Allosteric Effects
An allosteric activator

decreases the binding affinity
both (a) and (c)
increases the binding affinity
stabilizes the R state of the protein

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Allosteric Effects
Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because

it is displaced from the heme by oxygen
its binding pocket becomes too small to accommodate BPG
BPG binds to the R state with the same affinity as the T state
it is displaced from the heme by movement of the proximal histidine

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