Allosteric Effects
The specificity of a ligand binding site on a protein is based on

the absence of competing ligands
the amino acid residues lining the binding site
the presence of hydrating water molecules
the opposite chirality of the binding ligand

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

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

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