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Updated: Aug 17, 2026

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
Published on: May 4, 2022
Atomic force microscopy of thermally treated myosin filaments
Tomohito Iwasaki1, Masahiro Washio, Katsuhiro Yamamoto
1Department of Food Science, Rakuno Gakuen University, Ebetsu, Hokkaido 069-8501, Japan. iwasaki@rakuno.ac.jp
Abstract:
Heat-induced morphological change in myosin filaments was observed using atomic force microscope. The thickness of fixed native myosin filament was estimated to be 95 +/- 5 nm. When myosin filaments in 0.1 M NaCl at pH 6.0 were heated at 40, 55, and 70 degrees C for 10 min, the particulate structure appeared spirally on the surface of the filament at 40 degrees C, and the thickness of the filament was 75 +/- 10 nm. When myosin filaments were treated at 55 degrees C, several filaments were formed associated with side-by-side interaction through projected myosin heads to form a strand. The surface of the strand looked knobby. The thickness of thermally denatured filaments at 55 degrees C was 48 +/- 5 nm, and that of strands was about 80-110 nm, indicating the involvement of several filaments in a strand. The strands became to be rope-like at 70 degrees C, and the individual filaments in a strand were not distinguishable.
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