Actomyosin, a complex of actin filaments and myosin motor proteins, is responsible for force generation during muscle contraction. Toresolve the individual mechanical events of force generation by actomyosin, we have developed a new instrument with which we cancapture and directly manipulate individual myosin subfragment-1 molecules using a scanning probe. Single subfragment-1 moleculescan be visualized by using a fluorescent label. The data that we obtain using this technique are consistent with myosin moving along anactin filament with single mechanical steps of approximately 5.3 nanometres; groups of two to five rapid steps in succession oftenproduce displacements of 11 to 30 nanometres. This multiple stepping is produced by a single myosin head during just onebiochemical cycle of ATP hydrolysis.
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