Molecular determinant of the effects of hydrostatic pressure on protein folding stability.

ABSTRACT: Hydrostatic pressure is an important environmental variable that plays an essential role in biological adaptation for many extremophilic organisms (for example, piezophiles). Increase in hydrostatic pressure, much like increase in temperature, perturbs the thermodynamic equilibrium between native and unfolded states of proteins. Experimentally, it has been observed that increase in hydrostatic pressure can both increase and decrease protein stability. These observations suggest that volume changes upon protein unfolding can be both positive and negative. The molecular details of this difference in sign of volume changes have been puzzling the field for the past 50 years. Here we present a comprehensive thermodynamic model that provides in-depth analysis of the contribution of various molec

SUBMITTER: Chen CR 

PROVIDER: S-EPMC5309723 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature