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18 Nov 2019

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consider the unimolecular elementary reversible reaction:

A <--->B

with forward rate constant k1 and backward rate constant k-1.

The reversible folding kinetic equilibrium of a protein assumed to follow the unimolecular reversible

mechanism above (A=Unfolded and B = Folded) . A solution of protein of total concentration C=3.20μM is

investigated. At T=310 K the equilibrium concentration of unfolded proteins is measured to be [U]eq=0.27μM

The temperature of the sample is quickly raised to 330 K and the concentration of unfolded proteins is monitored

as a function of time. After 3.2 ms at the new temperature, the concentration of unfolded proteins increased to

[U]=0.313μM and reached equilibrium at a concentration of [U]eq=0.39μM .

(a) Compute the equilibrium constant for folding at 310 K, and 330 K.

(b) Compute the standard free energy ΔG∘ for folding at 310 K, and 330 K and estimate the entropy of folding.

(c) Compute the relaxation time constant at 330 K.

(d) Compute the folding and unfolding rate constants at 330 K.

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Beverley Smith
Beverley SmithLv2
30 Jan 2019

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