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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ISSN:0021-2148, 1869-5868
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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.
AbstractList 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.
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. [PUBLICATION ABSTRACT]
Author Foletti, Carlotta
Hilvert, Donald
Beld , Joris
Metanis, Norman
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  givenname: Carlotta
  surname: Foletti
  fullname: Foletti, Carlotta
  organization: Laboratory of Organic Chemistry, ETH Zürich, 8093 Zürich, Switzerland phone:+41 44 632-3176 fax:+41 44 632-1486
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  givenname: Joris
  surname: Beld 
  fullname: Beld , Joris
  organization: Laboratory of Organic Chemistry, ETH Zürich, 8093 Zürich, Switzerland phone:+41 44 632-3176 fax:+41 44 632-1486
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  givenname: Donald
  surname: Hilvert
  fullname: Hilvert, Donald
  email: hilvert@org.chem.ethz.ch
  organization: Laboratory of Organic Chemistry, ETH Zürich, 8093 Zürich, Switzerland phone:+41 44 632-3176 fax:+41 44 632-1486
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Snippet Selenoglutathione has been shown to have considerable potential as a catalyst of oxidative protein folding. Here we examine how this reagent modulates the...
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SubjectTerms bovine pancreatic trypsin inhibitor
Catalysts
Conversion
Folding
Pathways
Protein folding
Proteins
redox chemistry
selenoglutathione
thiol/disulfide exchange
Trypsin inhibitors
Title Selenoglutathione-Mediated Rescue of Kinetically Trapped Intermediates in Oxidative Protein Folding
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https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fijch.201100105
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Volume 51
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