An effective solvent theory connecting the underlying mechanisms of osmolytes and denaturants for protein stability.

ABSTRACT: An all-atom Gō model of Trp-cage protein is simulated using discontinuous molecular dynamics in an explicit minimal solvent, using a single, contact-based interaction energy between protein and solvent particles. An effective denaturant or osmolyte solution can be constructed by making the interaction energy attractive or repulsive. A statistical mechanical equivalence is demonstrated between this effective solvent model and models in which proteins are immersed in solutions consisting of water and osmolytes or denaturants. Analysis of these studies yields the following conclusions: 1), Osmolytes impart extra stability to the protein by reducing the entropy of the unfolded state. 2), Unfolded states in the presence of osmolyte are more collapsed than in water. 3), The folding transition in

SUBMITTER: Linhananta A 

PROVIDER: S-EPMC3021680 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature