Biochemistry - Allosteric Effects - Discussion

Discussion Forum : Allosteric Effects - Section 1 (Q.No. 3)
3.
Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because
it is displaced from the heme by oxygen
it is displaced from the heme by movement of the proximal histidine
its binding pocket becomes too small to accommodate BPG
BPG binds to the R state with the same affinity as the T state
Answer: Option
Explanation:
No answer description is available. Let's discuss.
Discussion:
1 comments Page 1 of 1.

Dagreton said:   1 decade ago
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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