Allosteric Effects
An allosteric activator

both (a) and (c)
increases the binding affinity
decreases the binding affinity
stabilizes the R state of the protein

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

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

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