2010 A Level Examination

H2 Biology Paper 2 Solutions

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PAPER 1


PAPER 2
Question 1
(a)
A Mitochondrion;;
1. encolosed by double membrane;;
2. inner membrane is folded to form cristae;;

B Rough endoplasmic reticulum;;
1. network of folded membranes forming sheets/ flattened membranous sacs (called cisternae);;
2. presence of ribosomes on surface of ER;;

Examiners comments: Candidates must ensure that when asked for visible features that they
only state features that they can see on the electron micrograph. Some listed sacs or tubes as
features of the rough endoplasmic reticulum. These were not clearly visible on the diagram and
reflect what the candidate had learnt rather than what they could see.

(b) (i)
A - site of ATP synthesis;; R: energy is produced
B site of protein synthesis/ protein transport/ vesicle formation;;

(ii)
A provides ATP for protein synthesis at B;;
Mitochondrial proteins are synthesised at B before transported to A;;

(iii)
Compartmentalisation;;
2010 A Level Examination
H2 Biology Paper 2 Solutions
Page 2 of 8
different conditions are required to maintain optimum conditions for enzyme reaction/ to
increase surface area;;
AVP:
maintain high concentrations of reactants at specific sites;;
provide different local environments that facilitate biochemical pathways;;
prevent intermediates of one pathway from mixing with those of another;;
ensure that harmful substances are enclosed within structures and hence, kept away from the
rest of the cell;;

Question 2
(a)
DNA polymerase only works in one direction from 5 to 3, adding new nucleotides to the free 3
end;;
the two parental DNA strands are antiparallel;;

(b)
both strands of parental DNA separate and act as templates for the synthesis of daughter DNA
strands;;
each daughter DNA double helix comprises one parental DNA strand and one daughter DNA
strand;;

(c)
deoxyribonucleoside triphosphate/ ATP/ helicase/ DNA ligase/ RNA primer/ primase [any three]

(d)
DNA polymerases may insert the wrong nucleotides, or too many or too few into the sequence;;
Repair enzymes failed to recognised these improperly paired nucleotides;;

(e)
Most of the descriptions given centred on either sickle-cell anaemia or oncogenes and were
well known. Candidates must ensure that they describe the whole process and not miss the
initial effects in an attempt to include all of the detail they have learnt about a given mutation.
Many candidates began their responses beyond the immediate effect of a mutation, namely the
alteration in the base sequence or codon and the subsequent change in amino acid.

Sickle-cell anaemia
caused by a single missense mutation/ base pair substitution of the -globin gene;;
due to this mutation, the glutamic acid (hydrophilic) in the normal polypeptide is changed to a
valine (hydrophobic) in the mutant polypeptide;;
this alteration generates a sticky patch on the surface of the -chain , the deoxygenated form of
the mutant Hb (HbS) is insoluble in erythrocytes and forms crystalline arrays;;
the erythrocytes of affected individuals become rigid and their transit through capillaries is
blocked, causing severe pain and tissue damage;;

Question 3
(a)
tail sheath;;
base plate;;

(b)
1. T4 phage tail fibres bind to specific receptor sites;
2. on host bacterium cell wall;
3. The tail sheath contracts;
4. driving a hollow tube;
5. through the bacterial cell wall;
6. The T4 phage dsDNA genome is injected into the bacterial cytoplasm;
2010 A Level Examination
H2 Biology Paper 2 Solutions
Page 3 of 8
(c)
Feature Lytic cycle Lysogenic cycle
Integration
of viral
genome
Viral genome is not incorporated into the
bacterial chromosome/ the host cells
genome is hydrolysed;
Viral genome is incorporated into the
bacterial chromosome;
Lysis of host
cell
Replication of virus culminates in lysis
and death of host cell;
The phage genome replicates
without killing the host bacterial cells;
Number of
host cell
infected
Only 1 host cell is infected; The host cell divides, viral DNA also
replicates, results in many daughter
cells infected with prophage;
Initiation of
lytic pathway
Viral DNA can immediately initiate the
lytic pathway after entering the host cell;
Prophage enters the lytic pathway
upon stimulation;
Synthesis of
viral protein
Synthesis of phage proteins occurs
immediately after entry;
Transcription of prophage genes is
blocked by lambda repressor;

(d) (i)
Presence of capsid enclosing the viral genome;;
Capsomeres are arranged in a precise and symmetrical pattern around the nucleic acid;;

(ii)
Absence of tail/sheath/collar;;
Presence of RNA instead of DNA;;

Question 4
(a)
A- Nucleosome;; Reject: nucleosome core, solenoid
B - Deoxyribonucleic Acid or linker Deoxyribonucleic acid;; Reject: abbreviation

(b)
Packaging of eukaryotic genomic DNA into nucleosomes
1. makes it compact/ condensed; thus DNA can be packed / contained within the cells
nucleus;
2. shields the nitrogenous bases from the enzymes in the nucleus; thus preventing DNA
mutation; reject: prevent degradation by enzymes
3. prevents the long DNA molecules (of different chromosomes); from getting knotted or
tangled;
4. prevent the access of transcription factor if promoter is part of the nucleosome, regulating
gene expression/ transcription;;
[any three]

