Amino acid residues important for folding of thioredoxin are revealed only by study of the physiologically relevant reduced form of the protein.

ABSTRACT: Thioredoxin-1 from Escherichia coli has frequently been used as a model substrate in protein folding studies. However, for reasons of convenience, these studies have focused largely on oxidized thioredoxin and not on reduced thioredoxin, the more physiologically relevant species. Here we describe the first extensive characterization of the refolding kinetics and conformational thermodynamics of reduced thioredoxin. We have previously described a genetic screen that yielded mutant thioredoxin proteins that fold more slowly in both the oxidized and reduced forms. In this study, we apply our more detailed analysis of reduced thioredoxin folding to a larger number of folding mutants that includes those obtained from continuation of the genetic screen. We have identified mutant proteins that di

SUBMITTER: Huber D 

PROVIDER: S-EPMC2953564 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature