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Updated: Aug 11, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
Published on: February 4, 2021
Flexibility in actin-myosin motility system revealed by in vitro motility assay
1Department of Biology, Ochanomizu University, Tokyo, Japan.
Abstract:
Flexibility of myosin molecule was studied by in vitro motility assay in terms of the direction of actin movement. Electron microscopy showed that HMM scattered on a nitrocellulose surface can bind actin filaments and form arrowhead-like patterns. Actin filaments can move in both directions on tracks of HMM made on a nitrocellulose surface. Further, actin filaments can move bidirectionally along native thick filaments over their central bare zone. These observations indicate that there is considerable flexibility in a myosin molecule and that the direction of the movement is determined by the polarity of actin filaments.
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