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Updated: May 11, 2026

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
Published on: October 2, 2018
Synthesis, Redox Properties, and Conformational Analysis of Vicinal Disulfide Ring Mimics
Erik L Ruggles1, P Bruce Deker, Robert J Hondal
1Department of Biochemistry, 89 Beaumont Ave., Given Building, University of Vermont, Burlington VT 05405 U.S.A.
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.
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