OCR A Biology

3.1
Summary Questions

1 Atoms form bonds with each other when pairs of electrons are shared (1) according to the bonding
rules (1).
2 A cation is an ion with a net positive charge (1), i.e. it has lost one or more electrons (1). An
anion is an ion with a net negative charge (1), i.e. it has gained one or more electrons (1).
3 Water – one oxygen atom binds to two hydrogen atoms (1), oxygen can form two bonds, each
hydrogen can only form one bond (1). Carbon dioxide – one carbon atom and two oxygen atoms
(1), carbon can form four bonds, each oxygen atom can form two bonds, therefore carbon forms a
double bond with each oxygen atom (1).
4 a X ray diffraction does not involves lenses (1) / electron microscope uses electromagnetic lenses
(1) / beams focused in electron microscopy to produce image (1).
b Cells are larger than ribosomes (1) / cells are larger than, half the wavelength / resolution limit, of
light (1) / electron microscopes have greater resolution (than light microscopes)
(1) / idea that molecules are smaller than resolution limit of light and larger than resolution limit of
electron beam (1).

3.2
Summary Questions

1 Oxygen and hydrogen share electrons unequally when they bond. Oxygen, has a greater share/ is
more negative (1). Hydrogen, has a smaller share/is more positive (1). The more negative oxygen
atom is attracted to the more positive hydrogen atom (1).
2 Water is composed of hydrogen and oxygen atoms and bonds between oxygen and hydrogen
involve unequal sharing of electrons (1) in bonds resulting in the oxygen atom being more negative
and the hydrogen atoms being more positive (1).
3 Liquid so transport medium (1); polar solvent (1); (many) biological molecules / examples
(e.g., enzymes, glucose), are polar (1); ions are charged (1); coolant so (relatively) resistant to
temperature change (1).
4 (water is) liquid (1) / allows movement of substrates and enzymes (1) / idea that this is necessary
for reactions to occur (1) / (water is) a polar solvent (1) / substrates / enzymes / products, are, polar /
ionic (1) / (water is) substrate for (some) reactions (1).

3.3
Summary Questions

1 Hydroxyl group on carbon 1 is in a different position (1); in alpha glucose it is below the ring in beta
glucose it is above the ring (1).
2 Bond formed between two glucose molecules (1) – hydroxyl group of carbon 1 on one molecule
(1) and carbon 4 (1) on the other interact in a condensation reaction/removal of water molecule (1) to
form an ‘oxygen bridge’.
3 Cellulose is straight chain molecule (1) with many hydrogen bonds between individual chains (1)
and staggered ends (1). This confers strength to the fibres (1).
4 In beta glucose the hydroxyl group at carbon 1 is above the ring (1) so alternate glucose molecules
must rotate 180 degrees (1) so the hydroxyl groups on carbon 1 and carbon 4 are close enough to
react (1) condensation reaction (1) forming a glycosidic bond (1). The rotation of molecules produces
a straight chain molecule (1) – cellulose.

3.4
Quantitative methods to determine concentration
Colorimetry
1 100% – transmission % = absorbance % (1)
2 (to) maximise absorption (1); complementary colour / red for Benedict’s solution (1)
3 use distilled water (1); set colorimeter to 100% (1)
4 unreacted Benedict’s solution (1); supernatant (1)

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5 correct axes (1); correct plots (1); line of best fit (1)
6 concentration of glucose at 44% absorbance (1); units (1)

Biosensors
1 Biological detector (1); presence of (toxic) gas causes a change (1); distress of bird is display (1);
canary in a cage is a biosensor (1); disadvantage not specific to one gas (1); ethical considerations of
causing harm to an animal (1).

Summary Questions

1 (enzymes have) active site (1); (active site) specific (1); to, substance / molecule, testing for (1)
2 Reducing sugars react with copper ions in Benedict’s reagent resulting in the addition of electrons to
blue Cu2+ ions (1), reducing them to Cu+ ions which form a brick red precipitate (1).
3 In an iodine test a purple/black colour indicates the presence of starch (1). Starch is a product of
photosynthesis (1). The test shows that starch is produce when light is available to the plant, but not
when the plant is kept in the dark (1).
4 Reagent strips are quantitative (1); they can be used to estimate the concentration (1) of reducing
sugar (glucose) (1) in the blood. They are simple to use and interpret (1).

3.5
Fats in our diet
1 hydrogenation / addition of hydrogen (1); removes double bonds in fatty acids (1); closer packing of
molecules (1)
2 unsaturated and saturated fat have high energy content (1); excess energy intake leads to obesity
(1)

Summary Questions

1 Oils are (usually) unsaturated (1); unsaturated fatty acids contain double bond(s) (1); molecules
cannot pack closely (1); fats are usually saturated so fatty acids have no double bonds (1).
2 Hydroxyl group from glycerol (1); hydroxyl group from fatty acid (1); condensation reaction (forms
ester bond) (1); idea that hydrolysis is reverse of the process described (1).
3aA
b Both have phosphate group attached to glycerol (1); both have fatty acid (tail) (1); cross links
between fatty acid tails in A (1) ; no oxygen attached by double bond (on A) / ester bond not present
(on A) (1).
c Cross links (1); stabilise membrane (1)
4 procedure for emulsion test statement 2, sample / lipid, dissolved in ethanol (1); water is mixed with
ethanol (and lipid) solution (1); statement 3, idea that water displaces lipid from ethanol forming
suspension (1); statement 1, (suspension forms because) lipids not soluble in water (1)

3.6
Separating amino acids using thin layer chromatography
1 a to prevent contaminating stationary phase (1); idea of biological material (on skin) (1) b testing
unknown compounds (1); not known whether, polar / non-polar (1); idea that the different solvents will
dissolve both polar and non-polar compounds (1)
c so the concentrated spots were not covered (1)
d (so) air inside jar is saturated with (solvent) (1); prevents evaporation of solvents (1)
2 a from bottom to top glycine, proline, phenylalanine (1)
b from bottom to top alanine, methionine (4)

Identification of proteins
1 mauve / lilac / purple (1)
2 no peptide bonds present (as no protein) (1); test is negative (1); solution (remains) blue (1); as
copper sulfate solution is blue (1)
3 Biuret test identifies peptide bonds (1); degree of colour change dependent on number of peptide
bonds (1); different proteins have different numbers of peptide bonds (1); idea that different degrees
of colour change could indicate different proteins not different quantities of protein (1).

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 OCR A Biology

Summary Questions

1 Diagram showing the amine group (1); carboxylic acid group (1); and variable group (1); in correct
positions. See Figure 1 in Topic 3.6, Structure of proteins.
2 Condensation reaction (1) between amine group of one amino acid (1) and carboxylic acid group of
another (1), forming a water molecule.

3a
b Oxygen is relatively negative and hydrogen (attached to nitrogen) is relatively positive (1); oxygen
and hydrogen are attracted to each other (1).
c Secondary structures are (simple) repeating structures (1); globular protein / haemoglobin, has a
tertiary structure (1); tertiary structure is formed from complex folding of secondary structure (1).
4 R groups on amino acids interact (1); tertiary structure – interactions within a protein molecule (1)
determines shape of molecule (1); quaternary structure – interactions between protein molecules (1);
holds molecules together (1). Both involve the same interactions (1), i.e., hydrogen bonds, ionic
bonds, disulfide bonds, and hydrophobic and hydrophilic interactions.

3.7
The structure of fibrous proteins – elastin and collagen
1 strength, non-elastic
2 (collagen is a) large molecule so unlikely to enter skin (collagen), has a complex structure, idea of
individual components arranged in hierarchical structure, idea that new molecules would not
incorporate into existing collagen
3B

Summary Questions

1 Conjugated proteins contain a non-protein group (1) called a prosthetic group (1), simple proteins
do not (1).
2 insulin globular protein (1); soluble (1); specific shape (1); binds to receptor (1); chemical
messenger / described (1); keratin fibrous protein (1); strong (1); structural function / example (e.g.
hair, nails)
3 globular proteins hydrophobic R groups, in the centre (of the molecule) not in contact with water (1);
hydrophilic R groups, on the outside (of the molecule) / in contact with water (1); hydrophobic R
groups are repelled by water / hydrophilic R groups are attracted to water (1); fibrous proteins have R
groups on the outside of the molecule (1)
4 similarities globular (protein) (1); alpha helices (1); prosthetic group (1); hydrophobic R groups
positioned towards the centre (of the molecule) (1); differences single polypeptide not four
polypeptides / myoglobin tertiary not quaternary (1); no beta chains (1)

3.8
DNA extraction
1 reduce activity of enzymes (1); reduce breakdown of DNA (1)
2 disrupts membrane structure (1); phospholipids form suspension in aqueous solution (1)

Summary Questions

1 DNA nucleotide – deoxyribose sugar, thymine base (1); RNA nucleotide – ribose sugar, uracil base
(1).
2 A pyrimidine base always pairs with a purine base (1). Adenine and thymine/uracil always hydrogen
bond together (1) and cytosine and guanine always hydrogen bond together (1).
3 Polymer so contains a lot of information (1); idea that base sequence is used as a code (1); double
stranded so molecule is stable (1); double stranded so accurate replication (1).

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4 Adenine always base pairs with thymine, so same amount of thymine (17%) (1). Adenine and
thymine together is 34%, so cytosine and guanine must be 100 – 34 = 66% (1). Cytosine always base
pairs with guanine so cytosine amount equals guanine, 66/2 = 33. Therefore cytosine 33% and
guanine 33% (1).

3.9
Continuous and discontinuous replication
1 Continuous replication – DNA polymerase binds to the end of a strand, free DNA nucleotides added
without any breaks; discontinuous replication – DNA polymerase cannot bind to the end of a strand,
free DNA nucleotides added in sections, sections then joined.
2 Enzymes are (substrate) specific (1); DNA polymerase catalyses the joining of nucleotides (1);
nucleotides have a different shape to Okazaki fragments (1).

Summary Questions
1 Semi-conservative means ‘half the same’ (1). When DNA replicates the double helix unwinds
into two separate strands (1); free nucleotides pair with their complementary bases (1); two new
molecules of DNA are produced (1); each with one old strand and one new strand (1).
2 The triplet code is a particular sequence of three bases (1); that codes for a specific amino acid (1).
3 A mutation in the DNA changes the triplet code (1); meaning different amino acids are incorporated
into the protein/enzyme (1); that the DNA codes for. If such a change affects the precise structure of
the active site (1); a substrate may not be able to bind (1), rendering the enzyme non-functional.
4 The triplet code of DNA is degenerative (1), there are 64 different triplets/codons but only 20 amino
acids (1); therefore an amino acid can be coded for by more than one codon (1); so more opportunity
for differences in DNA sequence than amino acid sequence (1).

3.10
Summary Questions
1 From column left to right: UAC CGG AGU GCA
2 mRNA – copies gene from DNA (1), takes copy to ribosome (1); tRNA – brings amino acid to
ribosome (1); rRNA – formation of ribosome (1)
3 a catalyse the formation of bond between two amino acids (1); peptide bond (1)
b bind to tRNA (1); complementary base pairing (1)
c free floating ribosomes produce proteins for use in, cell / cytoplasm (1); bound ribosomes produce
proteins for export from the cell (1)
4 a role of protein dependent on structure (1); shape / 3D structure, dependent on primary structure /
sequence of amino acids (1); base triplets / codons, on mRNA, code for amino acids (1); introns
would code for, unnecessary amino acids / stop signal (1); codons could cause frameshift (1)
b different proteins produced from one gene (1)
c idea that originally functional gene(s) (1); mutation/s (1); base sequence/s changed (1); no longer
code for (useful) amino acids (1)

3.11
Summary Questions

1 sugar/ribose sugar (1); joined to a base/adenine (1); and to three phosphates (1)
2 It is present in all cells (1); it is present in all organisms (1). It releases energy in, small/ manageable
quantities (1).
3 (fat is) long term energy store (1); idea that fat is stable molecule and ATP is unstable molecule (1);
fat has other uses (1); e.g., insulation (1)
4 a bond formation releases energy (1); bond uses energy (1)
b ATP provides energy for, reactions / processes (1); ATP is present in all living organisms (1); idea
that there is no other equivalent molecule (1); therefore statement is valid (1).

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