Abstract
We sumrnarize the mechanical and functional properties of a motormolecule of muscle studied with a new type of an in vitro motility assay system and a multi-imaging microscope system. First, supercoiling of an actin filament is shown, suggesting that the filament moves forward like a right-handed screw. Second, we describe the unbinding force and the lifetime of a rigor bond between a single myosin molecule and an actin filament measured by using optical tweezers. From these results, the mechanism of sliding and force generation of the motor molecule is discussed.
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