Abstract
Motion and force are produced by myosin and actin in muscle and nonmuscle cells when myosin heads move along the surface of actin filaments. The energy is provided by the hydrolysis of ATP on the head of the myosin molecule. The details of the molecular motion in the myosin crossbridge have resisted characterization, in part because the crossbridge act asynchronously, even in the semicrystalline array of filaments found in striated muscles. Consequently, averaging techniques, including spectroscopic methods, tend to record a blurred signal from a large population of crossbridges.One way to circumvent this problem is :to examine individual myosin heads as they go through their cycle of ATP hydrolysis on the surface of the actin filament. The heads of myosin are large enough to image by EM, but the low affinity of active crossbridges for actin filaments complicates the situation.
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Schedule a callMore From: Proceedings, annual meeting, Electron Microscopy Society of America
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