Protein folding often has a negative change in entropy ( delta S = - X kJ/mol).

Question

Protein folding often has a negative change in entropy ( delta S = - X kJ/mol). However, the magnitude of this change is usually not large. Given that a folded protein seems to exhibit a high degree of order, why is delta S not of large negative magnitude? Protein folding often has a negative change in entropy ( delta S = - X kJ/mol). However, the magnitude of this change is usually not large. Given that a folded protein seems to exhibit a high degree of order, why is delta S not of large negative magnitude? Protein folding often has a negative change in entropy ( delta S = - X kJ/mol). However, the magnitude of this change is usually not large. Given that a folded protein seems to exhibit a high degree of order, why is delta S not of large negative magnitude?

Explanation / Answer

according to thermodynamics, a process occurs sspontaneously if its chanbe in Gibbs energy is negative. now when the protein foLDS itself, it gets ordered, and hence its entropy decreases. However forming od disulfide bonds and other weak interactions during the folding of protein counterbalance the rising negative entropy. hence the delta S is nit of large magnitude.

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