The titin-telethonin complex is a directed, superstable molecular bond in the muscle Z-disk

Morten Bertz, Matthias Wilmanns, Matthias Rief*

*この研究の対応する著者

研究成果: Article査読

79 被引用数 (Scopus)

抄録

Mechanical stability of bonds and protein interactions has recently become accessible through single molecule mechanical experiments. So far, mechanical information about molecular bond mechanics has been largely limited to a single direction of force application. However, mechanical force acts as a vector in space and hence mechanical stability should depend on the direction of force application. In skeletal muscle, the giant protein titin is anchored in the Z-disk by telethonin. Much of the structural integrity of the Z-disk hinges upon the titin-telethonin bond. In this paper we show that the complex between the muscle proteins titin and telethonin forms a highly directed molecular bond. It is designed to resist ultra-high forces if they are applied in the direction along which it is loaded under physiological conditions, while it breaks easily along other directions. Highly directed molecular bonds match in an ideal way the requirements of tissues subject to mechanical stress.

本文言語English
ページ(範囲)13307-13310
ページ数4
ジャーナルProceedings of the National Academy of Sciences of the United States of America
106
32
DOI
出版ステータスPublished - 2009 8月 11
外部発表はい

ASJC Scopus subject areas

  • 一般

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