Proteins Exam QS

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Proteins Exam Questions

1. (a) Insulin and collagen are both proteins that have a primary structure made up of amino
acids joined together by peptide bonds.

(i) Explain what is meant by the term primary structure of a protein.

....The primary structure of a protein is comprise of a linear chain of amino


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

(ii) Name the type of reaction that occurs when a peptide bond is broken causing a
dipeptide to split into two amino acids.

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

(b) Insulin and collagen both contain the amino acids glycine and serine. The diagram below
shows a dipeptide formed from these two amino acids. Complete the diagram to show the
structure of serine when the peptide bond breaks.

H O H H
H O
N— C— C— N— C— C
H OH
H CH2

OH

H
H O
N— C— C +
H OH
H

G ly c ine S erin e
(1)
(Total 3 marks)

2. Proteins have a wide range of functions in living organisms. The function of a protein is related
to its precise three-dimensional shape, which is determined by its specific sequence of amino
acids. The diagram below shows a model of a typical protein molecule.

(a) (i) Complete the diagram below to give the structure of the amino acid glycine.

H
(2)

(ii) Explain how a specific sequence of amino acids can form the precise three-
dimensional shape of a protein molecule.
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(3)
(Total 5 marks)

3. (a) The diagram below shows the structures of two amino acids, alanine and serine.

H H O H H O
N C C N C C
H CH OH H CH 2 OH
3

OH
A lan in e S erin e

In the space below, draw a diagram to show a dipeptide formed when these two
molecules bond together.

(2)

b) Computer-generated models were used to measure the length in nanometres (nm) of a


polypeptide containing a large number of amino acids. Measurements were made of the
primary and secondary structure of the polypeptide. The models were used to measure the
length of the polypeptide at 25 °C and at 55 °C. The results are shown in the table below.

Length of polypeptide/nm
Structure of polypeptide at 25 °C at 55 °C
Primary 505 505
Secondary 48 70

(i) Explain what is meant by the term secondary structure of a protein.

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(2)

(ii) Compare the results obtained at 25 °C with those obtained at 55 °C.

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(2)

(iii) Suggest why the increase in temperature has this effect on the length of the
secondary structure of the polypeptide.

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(2)
(Total 8 marks)

4. The diagram below shows the structure of a human insulin molecule. Each circle
represents one amino acid.
S S
A ch ain
G ly Ile Val G lu G lu C y s C y s T h r S e r Ile C y s S e r L eu Ty r G lu L eu G lu A sn Ty r C y s A s n
S S
S S
P h e Val A sn G lu H is L eu C y s G ly S e r H is L e u Val G lu A la L e u Tyr L eu Val C ys G ly G lu A rg G ly P h e P he Ty r T h r P ro Ly s T h r

B c h a in

Insulin is a protein that has a tertiary structure and a quaternary structure.

(a) (i) Name two types of bond that help to maintain the tertiary structure.

1. .....Ionic bonds

2. ......Hydrogen bonds
(2)

(ii) What evidence is there in the diagram that insulin has a quaternary structure?

.......Linked by disulfide bonds which are shown by (S-


S) .......................................................................................................................
.

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(1)

(b) (i) When insulin molecules are formed they fold into a specific shape. Explain why all
human insulin molecules fold into the same shape.

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(2)
(Total 5 marks)

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