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      Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization.

      Science (New York, N.Y.)

      metabolism, Actin Cytoskeleton, Rhodamines, Protein Structure, Tertiary, chemistry, Myosin Type V, Myosin Light Chains, Molecular Motor Proteins, Models, Biological, Microscopy, Fluorescence, Mathematics, Kinetics, Fluorescent Dyes, Fluorescence, DNA, Catalytic Domain, Carbocyanines, Calmodulin, Binding Sites, Adenosine Triphosphate, Actins, ultrastructure

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          Abstract

          Myosin V is a dimeric molecular motor that moves processively on actin, with the center of mass moving approximately 37 nanometers for each adenosine triphosphate hydrolyzed. We have labeled myosin V with a single fluorophore at different positions in the light-chain domain and measured the step size with a standard deviation of <1.5 nanometers, with 0.5-second temporal resolution, and observation times of minutes. The step size alternates between 37 + 2x nm and 37 - 2x, where x is the distance along the direction of motion between the dye and the midpoint between the two heads. These results strongly support a hand-over-hand model of motility, not an inchworm model.

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          Journal
          10.1126/science.1084398
          12791999

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