[erv10s]

I am reviewing for a test and wanted to clarify some aspects of the protein folding process.

I understand the entropic factors involved in protein folding...that the primary force driving protein folding is maximizing the entropy of the solvent.

I also understanding that as a peptide chain folds, the entropy of the chain decreases while the entropy of the solvent increases.

However, I seem to have difficulty in understanding the enthalpic factors involved in protein folding. Am I correct in thinking that peptide chain folding leads to a decrease in enthalpy because bonds are being formed in an exothermic process? Also, what is considered enthalpically unfavorable?

[macman104]

Exactly correct, the bonds formed are an exothermic process and thus enthalpicly (did I just make up a word? ) favored.  Enthalpically (maybe that's how we should spell it ) unfavorable processes would include things like bond breaking.  Maybe bonds break to form more molecules of gas, which while enthapically (yea, I like this one) are more entropically (and I'm pretty sure this one's right) favored.