Conformations of unsolvated glycine-based peptides
被引:30
作者:
Hudgins, RR
论文数: 0引用数: 0
h-index: 0
机构:
Northwestern Univ, Dept Chem, Evanston, IL 60208 USANorthwestern Univ, Dept Chem, Evanston, IL 60208 USA
Hudgins, RR
[1
]
Jarrold, MF
论文数: 0引用数: 0
h-index: 0
机构:
Northwestern Univ, Dept Chem, Evanston, IL 60208 USANorthwestern Univ, Dept Chem, Evanston, IL 60208 USA
Jarrold, MF
[1
]
机构:
[1] Northwestern Univ, Dept Chem, Evanston, IL 60208 USA
来源:
JOURNAL OF PHYSICAL CHEMISTRY B
|
2000年
/
104卷
/
09期
关键词:
D O I:
10.1021/jp9935539
中图分类号:
O64 [物理化学(理论化学)、化学物理学];
学科分类号:
070304 ;
081704 ;
摘要:
The conformations of unsolvated glycine-based peptides have been probed using high-resolution ion mobility measurements and molecular dynamics simulations. Alanine-based Ac-Ala(n)-LysH(+) peptides have previously been shown to form helices in the gas phase. In contrast, the polyglycine analogues (Ac-Gly(n)-LysH(+)) do not form helices at room temperature; they adopt random globular conformations. Thus, the stabilities of alanine and glycine helices in vacuo are consistent with the helix propensities in aqueous solution, where alanine has the highest helix propensity and glycine has one of the lowest.