube
 Record your results in a calibration curve (absorbance against glucose
concentration)
 Test the unknown solution by using the colourimeter and reading it’s absorbance
value across on the calibration graph, it will tell you the concentration.

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Nucleic Acids
State that deoxyribonucleic acid (DNA) is a polynucleotide, usually double-stranded, made up of nucleotides containing the bases
adenine (A), thymine (T), cytosine (C) and guanine (G).

A nucleotide

 A phosphate group
 Adenine and Thymine bond together with 2
hydrogen bonds, Cytosine and guanine join with
3 hydrogen bonds
 Deoxyribose

Joined with covalent bonds (sharing of electrons)

State that ribonucleic acid (RNA) is a polynucleotide, usually single-stranded, made up of

nucleotides containing the bases adenine (A), uracil (U), cytosine (C) and guanine (G).

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Describe, with the aid of diagrams, how hydrogen bonding between complementary base pairs (A-T, G-C) on two anti-parallel DNA
polynucleotides leads to the formation of a DNA molecule, and how the twisting of DNA produces its double-helix shape.

Outline, with the aid of diagrams, how DNA replicates semi-conservatively, with reference to the role of DNA polymerase.

 The enzyme called DNA helicase breaks the hydrogen bonds between the two
polynucleotide DNA strands unzipping the helix to form two single strands,
exposing the bases.
 Each original strand is a template for a new strand, free floating DNA nucleotides
join to exposed bases on each original template strand by complementary base
paring (purine pyrimidine, A- -T, G- - -C)
 The nucleotides on the new strand are joined by DNA polymerase, and new
hydrogen bonds are formed between the bases on the old and new strand.
 Each DNA molecule contains one strand from the original DNA molecule and one
new strand.
State that a gene is a sequence of DNA nucleotides that codes for a polypeptide.

Gene  A gene is a length of DNA that carries the code for the synthesis of one or
more specific polypeptides.

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Outline the roles of DNA and RNA in living organisms (the concept of protein synthesis must be considered in outline only).

The sequence of bases on DNA are code instructions for proteins, they code for the
amino acid sequence present in the protein. This is a gene.

There are three forms of RNA:

Messenger RNA  Is a strand complementary to a strand of a DNA molecule, a

template strand that is a copy of the coding strand of the double helix

Ribosomal RNA  In ribosomes

Transfer RNA  Carries amino acids to the ribosomes and they are bonded together to
form polypeptides.

Enzymes
State that enzymes are globular proteins, with a specific tertiary structure, which catalyse metabolic reactions in living organisms.

Enzymes are:

Globular proteins and soluble in water

Able to break molecules down or build them up!

Biological catalysts

Specific- because they catalyse a reaction with only one type of substrate

Their globular structure has a pocket called an active site

Activity affected by temperature and pH (Rate of reaction)

Enzymes are large molecules with hundreds of amino acids. A lot of these amino acids
work to keep the specific tertiary structure of the enzyme. The function of the enzyme
depends on the shape, and for the enzyme to work correctly the tertiary structure must
be maintained specifically.

All of the structures (primary, secondary, tertiary) of the enzyme is involved in the
specific active site shape. (Where the catalytic activity of the enzyme happens)

Enzymes are faster than catalysts and because they are specific to one reaction they do
not produce unwanted by products.

An individual cell could contain over one thousand enzymes to catalyse every process,
like digestion, respiration, photosynthesis.

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State that enzyme action may be intracellular or extracellular.

Extracellular Enzymes catalase reactions outside of the cell

Intracellular Enzymes catalase reactions inside of the cell

Mould produces extracellular enzymes to digest bread.

Phagocytes take in and digest bacteria using lysosomal enzymes.

Describe, with the aid of diagrams, the mechanism of action of enzyme molecules, with reference to specificity, active site, lock-and-
key hypothesis, induced-fit hypothesis, enzyme-substrate complex, enzyme-product complex and lowering of activation energy.

Enzymes reduce the amount of activation energy needed, so reactions happen quickly
at lower temperatures, because of the way the active site is shaped to fit the substrate.

Enzyme’s active site is complementary to the shape of the substrate, they are specific.

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Describe and explain the effects of pH, temperature, enzyme concentration and substrate concentration on enzyme activity.

pH

pH is the measure of the H+ ion concentration. These ions are positive so they are
attracted to negatively charged ions, or parts of molecules and repelled by positive
parts. Hydrogen bonds and ionic bonds hold the tertiary structure of an enzyme in place
so the active site is maintained in it’s correct shape. The bonds are there because of
electrostatic attraction between opposite charges on the amino acids making up the
enzyme.

Hydrogen ions interfere with these bonds and can alter the tertiary structure of an
enzyme by altering their concentration.

Enzymes have their own optimum pH, the H+ ion concentration gives the enzyme the
best overall shape. Enzymes work in a narrow pH range usually, and their pH range
often changes with their location. E.g. Pepsin is in the stomach and has an optimum pH
of 2. Handy! Whereas Trypsin has an optimum pH of 7 which is good for the conditions
of the small intestine it works in, where it digests protein.

Temperature

 When you apply heat to molecules, they

move faster in a liquid or gas and they also
vibrate.

 The vibrations strain the bonds holding the

molecules.

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 In large molecules like enzymes the vibration of molecules can break weaker bonds like
hydrogen or ionic bonds.

 The weaker bonds are there in abundance in an enzyme molecule and hold the tertiary
structure in place, so they maintain the active site’s correct, specific shape.

 Increasing temperature = Increasing bonds broken

 And the tertiary structure is held less in the shape of the active site needed for it to work.

 So rate of reaction will decrease if the substrate can’t fit in the active site.

 If enough of the bonds are broken, the entire tertiary structure unravels and the
enzyme stops working.

 If the tertiary structure of an enzyme is changed enough it will not function and it is not
restorable  denaturation.

 Denaturation Changes only the tertiary structure of an enzyme so it can’t

function and its function can’t be restored, which changes the active site of the
enzyme.

Concentration

Increasing the enzyme concentration increases rate of reaction to a point, until it will not
increase anymore because substrate concentration is the limiting factor. Reactions
cannot be quick if there isn’t enough substrate left, and vice versa.

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Describe how the effects of pH, temperature, enzyme concentration and substrate concentration on enzyme activity can be
investigated experimentally.
Variable Method of Keeping
Constant
Temperature Carrying out the enzyme
controlled reaction in a
water bath with thermostat
Enzyme Concentration Use an accurate measured
volume of enzyme-solution
Living tissue Mass of
tissue has to be accurate
Whole pieces of tissue
same surface area and
mass
Substrate Concentration Accurately measured
substrate volume/mass
pH value Use pH buffers by keeping
H+ concentration constant
Explain the effects of competitive and non-competitive inhibitors on the rate of enzyme-controlled reactions, with reference to both
reversible and non-reversible inhibitors.
Competitive inhibitors have a similar shape to the substrate so they occupy the active
site and form an enzyme inhibitor complex but no product is made. So the enzyme
cannot catalyse a reaction and rate of reaction slows down. Depends on inhibitor and
substrate concentration, e.g. if you increase substrate rate of reaction may increase.
Non Competitive inhibitors don’t occupy the active site, but attach somewhere else on
the enzyme to distort the tertiary structure of the enzyme. So the active site changes
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Reasons
Room temperature changes
and fluctuations in the
temperature alters the
enzyme controlled reaction
so results will not reflect the
true action of the
independent variable that is
being found
Rate of reaction depends
on concentration of enzyme
molecules present; using
accurate volumes of
enzyme solution gives a
true constant conc. Of
enzyme molecules
Assume that the pieces of
tissue have the same
number of enzyme
molecules
The number of enzymes
that have contact with
substrate affects rate of
reaction, e.g. surface area
Rate of reaction depends
on substrate molecule
concentration
Rate of reaction depends
on pH because it alters the
shape of the active site of
the enzyme
Emily Summers

and the substrate can’t fit anymore, so no reaction can be catalysed and reaction rate
decreases. Increasing substrate concentration has no effect.

Reversible inhibitors are when the inhibitor isn’t there permanently and afterwards the
enzyme is unaffected.

Non Reversible inhibitors are usually non competitive and the enzyme is denatured.
Explain the importance of cofactors and coenzymes in enzyme-controlled reactions

Coenzymes take part in the reaction and are changed, but are recycled back to take
place in the next reaction.

Cofactors are there to ensure an enzyme controlled reaction takes place at an

appropriate rate, and some enzymes can only catalyse a reaction if a cofactor is there.
State that metabolic poisons may be enzyme inhibitors, and describe the action of one named inhibitor.

Lots of poisonous substances have their effects due to inhibiting or over-activating

enzymes. For instance, Potassium Cyanide inhibits respiration of cells, because it is a
non competitive inhibitor for a vital respiratory enzyme, cytochrome oxidase, in the
mitochondria. When cytochrome oxidase is inhibited the use of oxygen is reduced
and ATP cannot be produced. So the organism is only able to respire anaerobically,
which builds up lactic acid in the blood increasing its acidity.
State that some medicinal drugs work by inhibiting the activity of enzymes.

Viral infections are treated using chemicals that act as protease inhibitors, which stop
viruses from replicating by inhibiting the activity of protease- which are vital to viruses to
build their new virus coats. Usually these inhibitors are competitive.

Cystic Fibrosis sufferers have the problem that the passage of digestive enzymes that
are usually secreted from the pancreas into the gut is blocked, leading to digestive
problems. Enzymes in a tablet can overcome the problem; they are in an acid
resistant coat so they’re not destructed by acid/protein digesting enzymes located in
the stomach.

Health and disease

Discuss what are meant by the terms health and disease

Health is a complete state of physical, mental and social well being as well as the
absence of disease or infirmity.

Disease is a departure from full health caused by a malfunction of the mind or body
Define and discuss the meanings of the terms parasite and pathogen.

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Parasite Is an organism that lives in or on another living thing causing harm to the
host. External head lice Internal Tapeworm

Pathogen A general term for any organism that causes disease

Bacteria, fungi, viruses, protoctista

Describe the causes and means of transmission of malaria, AIDS/HIV and TB.

Malaria is caused by a eukaryotic organism, from the genus Plasmodium and most
commonly the species Plasmodium falciparum.

Malaria is spread by means of a vector. The female Anopheles mosquito carries the
plasmodium from an uninfected to an infected person, they feed on blood with adapted
mouthparts to penetrate a blood vessel and withdraw blood, malarial parasites live in
the erythrocytes of humans and feed on Hb.

HIV/AIDS

The virus enters the body and is un-active, but once the virus is active and
attacks/destroys T helper cells in the immune system your ability to resist infection is
greatly decreased. You are open to opportunistic infections which will eventually kill the
person with HIV/AIDS.

 Exchange of bodily fluids, e.g. blood to blood, sharing needles, unprotected sex
 Unscreened blood transfusions
 Mother to baby- across the placenta or during breast feeding

TB

TB is caused by a bacterium, M Bovis and Mycobacterium tuberculosis.

It is usually in the lungs and although it is common it usually remains unactive or the
immune system controls it, it is transmitted by a droplet infection.

 Overcrowding
 Poor ventilation
 Poor health, especially with HIV/AIDS
 Poor diet
 Homelessness
 Contact with those who migrate from countries where TB is common

Discuss the global impact of malaria, AIDS/HIV and TB.

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REMEMBER THE WORLD HEALTH ORGANISATION! They say good health is

a human right and see that in LEDC countries there may be:
 Poverty
 Lack of shelter and pure water
 Poor nutrition and hygiene
 Insufficient health services and insufficient education of disease

Malaria kills three million a year, but is limited to where the Anopheles can survive
which is tropical regions like Sub Saharan Africa. Global warming is a worry.

HIV/AIDS Pandemic. 45 million living with HIV/AIDS in 2005 and over half lived in sub
Saharan Africa.

TB Worldwide disease, new strains of Mycobacterium are resistant to drugs available
to treat it. Common in sub Saharan Africa but rising in Eastern Europe.
Define the terms immune response, antigen and antibody.

Immune response is the specific response to a pathogen involving the action of

lymphocytes and the production of antibodies.

Antigens are molecules that stimulate an immune response.

Antibodies are protein molecules that identify and neutralise antigens.

Describe the primary defences against pathogens and parasites (including skin and mucous membranes) and outline their
importance.

They try to prevent pathogens from entering the body, general mechanisms.
The skin
 Main primary defence
 Outer layer= epidermis
 Keratinocytes are made by mitosis at the base of the epidermis, during migration
they dry out and the cytoplasm is replaced by keratin- called keratinisation. When
these cells reach the surface they aren’t alive anymore and the dead cells come
off, but this layer of dead cells are a good barrier to pathogens.

Mucous Membranes
 In airways, lungs and digestive system
 Goblet cells secrete mucus and mucus lines airway passages to trap pathogens.
Cilliated epithelium beats rhythmically to waft mucus to the back of the mouth
where it is swallowed down to the digestive system, the acidic stomach kills most
pathogens by denaturing their enzymes

Eyes are protected by tear fluid antibodies and enzymes

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Ear canals are lined with wax to trap pathgogens

Describe, with the aid of diagrams and photographs, the structure and mode of action of phagocytes.

Describe, with the aid of diagrams, the structure of antibodies

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Outline the mode of action of antibodies, with reference to the neutralisation and agglutination of pathogens.

Antibodies cover the pathogen

binding sites and prevent the
pathogen from binding to a host
cell and entering the cell

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A large antibody can bind lots of pathogens together so the group of pathogens are too
large to enter a host cell.
Compare and contrast the primary and secondary immune responses

Compare and contrast active, passive, natural and artificial immunity .

Active Immunity Artificial Immunity

Exposure to antigen No exposure to antigen
Protection development takes a longer Protection is instant
period
Protection lasts a long while Protection lasts a short period
Memory cells made No memory cells made

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Active Immunity Passive Immunity

Natural Catch the disease Antibodies from mother to
baby across placenta
Artificial Vaccination Injected with antibodies

Module 3 Biodiversity & Evolution

Biodiversity
Define the terms species, habitat and biodiversity

A species is a group of similar individual organisms with similar appearance,

biochemistry, physiology and genetics whose members are able to interbreed freely to
produce fertile offspring

A habitat is a place where the organism lives

Biodiversity is the variety of life, the range of living organisms to be found

Use Simpson’s Index (D) to calculate the biodiversity of a habitat, using the formula D = (n/N)2.

D = (n/N)2.

There are three species of flower in a field, red, white and blue.
There are eleven organisms all together, so N = 11

There are three of the red species, five of the white and three of the blue

D = 1 – ((3/11)2 + (5/11)2 + (3/11)2 = 1 – 0.36 = 0.64 Quite high!

Outline the significance of both high and low values of Simpson’s Index (D).

The closer to one the index is, the more diverse the habitat is. A high value indicates
high biodiversity in a habit which is beneficial, a low one indicates low biodiversity in a
habitat which isn’t so good, and may suggest that conservation methods might have to
be put in place.

Classification
Define the terms classification, phylogeny and taxonomy.

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Classification is arranging organisms into groups based on similarities and differences

in appearance.

Phylogeny is the study of the evolutionary history of groups of organisms

Taxonomy is the study of classification

Explain the relationship between classification and phylogeny.

Describe the classification of species into the taxonomic hierarchy of domain, kingdom, phylum, class, order, family,
genus and species.

Outline the characteristic features of the following five kingdoms: Prokaryotae (Monera), Protoctista, Fungi, Plantae,
Animalia.

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Kingdom Example Features

Prokaryote Bacteria Single cell, no nucleus,

smaller than 5 micrometres

Protoctista Algae Eukaryotic, single celled or

simple multicellular

Fungi Mould, yeast, mushroom Chitin cell wall, eukaryotic,

saprotrophic

Plantae Moss, fern, roses Eukaryotic, multicellular,

cellulose cell wal, autotrophic

Animalia Mammals, reptiles, birds, fish, Heterotrophic, eukaryotic, no

insects cell wall, multicellular

Outline the binomial system of nomenclature and the use of scientific (Latin) names for species.

One international name in latin with two parts is given to every organism. The
first part is the genus and is a capital letter, and the second is the species and is
lower case- typed in italics or underlined when written. E.g. Homo sapien
Helps to avoid confusion within scientists as they’re standard scientific names.
Use a dichotomous key to identify a group of at least six plants, animals or microorganisms.

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Discuss the fact that classification systems were based originally on observable features but that more recent
approaches draw on a wider range of evidence to clarify relationships between organisms, including molecular evidence.

Early classification systems simply used observable features to put organisms

into groups, but this is problematic because the fact that some organisms look
similar doesn’t mean they’re closely related, e.g. sharks and whales look similar
and live in the sea, but sharks are fish and whales are mammals! Classification
systems today are based on more evidence, like:
 Molecular evidence protein and DNA similarities, e.g. how it’s stored,
closeness of bases.
 Anatomical Similarities in structure and function of body parts
 Behavioural evidence Similarities in behavior and social organization of
organisms

Compare and contrast the five kingdom and three domain classification systems.

