巯基和脲基基团的偶联效应对促进氧化蛋白质折叠的作用。
Coupling effects of thiol and urea-type groups for promotion of oxidative protein folding.
机构信息
Department of Applied Chemistry, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan.
出版信息
Chem Commun (Camb). 2019 Jan 15;55(6):759-762. doi: 10.1039/c8cc08657e.
PMID:30506074
Abstract
Coupling of thiol and urea-type -NHC([double bond, length as m-dash]X)NH2 (X = O or NH) groups is effective in promoting oxidative protein folding. In particular, a thiol compound coupled with a guanidyl (X = NH) group significantly accelerates the rates of folding processes and enhances the yields of native proteins.
摘要
巯基和脲型 -NHC([双键, 长度为破折号]X)NH2（X = O 或 NH）基团的偶联在促进氧化蛋白质折叠中是有效的。特别是，与胍基（X = NH）基团偶联的巯基化合物显著加速折叠过程的速率并提高天然蛋白质的产率。
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