fSECTIONB: SHORT/LONGANSWERQUESTIONS
Please answer ALL of the questions in this section.
QUESTION 3
[35)
3.1. Write a mechanism for the conversion of pyruvate to acetyl CoA. Assume all of the required
coenzymes are present.
[6]
3.2. What is protein denaturation? Is there any change in the primary structure when a protein is
denatured? What are some factors that can lead to protein denaturation?
[4]
3.3. Describe allosteric regulation of enzyme activity?
[4]
3.4. What is the prosthetic group that hemoglobin and myoglobin's oxygen binding ability
depends on?
[1]
3.5. Briefly explain the Cori cycle which is linked metabolic pathways
[5]
3.6. Define cooperativity to binding oxygen
[3]
3.7. What is oxidative phosphorylation?
[2]
3.8. List four (4) non covalent interaction in the biomolecules
[4]
3.9. How are proteins separated by electrophoresis?
[3]
3.10. What are Glycolipids and what are their important functions?
[3]
QUESTION 4: CALCULATIONS
[9]
4.1. What is the [H+] of a solution with a pH of 4.5?
[3]
4.2. What do you understand by pKa
[2]
4.3. Calculate the pH of a buffer that contains 0.7 M ammonia and 0.9 M ammonium chloride.
(pK0 = 9.248).
[4]
QUESTION 5: ENZYMES
[10)
5.1 At what substrate concentration would an enzyme with a kcatof 30.0 s-1 and a Kmof 0.0050 M
operate at one-quarter of its maximum rate?
[4]
5.2 Determine the fraction of Vmaxthat would be obtained at the following substrate
concentrations: [SJ=~km, 2 km,and 10 km
[3]
2
5.3 An enzyme that catalyzes the reaction X .= Y is isolated from two bacterial species. The
enzymes have the same Vmaxbut different Kmvalues for the substrate X. Enzyme A has a Kmof
2.0 µM, and enzyme B has a Km of 0.5 µM. The plot below shows the kinetics of reactions
carried out with the same concentration of each enzyme and with [X] = 1 µM. Which curve
corresponds to which enzyme?
[3]
Biochemistry/ introduction to biochemistry (B1O521S/IBC521S)
4
1stOpportunity November 2024