Selenoglutathione-Mediated Rescue of Kinetically Trapped Intermediates in Oxidative Protein Folding

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...

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Veröffentlicht in:Israel journal of chemistry Jg. 51; H. 8-9; S. 953 - 959
Hauptverfasser: Metanis, Norman, Foletti, Carlotta, Beld , Joris, Hilvert, Donald
Format: Journal Article
Sprache:Englisch
Veröffentlicht: Weinheim WILEY-VCH Verlag 01.11.2011
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Schlagworte:
bovine pancreatic trypsin inhibitor
Catalysts
Conversion
Folding
Pathways
Protein folding
Proteins
redox chemistry
selenoglutathione
thiol/disulfide exchange
Trypsin inhibitors
ISSN:0021-2148, 1869-5868
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Zusammenfassung: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.
Bibliographie:Israel Science Foundation
istex:3CC89C10F709CBB929C345BA7A056E75007A4B58
ArticleID:IJCH201100105
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ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0021-2148
1869-5868
DOI:10.1002/ijch.201100105