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

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

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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
movement of the proximal histidine towards the heme
binding of oxygen to the heme
reorganization of protein-protein contacts between the individual subunits

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