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

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

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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
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

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