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

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

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

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Allosteric Effects
O2 binding to hemoglobin results in

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

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