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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.

SUBMITTER: Ruggles EL 

PROVIDER: S-EPMC3653589 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature

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Synthesis, Redox Properties, and Conformational Analysis of Vicinal Disulfide Ring Mimics.

Ruggles Erik L EL   Deker P Bruce PB   Hondal Robert J RJ  

Tetrahedron 20090201 7


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. ...[more]

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