Question

The folding of proteins is thermodynamically spontaneous. a. What does this mean? How is it defined? b. This spontaneity appears, on the surface, to be counterintuitive, because of the change in entropy, going from one state to another. Explain briefly. c. How is the apparent contradiction in part (b) overcome to ensure the spontaneity of the process?

Answer 1

The folding of proteins is thermodynamically spontaneous. That means during the folding of protein the Gibbs energy change is negative.

When the protein is folded then it goes from one state to another state. In the unfolded state the entropy of the protein is large and when it is folded the entropy become less that results the negative interrogative which interns increase the Gibbs energy change. That's why the protein folding its process in surface is counter intuitive as it goes through two different state.

This contradiction overcome increasing the the enthalpy of the process that mean when the protein is being for late there should be lots of non covalent interaction like hydrogen bonding vander Walls forces. Which by decreasing the the Gibbs energy change makes the process spontaneous.