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  Redox-active cyclic bis(cysteinyl)peptides as catalysts for in vitro oxidative protein folding

Cabrele, C., Fiori, S., Pegoraro, S., & Moroder, L. (2002). Redox-active cyclic bis(cysteinyl)peptides as catalysts for in vitro oxidative protein folding. Chemistry & Biology, 9(6), 731-740.

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Genre: Journal Article
Alternative Title : Chem. Biol.

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 Creators:
Cabrele, C.1, Author              
Fiori, S.1, Author              
Pegoraro, S.1, Author              
Moroder, L.1, Author              
Affiliations:
1Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565160              

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 Abstract: The active-site hexapeptides of glutaredoxin (Grx), thioredoxin (Trx), protein disulfide isomerase (PDI), and thioredoxin- reductase (Trr) containing the common motif Cys-Xaa-Yaa-Cys were conformationally restricted by backbone cyclization, and their redox potentials were found to increase in the rank order of Trr < Grx < Trx < PDI peptide, with E'(o) values ranging between -204 mV and -130 mV. In each peptide the thiol pK(a) of one Cys residue was found to be lower than the other (e.g., 7.3 against 9.6 in the PDI peptide). Both the yield and rate of refolding of reduced RNase A in the presence of the bis(cysteinyl)peptides increased with the oxidizing character of the cyclic compounds. These results show that small peptides can function as adjuvants for the in vitro oxidative folding of proteins.

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Language(s): eng - English
 Dates: 2002-06
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 31373
ISI: 000176418100011
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Title: Chemistry & Biology
  Alternative Title : Chem. Biol.
Source Genre: Journal
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Pages: - Volume / Issue: 9 (6) Sequence Number: - Start / End Page: 731 - 740 Identifier: ISSN: 1074-5521