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1.3 Biological Molecules:

Proteins

Question Paper

Course AQA A Level Biology

Section1. Biological Molecules

Topic 1.3 Biological Molecules: Proteins

Di cultyMedium

Time allowed: 60

Score: /49

Percentage: /100

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Question 1a
Describe how a dipeptide would form from two amino acids.

[3 marks]

Question 1b
Polypeptides are formed from hundreds of amino acids joined together. A polypeptide

contains 288 peptide bonds.

What would be the total number of amino acids in this polypeptide?

Explain your answer.

[3 marks]

Question 1c
How does a functional protein di er from a polypeptide?

[3 marks]

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Question 1d
There is a general structure that can be applied to all amino acids. Figure 1 below
shows the structure of the amino acid valine.

Figure 1

Draw a circle around the part of the molecule that would be identical in all amino
acids

[1 mark]

Question 2a
Describe how a polypeptide is formed.

[2 marks]

Question 2b
DNA polymerases are a vital group of enzymes. Di erent variations are found in all
living cells. DNA polymerases are responsible for replicating DNA during semi-
conservative replication.

Explain why most cellular enzymes like DNA polymerases are made predominantly from protein.

[5 marks]

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Question 2c
Some washing powders contain molecules that break down and hydrolyse the
peptide bonds between amino acids. The degree to which a protein is broken down
can be called the degree of hydrolysis (DH). The DH value is calculated using the
equation

100 × Number of peptide bonds hydrolysed

DH = Total number of peptide bonds present

Washing powder was applied to a molecule of protein. The DH value after exposure to
the washing powder was 28 and a total of 140 peptide bonds were hydrolysed.
Calculate the number of amino acids in the protein.

[1 mark]

Question 2d
Suggest why it is beneficial for washing powders to contain molecules with the ability
to break down proteins.

[1 mark]

Question 3a
Collagen protein molecules have a quaternary structure and are vital in providing
structural support in a wide variety of organisms. There are di erent types of collagen
but all types share the same basic features.

One of the polypeptide chains that forms a molecule of collagen contains 1049
peptide bonds. Assuming all the chains that form collagen are identical in length, how
many amino acids would be found in a single molecule of collagen?

Explain your answer.

[3 marks]

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Question 3b
Explain why collagen is described as having a quaternary structure rather than a tertiary
structure.

[2 marks]

Question 3c
Scientists wanted to test for the presence of protein while developing a new meal
replacement shake. Describe the test that they should use and state what a positive
test result would look like.

[3 marks]

Question 3d
Compare and contrast the di erent chemical elements found in proteins and
carbohydrates.

[2 marks]

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Question 4a
Explain how a polypeptides’ tertiary structure is determined by bonds between amino
acids.

[4 marks]

Question 4b
Haemoglobin and collagen are both two important proteins found in the human body.
Fill in Table 1 below to accurately describe their properties.

Table 1

Haemoglobin Collagen

Globular or fibrous

Solubility in water

No. of polypeptide chains

Type of helix present

Prosthetic group present

[2 marks]

Question 4c
Describe the function of haemoglobin and collagen. Explain how their structure is
related to their function.

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[2 marks]

Question 4d
Haemoglobin is made of alpha and beta polypeptides. Each alpha polypeptide has
141 amino acids and each beta polypeptide has 146 amino acids. What is the total
number of peptide bonds present in one alpha polypeptide and one beta
polypeptide.

[1 mark]

Question 5a
Figure 1 below shows a single amino acid. Draw out the mechanism by which two
amino acids form a dipeptide.

Figure 1

[3 marks]

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Question 5b
A lab technician investigating the amino acid composition of new food supplement
decided to use paper chromatography to separate out and identify the di erent amino
acids present.

The technician placed a concentrated drop of the food supplement mixture on the
origin line. She then placed concentrated drops of known amino acids at other points
along the origin line. The paper was placed in a tank containing solvent for 2.5 hours.
When the solvent reached the top of the paper, she marked the solvent front using a
pencil. The paper was then sprayed with ninhydrin and heated in a 100oC oven. The
chromatogram results can be seen in Figure 2 below.

Figure 2

Which amino acids are not present in the food supplement. Explain your answer.

[2 marks]

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Question 5c
The Rf value of amino acid C was 0.2. Using the equation below work out the distance
in mm that the amino acid moved from the origin line.

Distance moved by solute ( amino acid )

Rf = Distance moved by the solvent

[1 mark]

Question 5d
The influenza A virus remains a prevalent human pathogen partly because of its ability
to evade human antibodies. The antibodies produced by humans in response to
influenza, are specific to the influenza attachment protein hemagglutinin (HA).
Changes in the influenza HA gene segment prevents human antibodies from binding.
Explain how.

[5 marks]

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