Solvent accessible surface area-assessed molecular basis of osmolyte-induced protein stability.

ABSTRACT: In solvent-modulated protein folding, under certain physiological conditions, an equilibrium exists between the unfolded and folded states of the protein without any need to break or make a covalent bond. In this process, interactions between various protein groups (peptides) and solvent molecules are known to play a major role in determining the directionality of the chemical reaction. However, an understanding of the mechanism of action of the co(solvent) by a generic theoretical underpinning is lacking. In this study, a generic solvation model is developed based on statistical mechanics and the thermodynamic transfer free energy model by considering the microenvironment polarity of the interacting co(solvent)-protein system. According to this model, polarity and the fractional solvent-a

SUBMITTER: Raghunathan S 

PROVIDER: S-EPMC11310836 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature