Feversham College

Q1.          The diagrams show four types of linkage, A to D, which occur in biological molecules.

(a)     Name the chemical process involved in the formation of linkage B.

......................................................................................................................
(1)

(b)     Give the letter of the linkage which

(i)      occurs in a triglyceride molecule;

.............................................................................................................
(1)

(ii)     might be broken down by the enzyme amylase;

.............................................................................................................
(1)

(iii)     may occur in the tertiary, but not the primary structure of protein.

.............................................................................................................
(1)

(c)     Describe how a saturated fatty acid differs in molecular structure from an unsaturated
fatty acid.

......................................................................................................................

......................................................................................................................

......................................................................................................................

......................................................................................................................
(2)
(Total 6 marks)

 
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Q2.          Uric acid is produced in the body. One of the reactions involved in the production of uric
acid is catalysed by xanthine oxidase.

xanthine
 oxidase
xanthine          uric acid

(a)     A sample of xanthine oxidase was tested by mixing with biuret reagent. Describe and
explain the result of this test.

......................................................................................................................

......................................................................................................................

......................................................................................................................

......................................................................................................................
(2)

(b)     Explain why xanthine oxidase is able to catalyse this reaction but it is not able to
catalyse other reactions.

......................................................................................................................

......................................................................................................................

......................................................................................................................

......................................................................................................................
(2)

(c)     Gout is a painful condition caused by uric acid crystals in the joints. It is often treated
with a drug that inhibits xanthine oxidase. The diagram shows a molecule of xanthine
and a molecule of this drug.

Xanthine                                  Drug used

to treat gout

Use the diagram to explain why this drug is effective in the treatment of gout.

......................................................................................................................

......................................................................................................................

......................................................................................................................

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......................................................................................................................

......................................................................................................................

......................................................................................................................
(3)
(Total 7 marks)

Q3.          Read the following passage.

During the course of a day, we come into contact with many poisonous substances.
These include industrial and household chemicals. The skin acts as a barrier and prevents
many of these substances entering and harming the body.

The skin is one of the largest organs in the body. It is composed of several layers of
5        tissue. The outer layer consists of dead cells packed with keratins. Keratins are a group
of proteins that differ from each other in their primary structure. Each keratin molecule
consists of several polypeptide chains, each individual chain wound into a spiral or helix.
The polypeptide chains include many sulphur-containing amino acids and these help to
give the keratin molecules their characteristic strength.

Use information from the passage and your own knowledge to answer the questions.

(a)     What is the evidence from the passage that keratin molecules have a quaternary
structure?

......................................................................................................................

......................................................................................................................
(1)

(b)     Explain how sulphur-containing amino acids help to give keratin molecules their
characteristic strength (lines 8–9).

......................................................................................................................

......................................................................................................................

......................................................................................................................

......................................................................................................................
(2)

(c)     Explain why differences in primary structure result in keratins with different properties
(line 6).

......................................................................................................................

......................................................................................................................

......................................................................................................................

......................................................................................................................
(2)

(Total 5 marks)

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 Q4.          (a)     Describe how you would use a biochemical test to show that a solution contained
protein.

......................................................................................................................

......................................................................................................................

......................................................................................................................

......................................................................................................................
(2)

The diagram shows the structure of two amino acid molecules, tyrosine and phenylalanine.

(b)     Copy from the diagram the R group in the phenylalanine molecule.

 
(1)

(c)     (i)      In the space below, draw the chemical bond formed when these two amino acids are joined
by condensation. You need only draw the parts of the molecules shown in the box.

 
(2)

(ii)     Name this bond.

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.............................................................................................................
(1)

(d)     Tyrosine can be made in the body by hydroxylating phenylalanine. Use the diagram to
explain the meaning of hydroxylating.

......................................................................................................................

......................................................................................................................
(1)
(Total 7 marks)

 Q5.          Sucrose is a disaccharide. It is formed from two monosaccharides P and Q. The diagram
shows the structure of molecules of sucrose and monosaccharide P.

(a)     (i)      Name monosaccharide Q.

.............................................................................................................
(1)

(ii)     Draw the structure of a molecule of monosaccharide Q in the space above.

(1)

(b)     The enzyme sucrase catalyses the breakdown of sucrose into monosaccharides. What
type of reaction is this breakdown?

......................................................................................................................
(1)

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(c)     The diagram shows apparatus used in breaking down sucrose. The enzyme sucrase is
fixed to inert beads. Sucrose solution is then passed through the column.

Describe a biochemical test to find out if the solution collected from the apparatus
contains

(i)      the products;

.............................................................................................................

.............................................................................................................

.............................................................................................................

.............................................................................................................
(2)

(ii)     the enzyme.

.............................................................................................................

.............................................................................................................

.............................................................................................................

.............................................................................................................
(2)
(Total 7 marks)

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Q6.          The diagram shows the structure of the amino acid serine.

(a)     (i)      Draw a box on the diagram around the R group of serine and label the box with
the letter R.
(1)

(ii)     Draw a circle around each of the parts of the serine molecule which would be
removed when two other amino acid molecules join directly to it.
(1)

(b)     (i)      Which two substances are formed when two amino acid molecules join together?

1 ..........................................................................................................

2 ..........................................................................................................
(1)

(ii)     Name the type of bond formed between the joined pair of amino acid molecules.

.............................................................................................................
(1)

(c)     Explain how a change in the primary structure of a globular protein may result in a
different three-dimensional structure.

......................................................................................................................

......................................................................................................................

......................................................................................................................

......................................................................................................................

......................................................................................................................

......................................................................................................................
(3)
(Total 7 marks)

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Q7.Essay

You should write your essay in continuous prose.

Your essay will be marked for its scientific accuracy.

It will also be marked for your selection of relevant material from different parts of the
specification and for the quality of your written communication.

The maximum number of marks that can be awarded is

 
Scientific 16
Breadth of knowledge 3
Relevance 3
Quality of written communication 3

Write an essay on the following topic:

How the structure of proteins is related to their functions.

(Total 25 marks)

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M1.          (a)     (i)      condensation;
1

(b)     (i)      D;
1

(ii)     C;
1

(iii)     A;
1

(c)     absence of a double bond;

in the (hydrocarbon) chain;
unable to accept more hydrogen / saturated with hydrogen;
2 max
[6]

M2.          (a)     Lilac / purple / mauve / violet;

Xanthine oxidase is a protein;

Reject pink or blue as the resulting colour with biuret.
2

(b)     Substrate has specific shape;

Allows binding / fitting / forms ES complex with active site;

Or

Active site has specific shape;

Allows binding / fitting / forms ES complex with substrate;

Accept structure ≡ shape
2

(c)     Xanthine similar shape to drug;

Drug fits active site / competes for active site / is a competitive inhibitor;

Less / no uric acid formed;

3
[7]

M3.          (a)     Several / more than one polypeptide chain in molecule;

Evidence must only relate to 4º structure
1

(b)     Chemical bonds formed between sulphur-containing groups /

R-groups / form stronger disulphide bonds;
Bind chain(s) to each other;
2

(c)     Different number / sequences of amino acids;

Bonds in different places which gives different shape;
2

(d)     Outer layer of skin cells are dead / do not respire

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Do not contain mitochondria / do not produce ATP / release energy;
Cells do not have required proteins / carriers;
3

(e)     Advantages:

1       Small objects can be seen;

2       TEM has high resolution as wavelength of electrons shorter;

Accept better

Limitations:

3       Cannot look at living cells as cells must be in a vacuum;

4       must cut section / thin specimen;

5       Preparation may create artefact

6       Does not produce colour image;

6
[14]

M4.          (a)     (i)      Biuret / alkali + copper sulphate;

Lilac / purple / mauve / violet;
Do not give credit for blue or pink. Ignore references to heating.
2

(b)     R group of phenylalanine copied accurately;

1

(c)     (i)      Bond shown linking carbon and nitrogen;

OH and H removed, =O and –H remaining;
2

(ii)     Peptide bond;

1

(d)     Addition of hydroxyl / OH group;

Candidate must distinguish clearly between hydroxylation and
hydrolysis
1
[7]

M5.          (a)     (i)      fructose;

1

(ii)     correctly drawn (OH group at bottom left);

1

(b)     hydrolysis;
1

(c)     (i)      heat with Benedict’s solution (disqualify if HCl added);

orange / brown / brick red / green / yellow colour or precipitate;
2

(ii)     biuret test / NaOH + CuSO4;

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purple / violet / lilac / mauve;
2
[7]

M6.          (a)     (i)      box drawn around R group (i.e. CH2OH group)
(allow circle if labelled R);
1

(ii)     circle drawn around either of the Hs on NH2 group and circle drawn
around the OH;
1

(b)     (i)      (di)peptide and water;

1

(ii)     peptide;
1

(c)     sequence of amino acids changes;

tertiary structure changes / folds in a different way;
bonds form in different places;
(Reject peptide bonds)
3
[7]

M7.          General Principles for marking the Essay:

Four skill areas will be marked: scientific content, breadth of knowledge, relevance and quality
of language. The following descriptors will form a basis for marking.

Scientific Content (maximum 16 marks)

 
Category Mark Descriptor
16 Most of the material reflects a comprehensive
  understanding of the principles involved and a
  knowledge of factual detail fully in keeping with a
programme of A-level study. Some material, however,
Good 14
may be a little superficial. Material is accurate and
 
free from fundamental errors but there may be minor
 
errors which detract from the overall accuracy.
12
     
10 Some of the content is of an appropriate depth,
  reflecting the depth of treatment expected from a
Average 8 programme of A-level study. Generally accurate with
  few, if any, fundamental errors. Shows a sound
6 understanding of the key principles involved.
     
4 Material presented is largely superficial and fails to
  reflect the depth of treatment expected from a
Poor 2 programme of A-level study. If greater depth of
knowledge is demonstrated, then there are many
0 fundamental errors.

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Breadth of Knowledge (maximum 3 marks)

 
Mark Descriptor
3 A balanced account making reference to most areas that might realistically
be covered on an A-level course of study.
2 A number of aspects covered but a lack of balance. Some topics essential
to an understanding at this level not covered.
1 Unbalanced account with all or almost all material based on a single
aspect.
0 Material entirely irrelevant or too limited in quantity to judge.

Relevance (maximum 3 marks)

 
Mark Descriptor
3 All material presented is clearly relevant to the title. Allowance should be
made for judicious use of introductory material.
2 Material generally selected in support of title but some of the main
content of the essay is of only marginal relevance.
1 Some attempt made to relate material to the title but considerable
amounts largely irrelevant.
0 Material entirely irrelevant or too limited in quantity to judge.

Quality of language (maximum 3 marks)

 
Mark Descriptor
3 Material is logically presented in clear, scientific English. Technical
terminology has been used effectively and accurately throughout.
2 Account is logical and generally presented in clear, scientific English.
Technical terminology has been used effectively and is usually accurate.
1 The essay is generally poorly constructed and often fails to use an
appropriate scientific style and terminology to express ideas.
0 Material entirely irrelevant or too limited in quantity to judge.

[25]

Additional guidance for assessing Scientific Content and Breadth of Knowledge in

Essays

The following provides guidance about topics which might be included in the essays. It is not
an exclusive list; the assessment of scientific content does not place restrictions on topics that
candidates might refer to, provided they are

•        relevant;

•        at an appropriate depth for A level and

•        accurate.

It is not expected that candidates would refer to all, or even most, of the topics to gain a top
mark; the list represents the variety of approaches commonly encountered in the assessment
to the essays.

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In both essays, topics either from the option modules or beyond the scope of the specification
were also given credit where appropriate.

How the structure of proteins in relation to their functions.

1.       Structure (S)

primary structure – peptide bond
secondary structure
tertiary structure. Globular - bonds between R groups give spherical shape – shape
determines function – active sites and receptor sites
(allow quaternary structure – haemoglobin incorporates ions for oxygen transport)

2.       Structural proteins (ST)

fibrous – regular pattern of hydrogen bonds – coiling,
(e.g. keratin coils twist together to form rope-like structures – flexible and  strong)
(e.g. collagen – coils more tightly bound – more rigid)

3.       Transport (T)

channel – complementary shape – charges – gated
carrier – complementary shape – can change shape
active transport – phosphate group attached by energy from
ATP – can change shape

4.       Enzymes (E)

active site, enzyme-substrate complex
activation energy reduction - explanation e.g. brings molecules closer

5.       Receptors (R)

synapse
insulin / glucagon
ADH
rhodopsin

6.       Muscle (M)

actin thin – binding site
myosin thick - cross bridges
tropomyosin – block binding sites

          Breadth of knowledge

3 marks      Four or more of the above 6 areas
2 marks      Three of the above 6 areas
1 mark        Two of the above 6 areas

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E1.          (a)     The vast majority of candidates gained the mark, with only a few confusing
hydrolysis with condensation.

(b)     Most candidates scored full marks, the most common error occurring in (ii) where the
substrate of amylase was identified as protein.

(c)     The difference between the types of fatty acids was well understood in terms of double
bonds but very few candidates then went on to mention the location of the bonds or
describe saturation with reference to hydrogen. Weaker candidates identified the bonds
involved as hydrogen and therefore failed to obtain any marks.

E2.          (a)     Although there was some confusion with Benedict’s test and the use of iodine, the
majority of candidates clearly associated the biuret test with proteins, and were able to
explain that the resulting lilac colour was due to the xanthine oxidase being an enzyme
and therefore a protein. A disappointing number, however, failed to commit themselves,
describing both positive and negative results or suggesting that a lilac colour would be
produced “if a protein was present“.

(b)     Better candidates gave clear and succinct answers explaining specificity in terms of the
concepts of molecular shape and binding to the active site. Others failed to gain credit for
the imprecise use of language.

(c)     In many accounts, it was unclear as to whether the answer was referring to xanthine or
to xanthine oxidase, or to the precise location of the active site with many candidates
clearly of the opinion that it formed part of the substrate. Candidates must appreciate
that they will be tested on their ability to apply their knowledge to material presented in
an unfamiliar context. This is a specification requirement. Those who recognised that
there was a basic similarity in the shape of the two molecules shown, were usually able to
describe the role of the drug as a competitive inhibitor which would prevent the synthesis
of uric acid. Others concentrated on differences between the molecules and attempted to
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draw on a knowledge of chemistry, much of it fanciful and all of it outside the realms of
the specification, in attempting to explain how the drug either bound to xanthine or
dissolved uric acid crystals.

E3.          (a)     Difficulties were experienced with this question where answers were frequently
unselective, relating not only to quaternary structure but to aspects of secondary and
tertiary structure as well. To gain credit here, candidates needed to confine their answers
to the fact that keratin molecules consisted of several polypeptide chains.

(b)     Most candidates clearly appreciated that the bonds formed between sulphur- containing
amino acids were strong and helped to bind the individual polypeptide chains. Less able
candidates often confused these bonds with peptide bonds or did little more than
paraphrase the wording of the question.

(c)     As was not infrequently the case with the answers to many of the questions in this
paper, less able candidates gave the impression of relying on the recall of mark schemes
from broadly similar past questions. In this case they either simply described the primary
structure of a protein, which gained little credit, or described how the primary structure of
a protein affected its tertiary structure which was potentially, at least, a better option.
Those who read the question carefully were usually able to comment on differences in
the amino acid sequence leading to differences in bonding and in molecular shape. There
was some confusion, presumably among candidates who had also completed Module 2 or
3, between amino acids, proteins and bases.

(d)     As in part (c), the principal requirement here was to answer the question as written.
Unfortunately, the response offered by many was no more than a description of active
transport. In this question candidates were expected to use this knowledge along with
information available in the passage to explain why substances were unable to pass
through the outer layer of skin cells. Those who approached the question in the right way
generally pointed out that the cells were dead and progressed to make an appropriate
comment about respiration and the release of energy or generation of ATP. A not
infrequent misconception was that since movement against a concentration gradient
involves active transport, active transport cannot be involved in movement down a
gradient.

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(e)     The many good answers to this part of the question suggested that most candidates had
a clear understanding of the principles of electron microscopy and were able to offer a
lucid account of its advantages and limitations. Less able candidates were usually able to
explain the advantages associated with high resolution but the limitations they suggested
concerning expense, size, the production of black and white images and the need for
technical support were of a more anecdotal nature and seldom gained significant credit.

E4.          (a)     A surprisingly high proportion of candidates failed to identify the required reagent
and either suggested the use of Benedict’s reagent or iodine as a test for proteins. Others
selected the appropriate test but disqualified their answers by referring incorrectly to the
addition of substances such as hydrochloric acid or sodium chloride. Those who based
their answers on the appropriate test were usually able to describe the expected result.

(b)     The significant number of incorrect responses here suggested that many candidates
were unable to apply their understanding of the general structure of an amino acid to the
example shown. The most frequent incorrect responses involved writing out the complete
structure of phenylalanine, giving the general formula of an amino acid, and copying the
R-group from the tyrosine molecule.

(c)     In part (i), able candidates demonstrated their familiarity with the structure of a peptide
bond. Others not infrequently failed to answer the question and wasted much time in
writing out the full structure of both amino acids. Most of the errors arose through linking
carbon to nitrogen by way of an oxygen atom. In part (ii) the bond was usually correctly
identified but there were occasional incorrect references to dipeptide and polypeptide
bonds as well as to glycosidic bonds.

(d)     There were good answers from candidates who made use of the stimulus material and
described hydroxylation as the addition of an OH or hydroxyl group. Others referred
rather imprecisely to the addition of oxygen and hydrogen; incorrectly to the removal of
an OH group or, perhaps inevitably, confused hydroxylation and hydrolysis.

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E5.          (a)     (i)      This question was well answered. Glucose was the commonest incorrect
response.

(ii)     A significant number of candidates failed to gain the mark on this question. The
most frequent error was to change the glycosidic bond to an H group instead of an
OH group. A number failed to use the information in the diagram, drawing a
glucose molecule or six-carbon ring. Inaccurate drawing was also a cause of
candidates failing to gain the mark.

(b)     Condensation was the most common mistake, but most candidates correctly stated
hydrolysis. Hydrolysation was occasionally given.

(c)     The responses to this question were surprisingly varied. Many candidates were either
unfamiliar with reducing and non-reducing sugars and their respective tests, or
misunderstood the action of the enzyme. Many gained a mark for the correct colour
change but gave muddled accounts incorrectly describing the use of hydrochloric acid or
omitting heat. Many candidates gave the Biuret test or stated the correct reagents.
Answers suggesting the mixture should be heated were not penalised. The correct colour
was usually given. The weakest candidates confused the two tests, and in some cases the
test for starch was given.

E6.          (a)     (ii)     Generally well answered with most candidates able to identify the R group.
Fewer candidates correctly labelled an H and the OH group.

(b)     (i)      Most candidates correctly named one substance, but many were unable to name
the second. References to polypeptide, protein and occasionally carbon dioxide,
were frequent.

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(ii)     This was well answered apart from occasional references to hydrogen bonds or
dipeptide bonds. Some misread the question or and gave condensation or
hydrolysis, as answers.

(c)     Many candidates gained full marks, but answers were often poorly expressed and
extended into discussions about enzymes and active sites. Some weaker candidates
confused amino acid sequence with base sequence and discussed the role of DNA.

E7.          More candidates attempted the essay on proteins than that on variation. The majority of
candidates provided a plan, but these varied greatly in their usefulness. Most candidates
attempted to provide essays with a reasonable breadth of knowledge and understanding, but
many included irrelevant material. The quality of written communication was generally poor, as
was the quality of much of the handwriting.

Most candidates had obviously prepared an essay on proteins, but attempts at relating
structure to function were generally weak except for enzymes.

Most essays began with a detailed account of the structure of proteins, but relation to function
generally only began with tertiary structure and proteins. Only the best candidates were able to
give good accounts relating structure to function in structural proteins. Although the ‘lock and
key’ and ‘induced fit’ models of enzyme action are generally well understood, only the very best
candidates related enzyme structure to reduction of activation energy.

Most candidates stated that proteins were used in transporting substances across membranes,
but very few gave structural details of these proteins. Usually, there was very little difference
between descriptions of membrane proteins and enzymes, the term ‘active sites’ being used in
both. It was rare to see descriptions of both channel and carrier proteins, and even more rare
to see explanations of active transport.

Most candidates included material on receptor proteins from module four, usually describing
blood sugar control or synaptic transmission, but rarely relating relevant protein structure to
function.

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Surprisingly few candidates made any real attempt to describe the proteins used in muscle
contraction. Whereas most candidates can describe muscle contraction in answers to module
four questions, relating the structures of actin, myosin and tropomyosin to their functions was
beyond most candidates.

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