Extreme stability of an unsolvated α-helix

被引：68

作者：

Kohtani, M ^{[1
]}

Jones, TC ^{[1
]}

Schneider, JE ^{[1
]}

Jarrold, MF ^{[1
]}

机构：

[1] Indiana Univ, Dept Chem, Bloomington, IN 47405 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2004年 / 126卷 / 24期

关键词：

D O I：

10.1021/ja048766c

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

High-temperature ion mobility measurements have been performed for α-helical Ac-A15K+H+ and globular Ac-KA15+H+ peptides. The α-helical and globular conformations do not melt into random coils as the temperature is raised. Instead, both conformations survive to the point where the peptide signals vanishes due to fragmentation. This occurs at 600 K for the globular Ac-KA15+H+ peptide and at 725 K for the α-helical Ac-A15K+H+. For the helical Ac-A15K+H+ peptide it appears that fragmentation is triggered by disruption of the helical conformation. Copyright © 2004 American Chemical Society.

引用

页码：7420 / 7421

页数：2

共 22 条

[1] Partition function zeros and finite size scaling of helix-coil transitions in a polypeptide [J].