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

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

213 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)251-254
Number of pages4
Issue number6546
Publication statusPublished - 1995
Externally publishedYes

ASJC Scopus subject areas

  • General


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