FFLD 8

Question 1

BPG binds to which part of haemoglobin?
A. The haem group
B. The central pocket/space between the sub units
C. The C-terminals of the beta-globins
D. A hydrophobic pocket in the globin

Answer 1

B

Question 2

BPG has its effect on haemoglobin by:
A. Replacing oxygen on the haem iron
B. Increasing the affinity of globin subunits for oxygen
C. Stabilising the R-state conformation of the globin subunits
D. Stabilising the T-state conformation of the globin subunits

Answer 2

D

Question 3

Decreasing the pH of the environment has its effect on haemoglobin by:
A. Unfolding/denaturing the globins
B. Increasing the affinity of globin subunits for oxygen
C. Promoting the R-state conformation of the globin subunits
D. Promoting the T-state conformation of the globin subunits

Answer 3

D

Question 4

Which ONE of the following is NOT part of the reason HbF has a different oxygen affinity to Hb?
A. HbF doesn’t bind BPG as tightly as HbA
B. HbF has a different subunit composition to HbA.
C. BPG binds less well to the T-state HbF because the foetal environment has a lower pH/more H+.
D.
The central pocket in HbF is less positively charged than in HbA.

Answer 4

C

Question 5

Mutations that cause the formation of met-haemoglobin (HbM):
A. Cause Hb to unfold
B. Make the Hb more likely to be in the R-state
C. Stabilise the Fe2+ state of the harm iron
D. Stabilise the Fe3+ state of the haem iron

Answer 5

D