41

(b) Glycogen may be broken down to form glucose. For

Examlnen
Fig. 2.2 sho\Ns region X from the glycogen molecule In Fig. 2.1 In more detail. u..

F1
H~o~o~o~o-
~:1 f~1
H OH H OH H OH H OH

. Fig. 2.2

Draw an annotated diagram in the space provided to explain how a glucose molecule is
formed from the free end of the glycogen molea.ile shown in Fig. 2.2.

{3]

[Total: 8]

08 9700/02/0/NJ'08
 42

AnS'Ner all the questions. F

Eran
u
1 (a) Fig. 1.1 shows the breakdown of a molecule of sucrose.

T
HOC~

HOCH2

a-glucose fructose
Flg.1.1

(I) Name the bond indicated byT.

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

(II} State the name given to this type of reaction in which water is involved .

..............................................................................................................................(11

(Ill) State two roles of water within plant cells other than taking part in breakdown
reactions.

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

2............................................................................................................................ (2]

(b) Enzymes are globular proteins. .

State what is meant by the term globular'.

..................................................... ,, ...............................................................................................
..............................................................................................................................................................................................
. ....................................................................................................................................... .
...................................................................................................................................... (21

0 9700/21JMIJ/10
 43

3 Starch is composed of two polysaccharides, amylose and amylopectln . .

Fig. 3.1 shows a molecule of a-glucose before being added to the end of a molecule of
amylase.

..... 0 0 0

H OH H OH H OH H OH

Fig. 3.1

(a) (I) Complete Fig. 3.1 to show how a molecule of a-glucose is added to the amylose.
[3]

(Ir) Name the bond that forms between glucose molecules in polysaccharides, such as
amylose.

.............................................••••..•.•.•......._. .................•............................................ [1]

(b) Glycogen and cellulose are two other polysaccharides.

Complete Table 3.1 to compare glycogen and cellulose with amylose.

Table3.1

feature amylase glycogen cellulose

monomer a-glucose

branched or
unbranched unbranched
molecule

role in
energy storage
organisms

[3]
 44

4 ..

2 Polysaccharides, such as glycogen, amylopectln and amylose, are formed by polymerisation

of glucose. Fig. 2.1 shows part of a glycogen molecule.

Flg.2.1

(a) Wrth reference to Fig. 2. 1,

(I) desaibe haw the structure of glycogen differs from the structure of amylase;

··············································································•····•··•···•································· [2]
(ii) desaibe the advantages for organisms in storing polysaccharides, such as
glycogen, rather than storing glucose.

•••••••••••••••••••••••••••• .. • .. ••• .. •• .. ••••••• .. •••oa•••••••••••••••• .. ••• • ••••• .. •• ....••• .. ••••••••••• .. ••••oa••• •• ••••••••••••••••••••

.......................................................................................................................................
····························•···········•····················•·········. ···········................................................. .
•••••• • ••••••••••••• .. ••• .. ••••• • ••••••••••• .. •••••••••••••u•• .. ••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••••

················································································•······•·······•·••························· [3]

18 970002/0/N/08
 45

12

5 Fig. 5.1 shows a diagram of the molecular structures of tristearin (a triglyceride) and
phosphatldylchollne (a phosphollpld).

H CH3
I I
H-C-N-LCH
I ' a
H-C-H CHa

6
o=t-o-
1
H H H H H 0
H-!-6-6-H
I I I
H-C-C-C-H
I I I I I I
0 0 0 0 0 H
I I I I I
C=O C=O C=O C=O C=O

tristearin
phosphatidylcholine

Flg.5.1

(a) Table 5.1 shows a structural difference between the two molecules shown in Fig. 5.1.

Complete Table 5.1 with two further structural differences other than in numbers of different
types of atoms.

Table 5.1

structural feature tristearin phosphatidylcholine

length of fatty acid chains all the same length different lengths

(2]
 46

2 Scientists have developed a variety of ways to represent the three dimensional structure of
proteins. Fig. 2.1 shows one way of representing the structure of the protein, haemoglobin.

Fig. 2.1

(a) (I) Name A and state its role.

name ........................................................................................................................

role ..•...•.•.•....•.•....................•......•.......•••..•.•.•..••••.•••....•.••.•..•.....•.•••.•••..•••...••.•••••.•.....

··········································································. ················ -······································

•·•••••·••••···•••••·••·····•·•·····•• -......................................................................................(3)

(ii} With reference to Fig. 2.1, explain why a molecule of haemoglobin is said to shCNV
both tertiary structure and quaternary strucue.

·····························································································........................................... .
·····························•···································•··············•···················•··•··························
................................................................................... ...........................................................
............................................................................ ................................................................................................................. ................................. ...................

··········································· ........................................................................... _...... [2)

7 9700A:l21Cln<W7
 47

3 Fig. 3.1 shows a molecule of haemoglobin. For

Ellnwlm
Un

Flg.3.1

(a) Explain how a molecule of haemoglobin shows the four levels of organisation of protein
molecules. .

primary structure ..............................................................................................................

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

., ............................................................................................................................................................................................................................................. .
secondary structure .........................................................................................................

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

,

........................................................................................................... -........................................................................................ .
tertiary structure ..............................................................................................................

,, ........................................................................................................................................
··································· . ·························•·········································· ....................................
·quaternary structure ........................................................................................................

, ............................................. ,.............................................................................................
.,........ ,...... ,,.. ,, .... ,.. ,.. ,........,, .............. ,...................... ...................................................... [4]

OUOW2011 9700J21/Q'Nl11
4 Penicillin is an antibiotic that Interferes ~§i the synthesis of cell walls in bacteria. Even before
penicillin became widely available In the 1940s, the enzyme penicillinase which breaks down
penicillin had been Isolated. This enzyme Is now found In many bacteria and giveS them
resistance to penlcillln.

Fig. 4.1 is a ribbon model of the structure of the enzyme peniclllinase. The arrC1'N indicates
the active site of the enzyme.

Flg.4.1

(a) Explain why the shape of the active site of an enzyme, such as penicillinase, is important.

........................................... ..................................................-....................................................
.................................................. ...................................................................................................................
························································•·····•··································. ·························•·····•···•··•·
...................................................................................................................................(3)
(b) Wrth reference to Fig. 4.1, identify the aspects of protein structure that are shown and '
those that are not shown.

aspects of protsln structure shown

······················································.......................................................................................... .
...... ................ ........... ........ . . .. ... ................ . .......... ....... ................ ........ .. ······~ .........................................
-.

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

... .......................... .... .... ........ .................................. ...................... ...... .. ... .. .................... ~······· .........
aspects of protein structure not shown

......................;·•· . ··.................................................................................................. ................................................ .

··•·•··•··••······•·································· .....................................................................
...........................................................................................................................
········· ............................................................................................................................. [3]
(b) Carbonic anhydrase Is an enzyme that lsJ,Jnd in blood, liver and kidneys.
Fig. 4.2 shows a molecular model of this enzyme.

Flg.4.2
(I) With reference to Fig. 4.2 and the parts labelled P and Q, explain the term secondary
structure.

··············· . ························································ . ...................................................................

................................................................................................................. ,. ........ ...................... .
···········································································································································
...........................................................................................................................................
······•······························································•·····································································
······································································--···································································
······· ................................................................................................................................ [31

(c) The walls of the trachea and bronchi contain elastic fibres.

Elastic fibres are made of bundles of the.fibr,ous protein .elastin.

• Each molecule of elastin is -a single polypeptide.

• 'T!he primary structure contains a large proportion of the amino acid glycine.
• Glycine has a hydrophobic R group.
• Glycine does not occur at regular intervals in the polypeptide.
• The polypeptide forms random coils that change shape as the elastic fibres are stretched
and recoil. .
• Elastln molecules are. joined to each other by many covalent bonds to form a
cross-linked network.

Describe two ways in which the structure of a collagen molecule differs from the structure of
an elastln molecule described above.

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

··················································································································································
.) ······················································································· ·····································"
••••• • ••••• • ••••• •• ••• ••• •• •••• •••• ••• •••••• ••• •• •• ••••••••• •••••••••••••• ••••• •• ••• • •••••• • •••• ••••••••••••• ••••• •••••• •••• ••••••• ••• •• ••• ••• •L-.i
 50

5
3 Fig. 3.1 ahow1 the 1truotur1 of th e enzyme ly1ozyme.

Fig. 3.1

(a) (I) Name the two types of covalent bond In the structure In Fig. 3.1 .

.. ... .. ... .. .... ..... .. ............. ............. .... .......... ... .. .. ..... .. .. .. .. ........ ..... .... ..... ............... .. .. ..........,t1l

(II) The primary structure of lyaozyme Is shown In Fig. 3.1.

Explain the meaning of the term primary structure.

I 1# , 1 , I I • 11 I I I Io lo I o o I I If I I I If f I Ito I I I f 1 1t fII I1 1111 I t I I I I t I f 11 I I I If 111 I I I ' I I I I I I I I . I \ I • I , I I \ 11 1 I I \ t \.t 1 > 1 1 I 1 • > 1 \ \ 1\. 1 \ ' \ 11 ._ , , , , t , , \ ', , ._, , , , , '< 1

11'100/11 /0,t,IIHI
 51

3 ~- 3.1 shows seven biological molecules, labelled D to K. For

&llffllnlr'I
0 u.e
D G

0 ~NH
II
HO-P-0~
.. Ac;>
I o
o·
H OH OH OH

E S-H
H o CH:.
I 11 I
CH2 H2N C CH OH
I '/'./'./
H:zN-C-COOH CH2 N C
I II
I H C
H

J
H
H CHs I
I I H2N-C-COOH
H-c-N•-cHs I
I ""- H
H- C- H CH3
I
0
I
F O=P-O" K
I
H H 0 H H H
I I I I I I
H-c-c-c-H H-c-c-c-H
I I I I I I
o O H 0 0 0
I I I I I
C=O C=O C=O C=O C=O

Fig. 3.1

)8
9700J02/M/J/08
 52

(a) Table 3.1 contains statements about the biological molecules in Fig. 3.1.
E
Complete the table by selecting the biological molecule from Fig. 3.1 that matches each
of the statements. Write the appropriate letter from Fig. 3.1 in the table. The first one has
been done for you.
You may use each letter once, more than once or not at all.

Table 3.1

statement letter
an amino acid that is a major constituent of collagen J
a component of RNA

a molecule that Is polymerised to form glycogen

a molecule with a peptide bond

an important store of energy, insoluble in water

a molecule with hydrophDic end hydrophobic regions
an amino acid that forms disulfide (disulphide) bonds in proteins [6]

(b) Describe two ways in which the structure of DNA differs from the structure of collagen.

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

2 .................................................. ·................ ·............................ _......................................

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

[Total: 8]

18 9700/02/M/J/08
 53

12

5 Fig. 5.1 shows five different biological molecules.

CH 2OH H OH CH2OH

, ~ o , P ~ Jt~y'\
K
'c,~ ~ o / b ~ H
H OH CH OH H OH

: '°~
2

L
H H 2
0~ .
HO{;CH
O
o~o
H OH H OH
OH ""CH2 OH
0 I I
OH CH-CH
I I I
CH2OH CH 2OH CH2 CH2OH HN CH
I I
C=O HC
, ~H O H ~O H H ~O H H ~OHH 1 I I
\ OH H OH H H H H H ,' CH2 CH 2
O O O O O
H 00 H 00 H 00 H 00

M
CH2OH CH 2OH . ·cH 2OH CH2OH

, ~H O H ~OH H~· O
HH~H OH 1

\ H H H H H H OH H ,'
0 0 0 0 0
H 00 H ™ H 00 H 00

Fig. 5.1

9700/2.1/M/J/11
 54

13

Complete Table 5.1 by indicating which molea.ile matches each statement

You may use each letter (H to M) once, more than once or not at all.

You should write only one letter in each box.

Table 5.1

statement letter

contains peptide bonds

part of the molea.de forms the hydrophobic part of cell
membranes
contains 1-4 and 1-6 glycosidic bonds
forms the primary structure of a protein
used for energy storage in plants
forms a helical structure
the sub-unit molecule is fl-glucose

[Total: 7]

,'J
9700/21/M/J/11 [T
 55

2 KeraUn and chitin are two important biological molecUeS Kerati1 is i::u'1d in ha.-, u aR:f an ,.,
Chitin is a modified polysaccharide found in a runber d different aganisms. iJr ~ ,pie~ ii:alllli
fungal cell walls and the hard outer skeletons cl insectS.

(a) Features of chitin and keratin are shc7.Yn in the boxes in Fig. 2.1 .

Keratin and chitin are

insoluble in water

example: cellulose
triglycuide
amylopectin
collagen

Keratin and chitin have Keratil is a fbous prceSl

structural functions

The monomers of chitin Keratil and chlirt contai't

are 1.4 linked nitrogen

Fig. 2.1

Write, in each box, the biological molecules from the Ust below that the same
feature.
Each box may contain one, or more than one, biological molecule. The first box has
been completed as an example.

amyk>pectln
'celh,llose
collagen
haemoglobln
mRNA
triglyceride

Q700,.2210t'Wt [Tu
 56

14

(c) Wafl!/f has many roles to play in cells and &mg organisms.

Canplele Table 52 below by slm1g 1he property of waler that alkMs each of 1he foloWWl9 to
take place.
Tabte5.2

role of water property of water

solvent for gtucose and ions

mowment in xylem
1

helps to decrease body

temperature in mammals

[3]

[Total: 9]
 57

Ill

humpback whale

kr:,~
. f
(small crustaceans)

phytoplankton
not drawn to scale (very small photosynthetic organisms)

(c) Desaibe the roles of water as an environment for organisms, such as those shown in
Fig.3.1.

····················································•················································· .................·-·······················
······························································· ...................................................................·-···························
..........................................................................................................................................
............. ···•·····························•····•··· ., ............ ··········································--·················· ........
················•··•······················ ................................................... ·············· ····································
··············•···•·······················································································•·······························
.................................................................... ·······•············ ..................................... ·············
..........................................................................................................................................
................................................................. .................................................................... [3]

[Total: 10]

9700/22/0/N/12
[Tum,
CUCLES2012