Polar or apolar--the role of polarity for urea-induced protein denaturation.

ABSTRACT: Urea-induced protein denaturation is widely used to study protein folding and stability; however, the molecular mechanism and driving forces of this process are not yet fully understood. In particular, it is unclear whether either hydrophobic or polar interactions between urea molecules and residues at the protein surface drive denaturation. To address this question, here, many molecular dynamics simulations totalling ca. 7 micros of the CI2 protein in aqueous solution served to perform a computational thought experiment, in which we varied the polarity of urea. For apolar driving forces, hypopolar urea should show increased denaturation power; for polar driving forces, hyperpolar urea should be the stronger denaturant. Indeed, protein unfolding was observed in all simulations with decreas

SUBMITTER: Stumpe MC 

PROVIDER: S-EPMC2570617 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature