Answers to Further Questions

CHEMICALS OF LIFE (Chapters 1–3): Mark Scheme

1 Biological molecules
Question No. Part Sub-part Marking Guidance Mark Comment
1 Statement Starch Glycogen Cellulose 4 1 mark for each correct row.
Empty cells should not gain any credit.
Polymer of α-glucose ✓ ✓ ✗
Glycosidic bonds present ✓ ✓ ✓
Unbranched chains only ✗ ✗ ✓
Energy store in animal cells ✗ ✓ ✗

2 a HO O OH H O H 2 1 mark for each monosaccharide correctly

drawn.
Check position of H and OH groups carefully.
H H HO OH

b Lactase 1
c (Add) Benedict’s solution; 3 Do not accept put in water bath for second
heat; mark unless qualified.
red/orange colour.
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3 a Plant cell wall 1
b i β-glucose 1 Reject glucose or α-glucose.
ii Hexose 1
iii 1 In long chains/microfibrils, cross linked by hydrogen bonds; 1
2 Strength/rigidity. 1
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4 a Amylopectin 1 Accept glycogen as it also has 1,6 glycosidic
bonds but not shown in textbook.
b The position of the H and OH groups (on carbon 4) are reversed 1 Accept a diagram clearly showing this as an
answer.

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 c i O O 2 One mark for water being used in hydrolysis;
O second mark for correct position of H and
OH groups where glycosidic bond has been
+ H2O broken.
O H O H
H H
OH OH OH OH

ii The position of the bond in molecule B means that the molecule is the 1 Accept – no cellulase enzyme in humans to fit
wrong shape to fit into the active site of the digestive enzyme shape of bond.
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5 a i NH2 at one end; 1
COOH at other end;
C in centre bonded to one R and one H.
ii Primary structure 1
iii Condensation reaction/removal of water; 3 Accept annotated diagram as answer.
OH from COOH and H from NH2;
peptide bond.
b i Transport of oxygen 1
ii Any three from: 3
globular;
quaternary structure;
made of four polypeptide chains;
idea of two different types of chain, e.g. α and β chains;
contains prosthetic group/haem;
iron part of prosthetic group/haem.
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6 a Add ethanol; 3 Must be in correct order of ethanol then water.
add water; Do not accept cloudy – must have white.
milky/cloudy white solution or emulsion.
b i X = phosphate; 2 Reject phosphorus
Y = glycerol.
ii Saturated fatty acids have no double bonds between carbon atoms, 2 Must refer to bonds between carbon atoms.
unsaturated fatty acids have at least one double bond between carbon atoms.
c Phospholipids have phosphate group and triglycerides do not; 1 Must have comparison.
OR
phospholipids have two fatty acids and triglycerides have three fatty acids.
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 7 a Amino (group); 1
b Further folding of the secondary structure; 2
disulfide bonds.
c Only one polypeptide chain. 1
d No prosthetic group. 1
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2 Enzymes
Question No. Part Sub-part Marking Guidance Mark Comment
8 a Active site 1
b The substrate has a shape which is complementary to the active site; 2 Reject same shape as active site.
only a substrate with this shape will form an enzyme-substrate complex
with the enzyme.
c A competitive inhibitor has a structure similar in shape to the substrate; 2 max Reject same shape as substrate.
the inhibitor competes with the substrate for the active site on the enzyme;
so slowing the rate of reaction/preventing enzyme-substrate complexes
from forming.
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9 a General points: 10 Take care not to award the same marking
Enzymes have a tertiary structure; point twice.
active site has a specific shape.
i Effect of high temperature:
Hydrogen bonds break;
enzyme denatures/active site changes shape;
substrate no longer fits in active site/enzyme-substrate complex cannot form.
ii Substrate specificity:
Substrate has a shape complementary to the active site of the enzyme;
enzyme only catalyses reaction for one type of substrate.

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 iii The effect of inhibitors:
Competitive inhibitors have similar shape to substrate;
competitive inhibitor competes with substrate for the active site of the enzyme;
non-competitive inhibitor binds to the enzyme at a site other than the active
site/allosteric site;
non-competitive inhibitor changes shape of enzyme/active site;
substrate no longer fits in active site/enzyme-substrate complex cannot form.
b Add more substrate to the reaction; 2
if rate of reaction increases then it is a competitive inhibitor/if no increase
in rate of reaction then it is a non-competitive inhibitor.
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10 a i The active site of the enzyme moulds itself around the substrate; 2
when the products are formed the active site reverts to its original shape.
ii The inhibitor has a similar shape to part of the substrate; 2
the inhibitor blocks the active site preventing the substrate from binding.
b The active site would be complementary to the substrate and would not 1
change shape.
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11 a i Active site 1
ii Enzyme has a tertiary structure; 4
active site moulds itself to the substrates;
lowers activation energy for the reaction;
active site reverts to original shape releasing the products.
b i 3 One mark for correct axes labels.
all active sites
now filled One mark for curve showing increase at start.
One mark for curve levelling off.
Not essential to have annotations as these
were not asked for in the question.
enzyme active sites
being filled

rate of reaction
substrate concentration

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 ii At low concentration of substrate there are plenty of enzyme active sites 3 max
available;
the rate of reaction increases with increased substrate concentration;
as the enzyme active sites become filled the rate of reaction slows;
once all the active sites are filled the rate of reaction becomes constant as
the enzyme is working at its maximum rate.
c The lower pH changes the hydrogen bonding in the enzyme and changes 2
the shape of active site;
(the substrate no longer fits as well so) fewer enzyme-substrate complexes
form.
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12 a i 3 One mark for exponential rise (rate should
double for every 10 °C rise).
One mark for up to optimum of approximately
40 °C.
One mark for sharp fall in rate after optimum.

rate of reaction
0 20 40 60 80
temperature / °C

ii At low temperatures an increase in temperature causes increase in kinetic 4 max

energy of molecules/enzyme and substrate;
more collisions occur between enzyme and substrate/more enzyme-
substrate complexes;
rate of reaction increases up to optimum temperature;
above the optimum the atoms in the molecules vibrate breaking hydrogen
bonds;
the active site changes shape/enzyme is denatured;
substrate no longer fits in active site.
b Enzymes have a tertiary structure; 4
changes in pH can alter the hydrogen bonding;
small changes in pH will alter the shape of the active site, but not denature
the enzyme/slow the rate of reaction;
large changes in pH denature the enzyme and substrates can no longer fit
in the active site/enzyme-substrate complexes no longer form.
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 13 a Enzymes have active sites with specific shapes; 2
only substrates with complementary shapes can bind to the active site. Reject same shape.
b Malonate has similar shape to succinate; 2 max Reject same shape; accept part of malonate
malonate can fit into active site of enzyme/succinate dehydrogenase; has same shape.
succinate is prevented from entering the active site.
4
14 a Two factors from: 2 max List rule applies, i.e. if more than two factors
pH; given and one is incorrect a mark is lost.
temperature;
volume of amylase;
volume of starch.
b Increases and levels out; 2 One mark for general trend;
increases and levels out at/after 10 minutes/at 6 g dm−3. two marks if correct figures from graph used.
c i Find the gradient of the line/divide concentration at X minutes by X. 1 Accept an answer where student has done the
calculation with working.
Do not accept a figure without working.
ii Less substrate/substrate used up/substrate is limiting factor; 2 Accept starch for substrate.
fewer collisions between enzyme and substrate/fewer enzyme-substrate
complexes.
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3 Nucleic acids and protein synthesis

Question No. Part Sub-part Marking Guidance Mark Comment
15 a W = phosphate; 4 Reject phosphorus.
  X = deoxyribose;
  Y = cytosine;
   Z = adenine.
b i C: 44% of 500 = 220; 4 Must show some working of how figures are
G: G pairs with C so also 220; obtained.
A: T + A = 500 – 440 = 60, so A = 30;
T: T pairs with A, so also 30.
ii May be start/stop codons; 2
may be part of introns. Accept other description of introns, e.g.
non-coding DNA.
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 16 a X = thymine; 3 Accept T, G and A.
Y = guanine;
Z = adenine.
b i Separates DNA strands; 2
by breaking hydrogen bonds.
ii Joins together nucleotides; 2 max
on new/missing (polynucleotide) strand;
by phosphodiester bonds.
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17 a Each strand is copied/acts as a template; 2 Do not accept half new and half old – must
(daughter) DNA molecule has one new strand and one original strand. refer to strands.
b i DNA in tube A (14N) is less dense than the DNA in tube B (15N). 1
ii Contains DNA with one heavy and one light strand; 2
new strand made with 14N/ new strand is light strand;
c Tube should show two bands of DNA: one band in same position as tube A; 2
one band in same position as tube C.
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18 a Try—Gly—Lys—Val—Gly 2 Two marks if all correct;
one mark if four correct.
b Substitution of G for C in second triplet (no mark); 3
amino acid changed from Gly to Ala;
alters the primary structure/amino acid sequence of protein;
tertiary structure altered/bond positions altered;
as structure altered function may be affected.
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19 a tRNA single stranded, DNA double stranded; 2 max Need to have comparison for mark.
tRNA has uracil (base), DNA has thymine (base);
tRNA has ribose (sugar), DNA has deoxyribose (sugar).
b Complementary bases/A with U and C with G; 2
(joined by) hydrogen bonds;
c i GAA 1
ii CUU 1
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 20 Statement DNA mRNA tRNA 6 1 mark for each correct row.
Empty cells should not gain any credit.
Attaches to ribosome ✗ ✓ ✗
Carries amino acid to ribosome ✗ ✗ ✓
Translated ✗ ✓ ✗
Transcribed but not translated ✓ ✗ ✗
Site of anticodon ✗ ✗ ✓
Site of codon ✗ ✓ ✗

21 a Stage 1 = transcription; 2
stage 2 = translation.
b Ribosomes 1
c Carries the specific amino acid; 3
to the mRNA;
with complementary codon to anticodon on the tRNA.
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