Hydrogen-bond kinetics in the solvation shell of a polypeptide

被引：229

作者：

Xu, HF

Berne, BJ

机构：

[1] Columbia Univ, Dept Chem, New York, NY 10027 USA

[2] Columbia Univ, Ctr Biomol Simulat, New York, NY 10027 USA

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2001年 / 105卷 / 48期

关键词：

D O I：

10.1021/jp012749h

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：

Analysis of a series of molecular dynamics simulations reveals that the kinetics of breaking and forming water-water hydrogen bonds is slower in the first solvation shell of a 16-residue polypeptide than in bulk water. The correlation time of hydrogen bonds persists significantly longer near hydrophobic groups than in bulk water. Hydrogen bonds are found to be stronger in the solvation shell of nonpolar groups. We show that the difference in hydrogen-bond kinetics in the different environments can be understood in terms of the energetics and the concerted forming and breaking of hydrogen bonds.

引用

页码：11929 / 11932

页数：4

共 27 条

[1]

Allen M. P., 1987, COMPUTER SIMULATIONS, DOI [10.1093/oso/9780198803195.001.0001, DOI 10.1093/OSO/9780198803195.001.0001]

[2]

AMALENDU C, 2000, PHYS REV LETT, V85, P768

[3]

Berendsen H., 1981, INTERMOLECULAR FORCE, V331, P331, DOI [DOI 10.1007/978-94-015-7658-1_21, 10.1007/978-94-015-7658, DOI 10.1007/978-94-015-7658]

[4] A SHORT LINEAR PEPTIDE THAT FOLDS INTO A NATIVE STABLE BETA-HAIRPIN IN AQUEOUS-SOLUTION [J].