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

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

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Allosteric Effects
O2 binding to hemoglobin results in

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

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

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