Proteins

GLOSSARY TERMS

Molecules Fibrous protein Disulphide bridge Phospholipids

Antibody Protein Hydrophobic Polypeptide

Protein channel Ribosome Receptor Nucleotides

Structural protein Hydrogen bond Peptide bond Protein channel

Alpha helix Hydrophilic Antigen Beta sheet

Primary structure Hormone Random coil Glycoprotein

Monomer Epitope Globular protein Enzyme

Amino acid Proteome Secondary structure Tertiary structure

Quaternary structure Chaperonin Denaturation Amine group

Condensation
Carboxyl group Variable R group Conjugated protein
polymersiation
 Proteins: Structure and Function
Use your textbook “Chapter 2.5 – Proteins” (starting at p115) to answer the following
questions.

1. In the table, classify the proteins into one of the types listed below.

Structural, enzyme, contractile, immunoglobulin, hormone, receptor, transport

Protein Type Function

ATP synthase
Haemoglobin
Antibodies
Insulin, Glucagon
Actin, Myosin
Collagen, keratin
Insulin receptors

2. All proteins are made up from chains of 20 possible Amino Acids.

Draw the general chemical

structure of an amino acid in
the box to the right and
highlight the amino and
carboxyl group.

3. Draw the condensation reaction below. Label the peptide bond produced.

4. Draw a simple sketch of each of the following:

Alpha helix Beta sheet Random coils

5. Summarise the features of each structure:

i. Primary Structure:
 ii. Secondary Structure:

iii. Tertiary Structure:

iv. Quaternary Structure:

Quick definitions:

Conjugate:

Nucleoprotein:

Inactive Protein:

Proteome:

Proteomics:
 1. Add the name of the appropriate biomolecule in each circle to illustrate the
relationship of amino acids, polypeptides and proteins.

Chain of monomers: Polymer:

Monomer:

polymerisation join with other chains

2. List two main functions of proteins that are essential for life?

3. Complete the table to show the monomer, the polymer, the elements present and examples of
proteins.

Monomer Polymer Elements present Examples

4. Describe the four levels of protein structure. Use your own graphics to illustrate these
structures.

Primary Structure Secondary Structure

Tertiary Structure Quaternary Structure

Test for proteins

Biuret reagent is used to test for proteins or peptides. The reagent causes a colour change in a two-step
process, where a sodium hydroxide solution is added followed by copper sulphate solution. A colour
change to violet indicates proteins and pink indicates peptides.

1. Mark three clean test tubes at the 2cm and 3cm levels and fill as follows. Record any colour
change.

Sodium Copper
Test Starch
Water Albumin Hydroxide Sulphate Total
tube solution
2M 1%
1 2cm 1cm 2-4 drops 3cm
2 2cm 1cm 2-4 drops 3cm
3 2cm 1cm 2-4 drops 3cm

Q12. Which test will produce a result?

Results for test for proteins

Test tube Colour change observations

1. Water
2. Albumin
3. Starch

Questions
Q13. Which of the above test tubes would be considered a control sample?

Q14. What is the purpose of the control in the tests above?

Q15. Why do experimental procedures include a control sample?

Q16. What would it mean for the test above if the control sample was positive?

Test for protein function

 Pepsin is a specific enzyme made of protein that breaks down proteins to peptides in the presence
of water as shown.

pepsin
Protein + water peptides

1. Mark two test tubes with 2cm, 4cm, 6cm and 8cm.
2. Fill as shown in the table. Shake and leave overnight.

Test tube Water Albumin Pepsin 0.2% HCl Total

1 2cm 2cm 2cm 6cm
2 2cm 2cm 2cm 6cm

3. Fill each to the 8cm mark with the biuret reagent. Observe any colour change and record your
results.

Results table testing protein function

Tube Colour change Explanation

1. Water
Pepsin
HCl
2. Albumin
Pepsin
HCl

Q17. What was the protein being tested?

Q18. Where is this protein found?

Q19. Draw a picture of pepsin acting upon the protein.

Q20. Why did pepsin not act upon water?

EXAM QUESTIONS
Question I: Scientists are now turning to the study of the proteome (all of the proteins) of an
organism rather than the study of single proteins.
a. Briefly outline one reason why the emphasis is now on the study of all the proteins of an
organism rather than on one protein at a time.

Protein molecules come in many shapes and forms that can be classified into primary,
secondary, tertiary and quaternary. The secondary, tertiary and quaternary shapes arise as a
result of different kinds of folding of a primary structure.
One kind of secondary structure is a pleated sheet where the primary molecule extends along
the folded sheet. The primary structures in the layers are held together by hydrogen bonding.

b. Explain why such a structure may be important in the function of a particular protein.

Proteins can also be classified on the basis of their general function. Three of these are shown
below.

c. Complete the table by giving an example of a protein for each of the functions listed.

Function of Protein Example

Structural
Transport
regulatory
Examiners report on the above questions

Question 1a

The emphasis is on the study of all proteins because of the interaction between proteins, and
the reliance that some have on others. Although this question was well answered by many
students, others failed to identify either of the points above.
Structures may be important because:
• of the ability of the protein to stretch or contract (elongate or shorten) in particular
situations
• pleating may strengthen the molecule and that may be important for its function
• particular structures may provide an active or binding site for an enzyme or other molecule.
Few students appeared to understand that secondary-structure proteins may have a particular
function in that state, with many writing only about them being part of a tertiary-structure
protein. Answers that gave general comments, such as ‘the protein could be an enzyme’,
without explaining the relevance of structure received no credit.

This question was generally well answered. Incorrect answers generally referred to
compounds such as carbohydrates and other non-protein compounds.

2007
Question 4
A protein-based polymer could be constructed from repeated monomers of:
A. C5H13N4COOH
B. CH3(CH2)nCOOH
C. Cx(H2O)y
D. C6H5COCl
77 11 7 4

Question 11
A haemoglobin molecule is composed of four protein (globin) chains each attached to an
iron-containing haem group. Two are identical alpha chains and two are identical beta chains.
The following diagram is a stylized representation of a haemoglobin molecule.
A haemoglobin molecule would be classified as having a
A. primary protein structure.
B. secondary protein structure.
C. tertiary protein structure.
D. quaternary protein structure.

5 15 12 68

Question 12
Insulin is a complex protein that is said to have a quaternary structure.
This means that insulin
A. cannot be denatured.
B. lacks disulphide bridges.
C. contains all the known amino acids.
D. has more than one polypeptide chain.

2 1 3 93

Question 17
Canavanine is an amino acid that is part of the defence system of some plants. Some insects
that eat seeds containing canavanine incorporate it into their own proteins in the place of the
amino acid arginine. This causes the insect to produce proteins with a modifed tertiary and/or
quaternary structure. The proteins containing canavanine can affect the nervous system of the
insect.
This information suggests that canavanine
A. is a plant hormone that affects insects.
B. is a pheromone that attracts insects.
C. makes seeds containing it distasteful to insects.
D. in insect proteins reduces the ability of an insect to feed.
Question 2 (2008)
Proteins may be classified as fibrous or globular depending on their 3-dimensional shape.
In fibrous proteins, the polypeptide chains are arranged in parallel to form long fibres or
sheets. In globular proteins, the polypeptide chains are folded into compact spherical or
globular shapes.
a) Name the subunit of a polypeptide. (1 mark)

Keratin, found in fingernails and claws, is an example of a fibrous protein.

b) Name another example of a fibrous protein and briefly outline its function. (1
mark)

c) Describe a distinctive property of a fibrous protein and explain how this property
is due to the arrangement of its polypeptides. (1 mark)
Question 1 (2009)
The diagram below shows the structure of a particular protein molecule.

The protein contains two distinctive types of polypeptide chains labelled X and Y. What are
the names of these two types?

Chain X:

Chain Y:
(2 marks)
2011
Question 1
The term used to indicate all proteins in an organism is:
A. protozoa
B. protease
C. proteome
D. Proterozoic

Question 1
The following figure represents a globular protein.

The molecule is likely to be highly soluble in water.

a. Outline why such a conclusion can be made about this molecule.
 (2 marks)

Question 8
Protein forms part of the structure of
A. polysaccharides.
B. transfer RNA.
C. phospholipids.
D. haemoglobin.

Question 3
Human insulin is a macromolecule composed of two amino acid chains. The chains are
connected by disulfide bonds.
a. To what group of macromolecules does insulin belong?

I mark
Insulin found in other animals varies from human insulin.
The following table compares all the differences seen in the primary structure of human, cow,
pig and sheep insulin.

b. What is meant by the term ‘primary structure’ of the insulin macromolecule? 1 mark
Humans with diabetes take insulin injections to maintain their health.
c. If supplies of human insulin were not available, which one of the other three animals listed in the
table would be the best source of insulin? Explain your reason for choosing this particular animal.

Animal

Explanation

2 marks

The table below contains the genetic code for protein production.

d. Use the information in the table to explain

i. the different sequence of nucleotides in humans and cows with respect to the DNA coding for the
amino acid at position 30.

ii. whether the sequence of nucleotides in DNA coding for the amino acid at position 30 will be
identical in cows, pigs and sheep.
1 + 1 mark = 2 marks