Selenoglutathione-mediated rescue of kinetically trapped intermediates in oxidative protein folding

Norman Metanis, Carlotta Foletti, Joris Beld, Donald Hilvert*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


Selenoglutathione has been shown to have considerable potential as a catalyst of oxidative protein folding. Here we examine how this reagent modulates the folding pathway of bovine pancreatic trypsin inhibitor (BPTI) and show that the diselenide increases the efficiency of this process primarily by accelerating the conversion of a kinetically trapped folding intermediate.

Original languageAmerican English
Pages (from-to)953-959
Number of pages7
JournalIsrael Journal of Chemistry
Issue number8-9
StatePublished - Nov 2011
Externally publishedYes


  • bovine pancreatic trypsin inhibitor
  • protein folding
  • redox chemistry
  • selenoglutathione
  • thiol/disulfide exchange


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