Allosteric Effects
In hemoglobin, allosteric effects occur

to minimize oxygen delivery to the tissues
to maximize oxygen delivery to the tissues
for maintaining Fe in the Fe2+ state
only in humans

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

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

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