Modeling of denatured state for calculation of the electrostatic contribution to protein stability.

ABSTRACT: Existing models of the denatured state of proteins consider only one possible spatial distribution of protein charges and therefore are applicable to a limited number of cases. In this article, a more general framework for the modeling of the denatured state is proposed. It is based on the assumption that the titratable groups of an unfolded protein can adopt a quasi-random distribution restricted by the protein sequence. The model was applied for the calculations of electrostatic interactions in two proteins, barnase and N-terminal domain of the ribosomal protein L9. The calculated free energy of denaturation, DeltaG(pH), reproduces the experimental data better than the commonly used null approximation (NA). It was shown that the seemingly good agreement with experimental data obtained by

SUBMITTER: Kundrotas PJ 

PROVIDER: S-EPMC2373658 | biostudies-literature | 2002 Jul

REPOSITORIES: biostudies-literature