Electrostatic effects in unfolded staphylococcal nuclease.

ABSTRACT: Structure-based calculations of pKa values and electrostatic free energies of proteins assume that electrostatic effects in the unfolded state are negligible. In light of experimental evidence showing that this assumption is invalid for many proteins, and with increasing awareness that the unfolded state is more structured and compact than previously thought, a detailed examination of electrostatic effects in unfolded proteins is warranted. Here we address this issue with structure-based calculations of electrostatic interactions in unfolded staphylococcal nuclease. The approach involves the generation of ensembles of structures representing the unfolded state, and calculation of Coulomb energies to Boltzmann weight the unfolded state ensembles. Four different structural models of the unfo

SUBMITTER: Fitzkee NC 

PROVIDER: S-EPMC2222714 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature