Ontology highlight
ABSTRACT:
SUBMITTER: Irvine AG
PROVIDER: S-EPMC3896340 | biostudies-literature | 2014
REPOSITORIES: biostudies-literature
Irvine Alistair G AG Wallis A Katrine AK Sanghera Narinder N Rowe Michelle L ML Ruddock Lloyd W LW Howard Mark J MJ Williamson Richard A RA Blindauer Claudia A CA Freedman Robert B RB
PloS one 20140120 1
In contrast to molecular chaperones that couple protein folding to ATP hydrolysis, protein disulfide-isomerase (PDI) catalyzes protein folding coupled to formation of disulfide bonds (oxidative folding). However, we do not know how PDI distinguishes folded, partly-folded and unfolded protein substrates. As a model intermediate in an oxidative folding pathway, we prepared a two-disulfide mutant of basic pancreatic trypsin inhibitor (BPTI) and showed by NMR that it is partly-folded and highly dyna ...[more]