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Vicinal disulfide turns.

Oliviero Carugo·Masa Cemazar·Sotir Zahariev·Ilona Hudáky·Zoltán Gáspári·András Perczel·Sándor Pongor
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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 degrees, with an average value of 171 degrees. 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.

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CysteineDisulfidesProtein EngineeringProtein FoldingProtein Structure, SecondaryJournal ArticleReview

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Oliviero Carugo, Masa Cemazar, Sotir Zahariev, Ilona Hudáky, Zoltán Gáspári, András Perczel, Sándor Pongor. 2003. Vicinal disulfide turns.. https://doi.org/10.1093/protein%2Fgzg088

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