Journal
PROTEIN ENGINEERING
Volume 16, Issue 9, Pages 637-639Publisher
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzg088
Keywords
beta-turns; disulfide bridge; protein structure; secondary structure
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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 -133degrees, with an average value of 171degrees. 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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