SolutionSet3-3

SolutionSet3-3 - Bioc100B Winter 2011 Rubin Solution Set #3...

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Bioc100B Winter 2011 Rubin Solution Set #3 1) Explain why in the symmetry model of allosterism, an inhibitor must have a positive homotropic effect on itself. Is this same behavior necessarily true of an allosteric inhibitor in the sequential model? The symmetry requires that all subunits be in either the tense (T) or relaxed states (R). Ligand affinity is higher in the relaxed state and ligand binding shifts the interconversion equilibrium between T and R to favor R in the case of positive cooperativitiy. An inhibitor has a negative cooperative effect on ligand by preferentially binding T and shifting the interconversion equilibrium towards T. Because of the symmetry rule, however, this means that it would be easier for a subsequent inhibitor to bind to the protein because the tense state is now favored. Thus, the inhibitor has a positive homotropic cooperative effect on itself. 2) Here is a proposal for an experiment to measure the dissociation rate of maltose from maltose-binding protein:
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SolutionSet3-3 - Bioc100B Winter 2011 Rubin Solution Set #3...

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