GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.

ABSTRACT: GroEL is an essential Escherichia coli molecular chaperon that uses ATP to facilitate correct folding of a range of proteins in a cell. Central to the GroEL substrate diversity is how GroEL recognizes the substrates. The interaction between GroEL and substrate has been proposed to be largely hydrophobic because GroEL interacts with proteins in non-native conformations but not in native forms. Analysis of GroEL substrate proteins reveals that one of its main substrates are proteins with alphabeta folding domains, suggesting that GroEL may stabilize the collapsed alphabeta core by binding to hydrophobic surfaces that are usually buried between the alpha and beta elements. In this study, we characterize the interaction between GroEL and a peptide derived from our previous selection via a phag

SUBMITTER: Li Y 

PROVIDER: S-EPMC2640968 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature