| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5223161 | Tetrahedron | 2009 | 11 Pages |
Abstract
A vicinal disulfide ring (VDR) results from disulfide-bond formation between two adjacent cysteine residues. This eight-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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Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Erik L. Ruggles, P. Bruce Deker, Robert J. Hondal,