TEMPERATURE-FAVORED ASSEMBLY OF COLLAGEN IS DRIVEN BY HYDROPHILIC NOT HYDROPHOBIC INTERACTIONS

被引：146

作者：

LEIKIN, S ^{[1
]}

RAU, DC ^{[1
]}

PARSEGIAN, VA ^{[1
]}

机构：

[1] NIDDKD, DIV INTRAMURAL RES, BETHESDA, MD 20892 USA

来源：

NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 03期

关键词：

D O I：

10.1038/nsb0395-205

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

It has become almost axiomatic that protein folding and assembly are dominated by the hydrophobic effect. The contributions from this, and other, hydrophilic interactions can now be better distinguished by direct measurement of forces between proteins. Here we report the measurement of forces between triple helices of type I collagen at different temperatures, pH and solute concentrations. We separate repulsive and attractive components of the net force and analyze the origin of the attraction responsible for the collagen self-assembly. In this case the role of the hydrophobic effect appears to be negligible, Instead, water-mediated hydrogen bonding between polar residues is the most consistent explanation.

引用

页码：205 / 210

页数：6

共 38 条

[1] CRYSTAL-STRUCTURE AND MOLECULAR-STRUCTURE OF A COLLAGEN-LIKE PEPTIDE AT 1.9-ANGSTROM RESOLUTION [J].