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

Nature volume 377, pages 251–254 (1995)Cite this article

Abstract

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.

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Authors and Affiliations

  1. Department of Physics, School of Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo, 169, Japan

    Takayuki Nishizaka & Shin'ichi Ishiwata

  2. Advanced Research Center for Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo, 169, Japan

    Shin'ichi Ishiwata

  3. Department of Physics, Faculty of Science and Technology, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama, 223, Japan

    Hidetake Miyata, Hiroshi Yoshikawa & Kazuhiko Kinosita Jr

Authors
  1. Takayuki Nishizaka
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  2. Hidetake Miyata
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  3. Hiroshi Yoshikawa
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  4. Shin'ichi Ishiwata
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  5. Kazuhiko Kinosita Jr
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Nishizaka, T., Miyata, H., Yoshikawa, H. et al. Unbinding force of a single motor molecule of muscle measured using optical tweezers. Nature 377, 251–254 (1995). https://doi.org/10.1038/377251a0

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