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Evolution
Define the term variation.

Variation  Presence of variety of differences between individuals

Discuss the fact that variation occurs within as well as between species.
Describe the differences between continuous and discontinuous variation, using examples of a range of characteristics
found in plants, animals and microorganisms.

Continuous variation  Variation in which there is a full range of intermediate

phenotypes between two extremes

Discontinuous variation  Variation in which there are discrete groups of phenotypes

with few or no individuals in between

Continuous Discontinuous
Height Dangling/attached ear lobes
Handspan Gender
Weight Blood groups
Shoe Size Bacteria with absence/presence of flagella

Continuous Discontinuous
Affected by environment & genes Unaffected by environment, just genes
Quantitative overlaps Qualitative no overlaps
Controlled by a large number of genes Controlled by few/one gene (monogenic)
(polygenic)
No distinct categories Distinct categories

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Like heart rate, muscle efficiency, IQ, growth This type of variation is rare in animals
rate, rate of photosynthesis but abundant in plants, like seed colour,
petal colour, etc.

Explain both genetic and environmental causes of variation.

Genetic Environmental
 Genes from our parents  Linked with genetic
 Combination of alleles  Like height is somewhat
 Not the same in any other living determined by your genes but
thing apart from identical twins the environment plays a part on
 Never a complete match the height you will reach. (diet)
 Human cells have 25,000  Environmental changes affect
different genes and a lot of them what genes in animals and plants
have more than one allele, so it are activated, bringing about
isn’t likely that any two changes we see
individuals will have the exact  Obesity diet  socio-economic
same allele combinations. issues. Westernized society has
more overweight people than
ledc’s

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Outline the behavioural, physiological and anatomical (structural) adaptations of organisms to their environment

Behavioural Physiological/Biochemical Anatomical

Behaviour of an organism
that enables it to survive it's
living conditions. Like when
you touch an earthworm it
quickly contracts and goes
back into it's burrow. This is
a behavioural adaptation
that avoids it being eaten.
A physiological/biochemical Any structure that enhances
adaptation that ensures survival of the organism is an
correct functioning of cell adaptation. Like bacteria that
processes. Like yeast can have flagella to allow them
respire sigars an/aerobically to move indepedently.
to get energy depending on Structural adaptation.
the amount of O22 in the
environment. Producing
correct enzymes to respire
the sugars in the
environment falls under this
category.

Explain the consequences of the four observations made by Darwin in proposing his theory of natural selection.

Individual in a species have differences from each other – so variation is present.

Offspring bare resemblance to their parents – those characteristics are inherited.
There are more offspring produced than survived to maturity - they suffer from
predation, disease and competition.
Populations have constant sizes
“Darwin concluded that individuals that were better adapted to their environment
compete better than the others, survive longer and reproduce more, so passing on more
of their successful characteristics to the next generation. Darwin used the memorable
phrases survival of the fittest, struggle for existence and natural selection.” Biology Mad

Define the term speciation.

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Formation of a new species from the evolution of one species

geographical isolation which is an example of allopatric speciation
reproductive isolation which is an example of sympatric speciation

Discuss the evidence supporting the theory of evolution, with reference to fossil, DNA and molecular evidence.

Outline how variation, adaptation and selection are major components of evolution.

Discuss why the evolution of pesticide resistance in insects and drug resistance in microorganisms has implications for humans.

Conserving biodiversity
Outline the reasons for the conservation of animal and plant species, with reference to economic, ecological, ethical and
aesthetic reasons.

Discuss the consequences of global climate change on the biodiversity of plants and animals, with reference to changing
patterns of agriculture and spread of disease.

Explain the benefits for agriculture of maintaining the biodiversity of animal and plant species.
Describe the conservation of endangered plant and animal species, both in situ and ex situ, with reference to the
advantages and disadvantages of these two approaches.
Discuss the role of botanic gardens in the ex situ conservation of rare plant species or plant species extinct in the wild,
with reference to seed banks.
Discuss the importance of international cooperation in species conservation with reference to the Convention in
International Trade in Endangered Species (CITES) and the Rio Convention on Biodiversity.
Discuss the significance of environmental impact assessments (including biodiversity estimates) for local authority planning
decisions

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