Question

A mutant form of hemoglobin uses disulphide bridges to stabilize the T-state instead of salt bridges. How would the behaviour of this mutant Hb differ from the regular version?

a) The mutant would bind oxygen easier than the regular version
b) The mutant would spend less time in the R-state than the regular version
c) The mutant would resist CO poisoning less than the regular version
d) The mutant would resist CO poisoning more than the regular version

Answer 1

A mutant form of hemoglobin that uses disulphide bridges to stabilize the T-state would spend less time in the R-state compared to the regular version.

Step-by-step explanation:

A mutant form of hemoglobin that uses disulphide bridges to stabilize the T-state instead of salt bridges would have different behavior compared to the regular version of hemoglobin. Specifically, the mutant form would spend less time in the R-state than the regular version.

Hemoglobin normally undergoes a conformational change when oxygen binds, transitioning from the T-state to the R-state. The R-state is the oxygen-bound state where hemoglobin has a higher affinity for oxygen. By stabilizing the T-state, the mutant form would have a reduced ability to transition to the R-state, resulting in spending less time in the oxygen-bound state.

Therefore, the correct answer is b) The mutant would spend less time in the R-state than the regular version.