A minimal protein folding model to measure hydrophobic and CH-π effects on interactions between nonpolar surfaces in water

被引：82

作者：

Bhayana, Brijesh ^{[1
]}

Wilcox, Craig S. ^{[1
]}

机构：

[1] Univ Pittsburgh, Dept Chem, Pittsburgh, PA 15260 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2007年 / 46卷 / 36期

关键词：

conformation analysis; Gibbs energy hydrophobic; interactions; protein folding; solvent effects;

D O I：

10.1002/anie.200700932

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Figure Presented) In the balance: A synthetic molecule that exhibits two-state folding behavior in water is described. Quantitative experiments reveal that the microscopic hydrophobic effect is similar in magnitude to the CH-π, interaction. These forces may therefore be equally important in the folding of aromatic-rich regions of proteins. The method allows a new approach to the direct measurement of excess surface energy associated with nonpolar surfaces. © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：6833 / 6836

页数：4

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