Biochemistry - Allosteric Effects - Discussion

Discussion Forum : Allosteric Effects - Section 1 (Q.No. 2)
2.
An allosteric activator
increases the binding affinity
decreases the binding affinity
stabilizes the R state of the protein
both (a) and (c)
Answer: Option
Explanation:
No answer description is available. Let's discuss.
Discussion:
3 comments Page 1 of 1.

Dagreton said:   1 decade ago
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.

Salmajallab@gmail.com said:   1 decade ago
I need more explain what's are state of protein?
(1)

Juwairia said:   1 decade ago
What is T & T state?

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