Ontology highlight
ABSTRACT:
SUBMITTER: Salari R
PROVIDER: S-EPMC4047600 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
The journal of physical chemistry letters 20100913 19
The prevalence of salt bridges across protein binding interfaces is surprising given the significant costs of desolvating the two charged groups upon binding. These desolvation costs, which are difficult to examine using laboratory experiments, have been computed in previous studies using the Poisson-Boltzmann (PB) implicit solvent model. Here, for the first time, we directly compare the PB implicit solvent model with several explicit water models in computing the desolvation penalties of salt b ...[more]