α因子的构象不受半胱氨酸12的S-异戊烯基化影响。

The conformation of a-factor is not influenced by the S-prenylation of Cys12.

作者信息

Gounarides J S, Broido M S, Xue C B, Becker J M, Naider F R

机构信息

Department of Chemistry, Hunter College, New York, NY.

出版信息

Biochem Biophys Res Commun. 1991 Dec 31;181(3):1125-30. doi: 10.1016/0006-291x(91)92055-o.

DOI:10.1016/0006-291x(91)92055-o

PMID:1764063

Abstract

Two-Dimensional NMR was used to examine the solution conformation of the lipopeptide a-factor, YIIKGVFWDPAC (S-farnesyl) OCH3, from the yeast Saccharomyces cerevisiae and five analogues containing various S-alkylated cysteines in DMSO-d6. NOESY data, NH temperature coefficients, and 3J alpha NH coupling constants indicate that the a-factor is a predominantly unstructured peptide in DMSO. Similar results were obtained for the other peptides indicating that S-prenylation of Cys12 does not affect the conformation of these peptides.

摘要

利用二维核磁共振技术研究了来自酿酒酵母的脂肽α-因子YIIKGVFWDPAC（S-法尼基）OCH₃及其在氘代二甲亚砜（DMSO-d6）中含有各种S-烷基化半胱氨酸的五个类似物的溶液构象。核Overhauser效应光谱（NOESY）数据、NH温度系数和³JαNH耦合常数表明，α-因子在DMSO中主要是一种无结构的肽。其他肽也得到了类似的结果，表明Cys12的S-异戊二烯化不影响这些肽的构象。