DIRECT MEASUREMENT OF FORCES BETWEEN SELF-ASSEMBLED PROTEINS - TEMPERATURE-DEPENDENT EXPONENTIAL FORCES BETWEEN COLLAGEN TRIPLE HELICES

被引：136

作者：

LEIKIN, S ^{[1
]}

RAU, DC ^{[1
]}

PARSEGIAN, VA ^{[1
]}

机构：

[1] NIDDKD, BIOCHEM & METAB LAB, BETHESDA, MD 20892 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1994年 / 91卷 / 01期

关键词：

D O I：

10.1073/pnas.91.1.276

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

We report direct measurements of force vs. separation between self-assembled proteins. These forces are observed between collagen triple helices in native and reconstituted fibers. They are a combination of a short-range repulsion, which varies exponentially over at least five decay lengths, and an inferred, longer-ranged attraction responsible for spontaneous assembly. From 5-degrees-C to 35-degrees-C the relative contribution of the attraction to the net force increases with temperature. These forces are strikingly similar to the ''hydration'' forces measured between several other linear macromolecules (DNA, polysaccharides) and between lipid bilayer membranes. The decay length of the repulsive force agrees well with a theoretical estimate based on axial periodicity of the triple helix, suggesting another connection between molecular architecture and protein-protein interaction.

引用

页码：276 / 280

页数：5

共 35 条

[1]

BRODSKY B, 1982, METHOD ENZYMOL, V82, P127

[2] DOMINANT FORCES IN PROTEIN FOLDING [J].