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

Norman Metanis; Carlotta Foletti; Joris Beld; Donald Hilvert

doi:https://doi.org/10.1002/ijch.201100105

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

Norman Metanis, Carlotta Foletti, Joris Beld, Donald Hilvert

Research output: Contribution to journal › Article › peer-review

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

All Science Journal Classification (ASJC) codes

General Chemistry

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https://doi.org/10.1002/ijch.201100105

Cite this

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title = "Selenoglutathione-mediated rescue of kinetically trapped intermediates in oxidative protein folding",

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.",

keywords = "bovine pancreatic trypsin inhibitor, protein folding, redox chemistry, selenoglutathione, thiol/disulfide exchange",

author = "Norman Metanis and Carlotta Foletti and Joris Beld and Donald Hilvert",

year = "2011",

month = nov,

doi = "https://doi.org/10.1002/ijch.201100105",

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journal = "Israel Journal of Chemistry",

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AU - Metanis, Norman

AU - Foletti, Carlotta

AU - Beld, Joris

AU - Hilvert, Donald

PY - 2011/11

Y1 - 2011/11

N2 - 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.

AB - 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.

KW - bovine pancreatic trypsin inhibitor

KW - protein folding

KW - redox chemistry

KW - selenoglutathione

KW - thiol/disulfide exchange

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DO - https://doi.org/10.1002/ijch.201100105

M3 - مقالة

SN - 0021-2148

VL - 51

SP - 953

EP - 959

JO - Israel Journal of Chemistry

JF - Israel Journal of Chemistry

IS - 8-9

ER -

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

Abstract

Keywords

All Science Journal Classification (ASJC) codes

Access to Document

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