Ontology highlight
ABSTRACT:
SUBMITTER: Roderer DJ
PROVIDER: S-EPMC4485320 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
Roderer Daniel J A DJ Schärer Martin A MA Rubini Marina M Glockshuber Rudi R
Scientific reports 20150630
Cis prolyl peptide bonds are conserved structural elements in numerous protein families, although their formation is energetically unfavorable, intrinsically slow and often rate-limiting for folding. Here we investigate the reasons underlying the conservation of the cis proline that is diagnostic for the fold of thioredoxin-like thiol-disulfide oxidoreductases. We show that replacement of the conserved cis proline in thioredoxin by alanine can accelerate spontaneous folding to the native, thermo ...[more]