Accurate prediction of DnaK-peptide binding via homology modelling and experimental data.

ABSTRACT: Molecular chaperones are essential elements of the protein quality control machinery that governs translocation and folding of nascent polypeptides, refolding and degradation of misfolded proteins, and activation of a wide range of client proteins. The prokaryotic heat-shock protein DnaK is the E. coli representative of the ubiquitous Hsp70 family, which specializes in the binding of exposed hydrophobic regions in unfolded polypeptides. Accurate prediction of DnaK binding sites in E. coli proteins is an essential prerequisite to understand the precise function of this chaperone and the properties of its substrate proteins. In order to map DnaK binding sites in protein sequences, we have developed an algorithm that combines sequence information from peptide binding experiments and structura

SUBMITTER: Van Durme J 

PROVIDER: S-EPMC2717214 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature