Vicinal disulfide turns

Oliviero Carugo, Maša Čemažar, Sotir Zahariev, Ilona Hudáky, Zoltán Gáspári, András Perczel, Sándor Pongor

Research output: Article

89 Citations (Scopus)

Abstract

The formation of a disulfide bond between adjacent cysteine residues is accompanied by the formation of a tight turn of the protein backbone. In nearly 90% of the structures analyzed a type VIII turn was found. The peptide bond between the two cysteines is in a distorted trans conformation, the omega torsion angle ranges from 159 to -133°, with an average value of 171°. The constrained nature of the vicinal disulfide turn and the pronounced difference observed between the oxidized and reduced states, suggests that vicinal disulfides may be employed as a 'redox-activated' conformational switch.

Original languageEnglish
Pages (from-to)637-639
Number of pages3
JournalProtein Engineering
Volume16
Issue number9
DOIs
Publication statusPublished - szept. 2003

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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  • Cite this

    Carugo, O., Čemažar, M., Zahariev, S., Hudáky, I., Gáspári, Z., Perczel, A., & Pongor, S. (2003). Vicinal disulfide turns. Protein Engineering, 16(9), 637-639. https://doi.org/10.1093/protein/gzg088