| Literature DB >> 23828656 |
Erik L Ruggles1, Robert J Hondal.
Abstract
The cyclocystine ring structure (CRS, 3), which results from a disulfide-bond between adjacent cysteine residues, is a rare motif in protein structures and is functionally important to those few proteins that posses it. This communication will focus on the construction of CRS mimics and the determination of their respective redox potentials.Entities:
Keywords: cyclocystine; dithiocine; thiol-disulfide redox; vicinal disulfide-bond
Year: 2006 PMID: 23828656 PMCID: PMC3698869 DOI: 10.1016/j.tetlet.2006.04.023
Source DB: PubMed Journal: Tetrahedron Lett ISSN: 0040-4039 Impact factor: 2.415