Biochemistry - Allosteric Effects - Discussion

Discussion :: Allosteric Effects - Section 1 (Q.No.3)


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

Answer: Option C


No answer description available for this question.

Dagreton said: (Jul 10, 2015)  
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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