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Multiple Choice
In the Concerted model for allosteric enzymes:
A
Relative affinities of substrate for the T & R states play a crucial role in reaction cooperativity.
B
Equilibrium between T and R states plays a minor role.
C
Enzymatic activity of the T state is considerably higher than that of the R state.
D
It is possible to describe the reactions of all allosteric enzymes accurately.
Verified step by step guidance
1
Understand the Concerted model (also known as the Monod-Wyman-Changeux model) for allosteric enzymes, which proposes that enzyme subunits are connected in such a way that a conformational change in one subunit is conferred to all others.
Recognize that in the Concerted model, enzymes exist in two states: the T (tense) state and the R (relaxed) state. The T state is less active, while the R state is more active.
Identify that the substrate has different affinities for the T and R states. Typically, the substrate binds more readily to the R state, which is the active form of the enzyme.
Acknowledge that the equilibrium between the T and R states is influenced by the binding of substrates or effectors, but the relative affinities of the substrate for these states are crucial for cooperativity.
Note that the statement 'Enzymatic activity of the T state is considerably higher than that of the R state' is incorrect in the context of the Concerted model, as the R state is the more active form.