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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Vydáno v:Israel journal of chemistry Ročník 51; číslo 8-9; s. 953 - 959
Hlavní autoři: Metanis, Norman, Foletti, Carlotta, Beld , Joris, Hilvert, Donald
Médium: Journal Article
Jazyk:angličtina
Vydáno: Weinheim WILEY-VCH Verlag 01.11.2011
WILEY‐VCH Verlag
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Témata:
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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Shrnutí: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.
Bibliografie:Israel Science Foundation
istex:3CC89C10F709CBB929C345BA7A056E75007A4B58
ArticleID:IJCH201100105
ark:/67375/WNG-WP6DFR9Z-Z
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0021-2148
1869-5868
DOI:10.1002/ijch.201100105