title: Synthesis, Redox Properties, and Conformational Analysis of Vicinal Disulfide Ring Mimics.
abstract: A vicinal disulfide ring (VDR) results from disulfide bond formation between two adjacent cysteine residues. This 8-membered ring is a rare motif in protein structures and is functionally important to those few proteins that posses it. This article focuses on the construction of strained and unstrained VDR mimics, discernment of the preferred conformation of these mimics, and the determination of their respective disulfide redox potentials.
authors.affiliation: Department of Biochemistry, 89 Beaumont Ave., Given Building, University of Vermont, Burlington VT 05405 U.S.A.
authors.forename: Erik L
authors.initials: EL
authors.lastname: Ruggles
authors.forename: P Bruce
authors.initials: PB
authors.lastname: Deker
authors.forename: Robert J
authors.initials: RJ
authors.lastname: Hondal
keywords: cyclocystine; dithiazacanones; dithiocine; eight-membered ring; thiol disulfide redox; vicinal cysteines