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2.3 Proteins
Question Paper
Course CIE A Level Biology

Section 2. Biological Molecules
Topic 2.3 Proteins
Difficulty Hard
Time allowed: 70
Score: /51
Percentage: /100
Page 1 of 12
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Question 1a
Fig. 1 shows the structure of myoglobin, an oxygen transporting protein found in muscles. Myoglobin is responsible for receiving oxygen
from the blood and transporting it to the mitochondria of muscle cells in order for cellular respiration to occur. Oxygen molecules will bind
to group X indicated on the diagram.
Fig. 1
Compare the structure of myoglobin, shown in Fig. 1, with haemoglobin.

[4 marks]
Page 2 of 12
Question 1b
Fig. 2 shows the oxygen dissociation curves for myoglobin and haemoglobin.
Fig. 2
(i)
Explain the difference in the dissociation curves in Fig. 2.
[3]
(ii)
Estimate the percentage saturation of myoglobin if the partial pressure of oxygen is 20 mmHg.
[1]
[4 marks]
Question 1c
Explain how the tertiary and quaternary levels of protein structure enable haemoglobin to perform its role in the transport of oxygen.
[3 marks]
Page 3 of 12
Question 2a
Albumin is a protein found in the plasma of the blood.
The gene that codes for human albumin is 16 961 DNA bases long. The protein is made up of 585 amino acids.
Calculate the ratio of non-coding to coding DNA in the albumin gene.
[3 marks]
Page 4 of 12
Question 2b
Fig. 1 shows the molecular structure of human albumin.
Wardell, M., Wang, Z., Ho, J.X., Robert, J., Ruker, F., Ruble, J., Carter, D.C.;visualization author: User:Astrojan, CC BY-SA 4.0 <https://creativecommons.org/licenses/by-sa/4.0>, via Wikimedia Commons
Fig. 1
(i)
Identify one example of secondary structure visible in Fig. 1.
[1]
(ii)
Describe the bond(s) found in the example identified in part (i).
[2]
[3 marks]
Page 5 of 12
Question 2c
Egg whites are mostly made of albumin.
When the albumin in egg white is denatured it changes the white of the egg from a colourless liquid to a white solid.
A student wanted to investigate how temperature affects the denaturing of albumin.
Outline a method that the student could use to carry out this investigation.
[4 marks]
Question 2d
When the albumin in the egg white is not denatured it is soluble in water, however, when it denatures it becomes insoluble.
This is due to the same mechanism that causes the colour change.
Explain how the albumin protein can have different properties before and after denaturing.
[2 marks]
Question 3a
A theoretical polypeptide chain is 26 amino acids long.
Calculate the number of different possible combinations of amino acids that could exist within this chain.
Give your answer in standard form.
[2 marks]
Page 6 of 12
Question 3b
In some rare circumstances some organisms have been found to contain unusual amino acids that are not shared with the
majority of other organisms.
Selenocysteine is one of them, and is shown in Fig. 1 below.
Fig. 1
Using the information in Fig. 1, state what makes selenocysteine so unusual.
[1 mark]
Question 3c
Use the information in Fig. 1 to draw the formation of a dipeptide from two molecules of selenocysteine.
[2 marks]
Question 3d
Some amino acids exist that have been artificially synthesises in a laboratory. These amino acids have never occurred in the
proteins of living organisms.
Describe the features that must exist in these synthetic molecules in order for them to be classified as amino acids.
[3 marks]
Page 7 of 12
Question 4a
Insulin is a protein that is produced naturally by most individuals. Patients with insulin-dependent diabetes, however, cannot
produce insulin and rely on injecting insulin to replace the protein that they cannot produce for themselves.
Suggest why the insulin must be injected into the blood instead of being taken orally.
[2 marks]
Question 4b
Many years ago insulin used to be taken from cows and pigs to treat people with diabetes.
Using your knowledge of protein structure, suggest why pig and cow insulin was less effective at regulating blood glucose
levels than human insulin.
[2 marks]
Page 8 of 12
Question 4c
Another example of a protein found in humans is fetal haemoglobin, the structure of which is shown in Fig. 1 below. Fetal
haemoglobin is the main type of haemoglobin found in a fetus up until birth. Fetal haemoglobin has a higher affinity for oxygen than adult
haemoglobin.
Fig. 1
(i)
Using the information in Fig. 1 and your knowledge of the structure of haemoglobin, contrast the structure of fetal
haemoglobin with that of adult haemoglobin.
[1]
(ii)
Suggest the impact of the difference in structure identified in part (i).
[1]
[2 marks]
Page 9 of 12
Question 4d
Fig. 2 below shows part of a haemoglobin molecule.
Fig. 2
(i)
Identify the part of the haemoglobin molecule shown in Fig. 2.
[1]
(ii)
Explain how the part identified at (i) facilitates the role of haemoglobin.
[2]
[3 marks]
Question 5a
Haemoglobin is a protein whose function depends on a prosthetic group.
Define the term prosthetic group and describe the components that make up the prosthetic group of haemoglobin.
[3 marks]
Page 10 of 12
Question 5b
Outline the mode of operation of the prosthetic group within a haemoglobin molecule.
[3 marks]
Question 5c
An individual red blood cell is thought to contain 280 million haemoglobin molecules.
Calculate how many oxygen molecules are bound within a single red blood cell when the cell is 7% saturated with oxygen.
State your answer to 2 significant figures.
[3 marks]
Question 5d
Explain why a prosthetic group is needed in a haemoglobin molecule.
[2 marks]
Page 11 of 12
Page 12 of 12

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Course CIE A Level Biology

Compare the structure of myoglobin, shown in Fig. 1, with haemoglobin.

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