Characterization of the cofactor-induced folding mechanism of a zinc-binding peptide using computationally designed mutants.

ABSTRACT: Metals are the most commonly encountered protein cofactors, and they play important structural and functional roles in biology. In many cases, metal binding provides a major driving force for a polypeptide chain to fold. While there are many studies on the structure, stability, and function of metal-binding proteins, there are few studies focusing on understanding the kinetic mechanism of metal-induced folding. Herein, the Zn(2+)-induced folding kinetics of a small zinc-binding protein are studied; the CH1(1) peptide is derived from the first cysteine/histidine-rich region (CH1 domain) of the protein interaction domains of the transcriptional coregulator CREB-binding protein. Computational design is used to introduce tryptophan and histidine mutations that are structurally consistent with

SUBMITTER: Tang J 

PROVIDER: S-EPMC2792901 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature