unit 1 proteins and enzymes

Question 1

Protein - Protein Structure (7)

Answer 1

1. Polymer of amino acids;
2. Joined by peptide bonds;
3. Formed by condensation;
4. Primary structure is order of amino acids;
5. Secondary structure is folding of polypeptide chain due to hydrogen bonding; (into alpha helix or beta pleated sheet)
6. Tertiary structure is 3-D folding due to hydrogen bonding and ionic/disulphide bonds between R groups;
7. Quaternary structure is more than one polypeptide chains;

Question 2

Test for a protein (2)

Answer 2

1. Add Biuret reagent to the sample
2. colour change to lilac

Question 3

Enzymes – “Induced Fit” Model (3)

Answer 3

1. (before reaction) active site not complementary to/does not fit substrate;
2. Shape of active site changes as substrate binds/as enzyme-substrate complex forms;
3. Stressing/distorting/bending bonds (in substrate leading to reaction);

Question 4

Enzymes – Increased temperature

and reaction rate (4)

Answer 4

1. particles have more kinetic energy
2. therefore they move more
3. so there are more collisions between substrates and active sites
4. so more ES complexes form

Question 5

Enzymes – Denaturation (5)

Answer 5

1. Heat above the optimum breaks hydrogen bonds
2. this causes the tertiary structure to unfold
3. so the active site changes shape
4. substrate can no longer bind to the active site, as it’s no longer complementary
5. so fewer ES complexes form

Question 6

Enzymes – Effect of Changes in pH

(4)

Answer 6

1. Ionic bonds holding tertiary structure break
2. active site distorts and substrate no longer binds to active site
3. charges on amino acids in active site affected
4. fewer ES complexes form

Question 7

Enzymes – Concentration of

Substrate (2)

Answer 7

1. (Rate of) increase in concentration of product slows as substrate is used up OR High initial rate as plenty of substrate/more E-S complexes;
2. No increase after 25 minutes/at end/levels off because no substrate left; Reject ref. to enzyme being used up

Question 8

Enzymes – Describe and explain

the temperature graph of enzyme

rate (5)

Answer 8

1. Initial rate of reaction faster at 37 °C (than 25 °C);
2. Because more kinetic energy
3. So more E–S collisions/more E–S complexes formed;
4. Graph reaches plateau /levels of at 37 °C;
5. Because all substrate used up;

Question 9

Enzymes – Comparison of

Competitive and Non Competitive

Inhibition (4)

Answer 9

1. Competitive inhibitor binds to active sites of enzyme but non-competitive inhibitor binds at allosteric site/away from active site;
2. (Binding of) competitive inhibitor does not cause change in shape of active site but (binding of) non-competitive does (cause change in size of active site);
3. So with competitive inhibitor, at high substrate concentrations (active) enzyme still available but with noncompetitive inhibitor (active) enzymes no longer available;
4. At higher substrate concentrations likelihood of enzyme-substrate collisions increases with competitive inhibitor but this is not possible with non-competitive inhibitor;