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Oxidative folding intermediates with nonnative disulfide bridges between adjacent cysteine residues

The oxidative folding of the Amaranthus α-amylase inhibitor, a 32-residue cystine-knot protein with three disulfide bridges, was studied in vitro in terms of the disulfide content of the intermediate species. A nonnative vicinal disulfide bridge between cysteine residues 17 and 18 was found in three...

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Detalhes bibliográficos
Main Authors: Čemažar, Maša, Zahariev, Sotir, Lopez, Jakob J., Carugo, Oliviero, Jones, Jonathan A., Hore, P. J., Pongor, Sándor
Formato: Artigo
Idioma:Inglês
Publicado em: The National Academy of Sciences 2003
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC156273/
https://ncbi.nlm.nih.gov/pubmed/12724517
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.2225470100
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