Spatially resolved free-energy contributions of native fold and molten-globule-like Crambin.

ABSTRACT: The folding stability of a protein is governed by the free-energy difference between its folded and unfolded states, which results from a delicate balance of much larger but almost compensating enthalpic and entropic contributions. The balance can therefore easily be shifted by an external disturbance, such as a mutation of a single amino acid or a change of temperature, in which case the protein unfolds. Effects such as cold denaturation, in which a protein unfolds because of cooling, provide evidence that proteins are strongly stabilized by the solvent entropy contribution to the free-energy balance. However, the molecular mechanisms behind this solvent-driven stability, their quantitative contribution in relation to other free-energy contributions, and how the involved solvent thermodyn

SUBMITTER: Heinz LP 

PROVIDER: S-EPMC8391029 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature