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

Norman Metanis; Carlotta Foletti; Joris Beld; Donald Hilvert

doi:10.1002/ijch.201100105

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 journal › Article › peer-review

24 Scopus citations

Abstract

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 language	English
Pages (from-to)	953-959
Number of pages	7
Journal	Israel Journal of Chemistry
Volume	51
Issue number	8-9
DOIs	https://doi.org/10.1002/ijch.201100105
State	Published - Nov 2011
Externally published	Yes

Keywords

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

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10.1002/ijch.201100105

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abstract = "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.",

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KW - redox chemistry

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KW - thiol/disulfide exchange

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

Abstract

Keywords

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