(c)
methylated histones are bound to proteins; OR which prevents histones from being acetylated
by histone acetyltransferase ;
positive charge on histone tail is maintained;
thus histone tail continues to interact with other nucleosomes; to result in a condensed
chromatin structure;
implication: transcription factors/RNA polymerase are not able to access the gene;;

(d)
only a particular sub-set of proteins are involved in cell differentiation;
only certain genes need to be expressed;
large numbers of genes need not be expressed/turned off; i.e. chromatin needs to be of the
condensed structure;
a high proportion of genome is non-coding/ large size of genome;;


2010 A Level Examination
H2 Biology Paper 2 Solutions
Page 4 of 8
(e)
reference to operator site; located in the promoter region;
reference to an active repressor protein; that binds to the operator site; Reject: regulatory
protein
RNA polymerase; prevented from binding the promoter;

Question 5
(a)
continuous variation;;

(b)
characteristic is controlled by many genes;;
each gene would have little overall effect;;
each individual allele has similar and additive effects on the same character;;
phenotypes are influenced by the environment;;

(c)
parents & F1 - individuals all genetically identical: all homozygous for parents, all heterozygous
for F1;
parents & F1 variation is due to only environment;

genotypes of F2 more varied than parent and F1:
formed as a result of meiosis in the formation of gametes (from F1);
processes such as independent assortment of homologous chromosomes;;
crossing over (between linked genes forming new linkage groups) leads to new combination of
alleles;;
random fusion of gametes during fertilization;;
each gene has its own number of alleles, leading to a large number of possible combinations of
alleles;;
phenotypes are influenced by the environment;;


Question 6
(a) (i)
ref to reduced NAD
+
(i.e. NADH/H
+
); or reduced FAD (i.e. FADH
2
) as immediate source of
electrons;
ref. to NAD
+
and FAD removing a pair of hydrogen atoms;
from respiratory substrates in glycolysis, link reaction and krebs cycle;;

(ii)
electron pairs combine with oxygen atoms;; which are very electronegative
each oxygen atom simultaneously picks up a pair of hydrogen ions from the aqueous solution;
forming water as the final product;

(iii)
allows a proton gradient to develop across the inner mitochondrial membrane;;
ref. to proton gradient as a source of potential energy for the synthesis of ATP;;

(b)
1. electron flow along the ETC from A to B releases free energy in a series of small steps;
2. free energy released is coupled to the pumping of protons;
3. across the inner mitochondrial membrane; from the mitochondrial matrix into
intermembranal space , i.e. C;
4. ref to inner mitochondrial membrane being impermeable to protons;;

2010 A Level Examination
H2 Biology Paper 2 Solutions
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(c)
Features Photophosphorylation Oxidative Phosphorylation
Sources of energy energy for making ATP comes
from light
energy for making ATP comes
from oxidation processes
Location

Thylakoid membrane of
chloroplast
Inner membrane of mitochondria
Electron donors

For non-cyclic reaction: water;
For cyclic reaction: PS I
NADH, FADH
2


Electron acceptors

Non-cyclic acceptor: NADP
+

Cyclic acceptor: PS I
Oxygen

Establishment of
proton gradient

H
+
pumped inwards, from stroma
to thylakoid space

H
+
pumped outwards, from matrix
to intermembranal space
[Any three]

Question 7
(a)
ref subjected to different selection pressures favouring different phenotypes;;
Birds with favourable phenotype survived and reproduced, passed on the alleles to the next
generation;;
ref to geographical isolation, no interbreeding and no gene flow;;

(b) (i)
the fossils shown are incomplete or damaged;;
limited structural similarities of the fossil skulls, it can be subjective;;
common ancestor skull is missing;;

(ii)
Quantifiable differences in base sequence can be counted/ every nucleotide will be a point of
comparison, e.g. if homologous regions of DNA from two species that are 1,000 nucleotides
long provide 1,000 points of comparison;;
Objective - Molecular character states are unambiguous: A, C, G and T are easily recognizable
and one cannot be confused with another;;

(c)
insufficient time for evolution of flightless birds;;
flightless birds are unable to cross the sea separating the islands;;

Section B
Question 8
(a)
1. E. coli regulates the production of the enzymes involved in lactose metabolism through
the lactose operon;

In the presence of lactose:
2. lactose enters bacterial cell;
3. lactose is converted to allolactose which binds to repressor protein;
4. results in a change in shape of repressor protein/inactive;
5. repressor protein no longer attached (to DNA/operator);
6. exposes operator site;
7. allows RNA polymerase to bind to the promoter;
8. transcription (of genes coding for proteins required to utilize lactose);
9. leading to synthesis of enzymes -galatosidase, permease, transacetylase;
10. with higher lactose concentration, more repressor proteins are inactivated more
transcription;
2010 A Level Examination
H2 Biology Paper 2 Solutions
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In the presence of both lactose and glucose:
11. only glucose is used;
12. In the presence of glucose, [cAMP] drops;
13. CAP is inactive and disengages from CAP binding site;
14. Though RNA polymerase binds to the promoter;
15. transcription occurs at a low level low levels of enzymes is produced;

(b)
1. Low blood glucose concentration below normal level is detected by -cells ;
2. Glucagon is secreted by -cells; of the islet of Langerhans; that will bind with receptors on
their liver (target) cells;
3. hormone-receptor complexes interact with G proteins and activate adenyl cyclase
4. which converts adenosine triphosphate (ATP) to cyclic adenosine monophosphate
5. cAMP activates protein kinase A, which subsequently phosphorylate relay proteins
6. transduced signal triggers cellular responses which include:
a. activation of enzymes involved in glycogenolysis;
i. the stored glycogen is converted to glucose; which can be metabolised for energy
or released into the bloodstream;
ii. enzymes involved in glycogenesis is inhibited;
b. activation of enzymes involved in gluconeogenesis;
i. Conversion of amino acids, fatty acids and glycerol to glucose;
7. Raising the blood glucose level to the norm;

(c)
1. Reception: signalling molecule from outside the cell binds to a receptor protein located at
the cells surface (cell membrane receptor) or inside the cell (intracellular receptor).
2. binding site of receptor is specific for a single chemical messenger (ligand), i.e. the
complementary fit
3. Transduction: ligand-receptor interaction changes the receptor protein, initiating the
process of transduction.
4. a multistep pathway whereby proteins are activated by: addition or removal of phosphate
groups; or
5. production / release of second messengers e.g. cAMP or ions (e.g. Ca
2+
)
6. Response: The transduced signal finally triggers a specific cellular response in the nucleus
or, in the cytoplasm
7. Activities include:
a. Protein synthesis:
i. Activation of protein synthesis: synthesis of mRNA, which will be translated in the
cytoplasm into a specific protein
ii. Inhibition of protein synthesis
b. Protein Activity
i. opening / closure of ion channels e.g. opening of voltage-gated calcium ion
channels in synaptic knob as a result of depolarisation
ii. activation / inhibition of metabolic enzymes e.g. glycogen synthetase in
carbohydrate metabolism, cyclin-dependent kinases in cell cycle control
iii. regulation of overall cell shape.

Question 9
(a)
1. reference to a central carbon atom (i.e. the -carbon atom); to which is bonded:
a. an amino group (-NH
2
);
b. a carboxyl group (-COOH);
c. a hydrogen atom; and

2010 A Level Examination
H2 Biology Paper 2 Solutions
Page 7 of 8
d. an R-group (or side chain); which is variable
amongst the 20 different amino acids;
occurring in nature.
2. a condensation reaction occurs between the carboxyl group of one amino acid; and the
amino group of another;
3. a molecule of water is removed in the condensation reaction;;
4. condensation reaction is catalysed by peptidyltransferase, a component of the large
ribosomal subunit;;


(b)
1. primary structure is the specific sequence of amino acids in a polypeptide chain;
a. specificity due to : (i) identity of amino acid at each position; and (ii) order of amino acids;
b. held by peptide bonds;
c. between amino and carboxyl groups;
2. in secondary structures, segments of the polypeptide chain are repeatedly; coiled or folded;
as a result of
a. held by hydrogen bonds;
b. at regular intervals along the polypeptide backbone;
3. tertiary structure is specific 3-dimensional conformation; in which polypeptide chain usually
bends and folds extensively;
Accept: precise, compact, globular shape
a. held by disulfide bonds, ionic bonds, hydrogen bonds and hydrophobic interactions;
b. formed between the R-groups of amino acid residues;
c. that are far apart in the linear sequence of the polypeptide chain;
4. quaternary structure comprises more than one; polypeptide chain / subunit;
a. held together by R-group interactions;
b. between subunits;

(c)
1. named globular protein: haemoglobin (Hb); Accept: enzyme
2. specific function: transport of oxygen; Accept: catalysis
3. globular in shape;
a. many Hb molecules can be packed into a single red blood cell;
4. consists of four subunits;
a. each subunit is capable of binding one O
2
molecule;
b. subunits exhibit cooperative binding of O
2
molecules;
c. cooperative binding maximises both the amount of O
2
loaded at the lungs and the
amount of O
2
released at the tissues;
5. bulk of the hydrophobic amino acids are buried in the interior; of the globular structure whilst
the hydrophilic amino acid residues are on the exterior;
a. haemoglobin molecule is soluble in the aqueous medium of blood;
6. haem-binding site is lined with hydrophobic amino acid residues;
a. to provide a hydrophobic environment for the binding of haem, which is largely
hydrophobic
7. haem group consists of a porphyrin ring and an iron (II) ion, Fe
2+
; Fe
2+
can combine
reversibly with O
2
;
2010 A Level Examination
H2 Biology Paper 2 Solutions
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a. enhances the release of O
2
in metabolically active tissues such as muscle;