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

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

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Allosteric Effects
The conformational changes from the T to the R state is initiated by

movement of the F-helix, which contains the proximal His
binding of oxygen to the heme
reorganization of protein-protein contacts between the individual subunits
movement of the proximal histidine towards the heme

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

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