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.
A vicinal disulfide ring (VDR) results from n class="Chemical">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: Adrian P Dobbs; Sebastien J J Guesné; Sasa Martinović; Simon J Coles; Michael B Hursthouse Journal: J Org Chem Date: 2003-10-03 Impact factor: 4.354
Authors: Fei Li; Patricia B Lutz; Yuliya Pepelyayeva; Elias S J Arnér; Craig A Bayse; Sharon Rozovsky Journal: Proc Natl Acad Sci U S A Date: 2014-04-25 Impact factor: 11.205
Authors: Viet Q Le; Roxana E Iacob; Yuan Tian; William McConaughy; Justin Jackson; Yang Su; Bo Zhao; John R Engen; Michelle Pirruccello-Straub; Timothy A Springer Journal: EMBO J Date: 2018-01-17 Impact factor: 11.598