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Kinesin ATPase cycles

Dynein, kinesin, and myosin are motor proteins with ATPase activity that convert the chemical bond energy released by ATP hydrolysis into mechanical work. Each motor molecule reacts cyclically with a polymerized cytoskeletal filament in this chemomechanical transduction process. The motor protein first binds to the filament and then undergoes a conformational change that produces an increment of movement, known as the power stroke. The motor protein then releases its hold on the filament before reattaching at a new site to begin another cycle. Events in the mechanical cycle are believed to depend on intermediate steps in the ATPase cycle. Cytoplasmic dynein and kinesin walk (albeit in opposite... [Pg.16]

Nishiyama M, Muto E, Inoue Y, Yanagida T, Higuchi H. 2001. Suhsteps within the 8-nm step of the ATPase cycle of single kinesin molecules. Nature Cell Biology 3 425. [Pg.20]


See other pages where Kinesin ATPase cycles is mentioned: [Pg.1088]    [Pg.1108]    [Pg.1]    [Pg.13]    [Pg.314]    [Pg.314]    [Pg.1884]    [Pg.1887]    [Pg.175]    [Pg.195]    [Pg.154]    [Pg.174]    [Pg.95]    [Pg.1885]    [Pg.1415]    [Pg.992]    [Pg.694]    [Pg.366]   
See also in sourсe #XX -- [ Pg.1108 , Pg.1109 ]




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ATPase cycle

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