I'm trying to figure out the relation between conformational entropy and protein folding.
I read the following in Lehninger principles of biochemistry, Principles of Biochemistry (6th edition):
Most of the net change in free energy as weak interactions form within a protein is therefore derived from the increased entropy in the surrounding aqueous solution resulting from the burial of hydrophobic surfaces. This more than counterbalances the large loss of conformational entropy as a polypeptide is constrained into its folded conformation.
In this context the meaning of conformational entropy is that the higher the stability of the proteïn is the lower the conformational entropy is (I think).
*Why does the surrounding entropy increases because of the burial of hydrophobic residus?*
*Why does the burial of those hydrophobic residus couterbalances the large loss of conformational entropy?*
I think maybe because the unfolded protein has more conformation then the protein when it's folded because of the hydorphobic core, it lowers the possible conformation because the hydrophobic interaction restrict the possiblity's. Am I right?
Why does the surrounding entropy increases because of the burial of hydrophobic residues?
Why does the burial of those hydrophobic residus couterbalances the large loss of conformational entropy?
I hope some of you can help answering the questions which came up to me.I think maybe because the unfolded protein has more conformation then the protein when it's folded because of the hydorphobic core, it lowers the possible conformation because the hydrophobic interaction restrict the possiblities. Am I right?
