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Allosteric Effects

Q1: An allosteric activator

A increases the binding affinity

B decreases the binding affinity

C stabilizes the R state of the protein

D both (a) and (c)

ANS:D - both (a) and (c)

The T state of the protein is the Tensed state, when no substrate is bound. T state has low energy and is more stable than are state.

The are state of the protein is the Relaxed state, when substrates are bound. R state has higher energy, thus it is more unstable.

Allosteric activators stabilize the are state, by moving the equilibrium towards the R state, thus increasing the affinity of the enzyme for the substrate.



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