Unbinding force of a single motor molecule of muscle measured using optical tweezers

Takayuki Nishizaka, Hidetake Miyata, Hiroshi Yoshikawa, Shin'ichi Ishiwata*, Kazuhiko Kinosita

*この研究の対応する著者

研究成果: Article査読

201 被引用数 (Scopus)

抄録

THE unbinding and rebinding of motor proteins and their substrate filaments are the main components of sliding movement1. We have measured the unbinding force between an actin filament and a single motor molecule of muscle, myosin, in the absence of ATP, by pulling the filament with optical tweezers2. The unbinding force could be measured repeatedly on the same molecule, and was independent of the number of measurements and the direction of the imposed loads within a range of ±90°. The average unbinding force was 9.2 ± 4.4 pN, only a few times larger than the sliding force3"5 but an order of magnitude smaller than other intermolecular forces6,7. From its kinetics8 we suggest that unbinding occurs sequentially at the molecular interface, which is an inherent property of motor molecules.

本文言語English
ページ(範囲)251-254
ページ数4
ジャーナルNature
377
6546
出版ステータスPublished - 1995
外部発表はい

ASJC Scopus subject areas

  • 一般

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