Ruggles Erik L, Deker P Bruce, Hondal Robert J
Department of Biochemistry, 89 Beaumont Ave., Given Building, University of Vermont, Burlington VT 05405 U.S.A.
Tetrahedron. 2009 Feb 14;65(7):1257-1267. doi: 10.1016/j.tet.2008.11.085.
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.
邻二硫环(VDR)是由两个相邻的半胱氨酸残基之间形成二硫键产生的。这个八元环在蛋白质结构中是一种罕见的基序,对拥有它的少数蛋白质具有重要的功能意义。本文重点关注张力和非张力VDR模拟物的构建、这些模拟物的优选构象的识别以及它们各自的二硫键氧化还原电位的测定。