Vicinal disulfide turns |
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Authors: | Carugo Oliviero; Cemazar Masa; Zahariev Sotir; Hudaky Ilona; Gaspari Zoltan; Perczel Andras; Pongor Sandor |
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Affiliation: | 1International Centre for Genetic Engineering and Biotechnology, Padriciano 99, 34012 Trieste,
2Department of General Chemistry, University of Pavia, Viale Taramelli 12, 27100 Pavia, Italy and
3Department of Organic Chemistry, Eötvös L. University, 1117, Pázmány P. s. 1/a Budapest, Hungary |
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Abstract: | The formation of a disulfide bond between adjacent cysteineresidues is accompanied by the formation of a tight turn ofthe protein backbone. In nearly 90% of the structures analyzeda type VIII turn was found. The peptide bond between the twocysteines is in a distorted trans conformation, the omega torsionangle ranges from 159 to 133°, with an average valueof 171°. The constrained nature of the vicinal disulfideturn and the pronounced difference observed between the oxidizedand reduced states, suggests that vicinal disulfides may beemployed as a redox-activated conformational switch. Received December 16, 2002; revised June 30, 2003; accepted July 30, 2003. |
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