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Allosteric Effects

Q1: Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because

A it is displaced from the heme by oxygen

B it is displaced from the heme by movement of the proximal histidine

C its binding pocket becomes too small to accommodate BPG

D BPG binds to the R state with the same affinity as the T state

ANS:C - its binding pocket becomes too small to accommodate BPG

The hole in the centre of the Hemoglobin consists of 6-positive charged amino residues. 2.3 BPG has a negative charge and can bind on the hemoglobin's hole solely on the T-state, because the hole that exists in the T-state essentially collapses on the R-state.



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