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Answers to EOCQs
Chapter 3
1 B;[1]
2 D;
[1]
3 D;[1]
4 C;
[1]
6 a
maximum activity / optimum pH, is pH 5;
activity gradually increases between pH 2
and pH 5, and decreases from pH 5 to pH 10;
activity very low at pH 2 and pH 10; AW
[max.2]
b
pH is a measure of the hydrogen ion
concentration;
hydrogen ions are positively charged;
hydrogen ions can interact with the R groups
of amino acids;
affects ionic bonding / affects ionisation of
Rgroups;
affects tertiary structure / affects 3D shape of
enzyme;
therefore substrate may not fit active site
(asprecisely);
[max. 4]
[Total: 6]
7 a
optimum temperature;[1]
b
37C; accept 40C
[1]
c
as temperature increases the kinetic energy
of the molecules increases;
the rate of collision between substrate and,
enzyme / active site, increases;
rate of reaction increases;
[3]
d
the enzyme is gradually being denatured;
when the rate is zero the enzyme is
completely denatured;
ORA enzyme loses tertiary structure;
substrate no longer fits into active site
/ active site loses its (specific) shape so
substrate does not fit;
AVP e.g.hydrogen bonds broken / increased
vibration of enzyme molecule;
[max. 3]
10
a replication increases reliability; AW[1]
e
the extra energy which must be given to the
substrate;
b
to act as a reference to show what happens if
before it can be converted into the product;
there is no denaturation; AW[1]
[2] c
40C is the optimum temperature for a
[Total: 10]
mammalian enzyme;[1]
enzyme / amylase (molecules) diffuse(s) from
8 a
succinic acid;[1] d
wells into the agar;
b
malonic acid acts as a competitive inhibitor;
enzyme / amylase digests the starch;
it has a similar shape / structure to succinic
to maltose;
acid;
forms rings / halos, of digested starch around
it therefore competes with succinic acid for a
the wells;
place in the active site of the enzyme;[3]
amount of digestion / rate of digestion, is
c i cysteine;[1]
related to degree of denaturation of enzyme /
ii
SH groups form disulfide bridges;
amylase;
[max. 4]
used to determine tertiary structure;
e
the more enzyme / amylase added, the
heavy metal would prevent formation of
greater the amount of digestion of starch
disulfide bridges;
or
want results to be due to differences in
could change shape of active site;
preheating times, not to differences in
heavy metal could affect shape either by
amount of amylase / enzyme; AW[1]
binding directly in the active site, or by
f
binding at another site which then results
in change in shape of the active site;
Time (heated) at 60C / min Diameter of halo / mm
substrate would not be able to fit into
0
24
active site;
[max. 4]
19
1
iii
(non-competitive) irreversible;[1]
[Total: 10]
10
5
9 a
carry out Benedicts test on solutions A, B
6
10
and C;
a positive result / brick-red precipitate will be
0
30
seen, with the glucose solution;
table drawn with ruled lines for border and
heat separate samples of the two remaining
to separate columns and headings (ideally
solutions, in boiling water bath / to high
ruled lines between rows, but not essential
temperature (e.g. 80C), for suitable time / at
for mark);
least two minutes (enzyme will be denatured);
correct headings to columns with units;
for each heated solution, mix it with an
first column is independent variable (Time
unheated sample of the other solution;
heated at 60C);
leave several minutes / suitable time (for
correct measurements of halos;[4]
reaction to take place);
g
measure the four halos and calculate the
carry out Benedicts test on the two tubes;
mean;[1]
only one will give a positive result (due to
(any anomalous results should be ignored)
presence of maltose) and this will be the one
which contained the unheated enzyme;
Accept alternative wording for all steps in
the procedure, provided the same logical
sequence is described
[max. 6]
b
hydrolysis;[1]
[Total: 7]
Cambridge International AS and A Level Biology Cambridge University Press 2014
h 24
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