Mechanical measurements of single actomyosin motor force

H. Miyata, H. Yoshikawa, H. Hakozaki, N. Suzuki, T. Furuno, A. Ikegami, K. Kinosita, T. Nishizaka, S. Ishiwata, P. Driezen, A. Mehta

Research output: Contribution to journalArticlepeer-review

41 Citations (Scopus)


To elucidate the mechanism of force generation by actomyosin motor, a measuring system was constructed, in which an in vitro motility assay was combined with an optical trapping technique. An actin filament of several μm long was attached to a gelsolin-coated polystyrene bead, and was allowed to interact with a small number (~1/1-μm actin filament) of rabbit skeletal heavy meromyosin (an active subfragment of myosin) molecules bound to a nitrocellulose-coated coverglass. The bead position was determined at 33-ms intervals. We measured the force generation event at relatively low (100-400 nM) ATP concentration so that the occurrence of individual force generation events could be detected with our time resolution. The actin-bound bead held in the optical trap moved in a stepwise manner in the direction of the actin filament only in the presence of ATP. At the trap strength of 0.3 pN/nm, the maximum size of the step was 11 nm, and the maximum force associated with the movement was 3.3 pN.

Original languageEnglish
Pages (from-to)286s-290s
JournalBiophysical Journal
Issue number4 SUPPL.
Publication statusPublished - 1995

ASJC Scopus subject areas

  • Biophysics


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