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Stability of protein folding, calculations of folded and unfolded states of proteins from G

Stability of protein folding, calculations of folded and unfolded states of proteins from G

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Answer #1

Any change in the Gibbs Free Energy (G) usually denotes if any chemical process is advantageous or not. If the value of delta G is less than 0, the process is disadvantageous and if the value of delta G is more than 0, the the process is advantageous and the resultant product is stable.

Hence, with respect to protein folding, higher the value of delta G, greater is the stability of protein.

Protein Molecules tend to undergo transitions between their native state (N) to unfolded state (U). This can be represented by the formula:

wherein,

R is the Gas Constant and T is the value of absolute temperature (in Kelvin).

In this case Keq can be found out by applying the formula:

Keq= Ku/Kf = [U]eq / [N]eq

Hence,   is found to be positive if the unfolded state is less stable and is disfavoredwith respect to its relative native state.

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