Effects of pH on proteins: predictions for ensemble and single-molecule pulling experiments.

ABSTRACT: Protein conformations change among distinct thermodynamic states as solution conditions (temperature, denaturants, pH) are altered or when they are subjected to mechanical forces. A quantitative description of the changes in the relative stabilities of the various thermodynamic states is needed to interpret and predict experimental outcomes. We provide a framework based on the Molecular Transfer Model (MTM) to account for pH effects on the properties of globular proteins. The MTM utilizes the partition function of a protein calculated from molecular simulations at one set of solution conditions to predict protein properties at another set of solution conditions. To take pH effects into account, we utilized experimentally measured pK(a) values in the native and unfolded states to calculate

SUBMITTER: O'Brien EP 

PROVIDER: S-EPMC3262061 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature