Dynameomics: a consensus view of the protein unfolding/folding transition state ensemble across a diverse set of protein folds.

ABSTRACT: The Dynameomics project aims to simulate a representative sample of all globular protein metafolds under both native and unfolding conditions. We have identified protein unfolding transition state (TS) ensembles from multiple molecular dynamics simulations of high-temperature unfolding in 183 structurally distinct proteins. These data can be used to study individual proteins and individual protein metafolds and to mine for TS structural features common across all proteins. Separating the TS structures into four different fold classes (all proteins, all-alpha, all-beta, and mixed alpha/beta and alpha +beta) resulted in no significant difference in the overall protein properties. The residues with the most contacts in the native state lost the most contacts in the TS ensemble. On average, re

SUBMITTER: Jonsson AL 

PROVIDER: S-EPMC2784564 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature