圆二色性
乙腈
两亲性
位阻效应
螺旋(腹足类)
化学
肽
α螺旋
立体化学
氨基酸
蛋白质二级结构
侧链
结晶学
有机化学
生物化学
共聚物
生物
聚合物
生态学
蜗牛
作者
Lars G.J. Hammarström,Ted J. Gauthier,Robert P. Hammer,Mark L. McLaughlin
出处
期刊:Journal of Peptide Research
[Wiley]
日期:2001-08-01
卷期号:58 (2): 108-116
被引量:13
标识
DOI:10.1034/j.1399-3011.2001.00858.x
摘要
A series of short, amphipathic peptides incorporating 80% C(alpha),C(alpha)-disubstituted glycines has been prepared to investigate amphipathicity as a helix-stabilizing effect. The peptides were designed to adopt 3(10)- or alpha-helices based on amphipathic design of the primary sequence. Characterization by circular dichroism spectroscopy in various media (1 : 1 acetonitrile/water; 9 : 1 acetonitrile/water; 9 : 1 acetonitrile/TFE; 25 mM SDS micelles in water) indicates that the peptides selectively adopt their designed conformation in micellar environments. We speculate that steric effects from ith and ith + 3 residues interactions may destabilize the 3(10)-helix in peptides containing amino acids with large side-chains, as with 1-aminocyclohexane-1-carboxylic acid (Ac(6)c). This problem may be overcome by alternating large and small amino acids in the ith and ith + 3 residues, which are staggered in the 3(10)-helix.
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