imagine a mutant of human adult hemoglobin (I don\'t know if this sort of mutati
ID: 877779 • Letter: I
Question
imagine a mutant of human adult hemoglobin (I don't know if this sort of mutation actually exists) in which the T form is destabilized, that is, in which the T < === > R equilibrium is shifted towards R in the absence of oxygen. Which of these would be the effect of such a mutation? (Note: in this mutant, the binding of 2,3-bisphossphoglycerate to the T form is unaffected.)
A. In red blood cells, the oxygen binding curve of hemoglobin would be to the left (to lower oxygen pressure) compared to normal (wild-type) hemoglobin's.
B. In red blood cells, the oxygen binding curve of hemoglobin would be to the right (to higher oxygen pressure) compared to normal (wild-type) hemoglobin's.
C. There would be no effect on hemoglobin's oxygen binding curve in the absence of 2,3 bisphosphoglycerate.
D. This mutation would have no effect, under any condition, on the oxygen binding curve of hemoglobin.
Explanation / Answer
B) in red blood cells, the oxygen binding curve of haemoglobin would be to the right.
This is because mutant haemoglobin has decreased affinity for oxygen.
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