thebillsfan

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that is, if there's a protein that exhibits quaternary structure (dimer, trimer subunits) then would binding of an allolsteric activator at one always lead to cooperative binding unless otherwise stated? obviously if there's just one protein subunit cooperativity is not an option
 

maverick09

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generally, a multisubunit protein allows for the subunits to influence each other's behavior (i.e hemoglobin and binding oxygen). therefore i would think that an activator would elicit cooperative binding in all the cases we would see on the mcat (unless otherwise stated of course)
 

medscholhopeful

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that is, if there's a protein that exhibits quaternary structure (dimer, trimer subunits) then would binding of an allolsteric activator at one always lead to cooperative binding unless otherwise stated? obviously if there's just one protein subunit cooperativity is not an option
i think of it like this.. cooperative binding is a form of allosteric regulation of the enzyme meaning that a allosteric activator can allosterically bind to an enzymes at an allosteric site(not active site) to affect an enzyme's function.

On the other hand, cooperative binding is the substrate binding to the enzyme's active site, which then increases the affinity of the substrates at other various active sites on the same enzyme. (usually happens with enzymes that have multiple active site)