By Polarz S.
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J. (2004) Is the dynein motor a winch? Curr. Opin. Struct. , 14, 138–146. , and Oiwa, K. (2003) Dynein structure and power stroke. Nature, 421, 715–718. L. (2006) Swimming efficiency of bacterium Escherichia coli. Proc. Natl. Acad. Sci. U. S. , 103, 13712–13717. , and Bryant, Z. (2012) Engineering controllable bidirectional molecular motors based on myosin. Nat. , 7, 252–256. Childress, S. (1981) Mechanics of Swimming and Flying. K. , and Vogel, V. (2004) Motor-protein “roundabouts”: microtubules moving on kinesin-coated tracks through engineered networks.
Kinesin thus performs about 100 steps before detaching from the microtubule. Such cellular transport greatly benefits from the high force of kinesin motors. 2 Chemically Powered Motor Proteins 19 of a single ATP molecule, implying an energy conversion efficiency higher than 50%. 4 Myosins Myosins constitute a large family of ATP-driven motor proteins, which has been shown to interact with actin, hydrolyze cellular ATP, and produce force and movement (Sellers, 1999). Myosin-based molecular machines are involved in the process of force generation during muscle contraction, wherein thin actin filaments and thick myosin filaments slide past each other.
1 Stimuli-Responsive Rotaxane, Pseudorotaxane, and Catenane Nanomachines Interlocked molecular systems based on rotaxane, pseudorotaxane, and catenane structures can be cycled reversibly as a consequence of an external stimulus, and hence have considerable potential as components of molecular machinery. Such artificial molecular switches commonly rely on reversible changes in the relative positions of the interlocked components in response to such an external input. These interlocked systems have experienced a remarkable progress over the past decade, as noncovalent forces have been utilized to effectively assemble interlocked nanostructures in which at least two molecular components are mechanically intertwined, without any covalent bonds between them.