Allosteric Effects
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

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Allosteric Effects
O2 binding to hemoglobin results in

100-fold higher affinity for the last O2 bound than for the first
extensive protein conformational change
both (a) and (b)
100-fold lower affinity for the last O2 bound than for the first

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