Protein Engineering vol. 16 no. 9 pp. 637-639, 2003
© 2003 Oxford University Press
Vicinal disulfide turns
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ar11International 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
4 To whom correspondence should be addressed. e-mail: pongor{at}icgeb.trieste.it
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.
Received December 16, 2002; revised June 30, 2003; accepted July 30, 2003.
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