Abstract
Muscle contraction results from alternate formation and breading of cross-links between the myosin head (subfragment 1; S-l), extending from the thick filament and a neighboring thin filament (Huxley A. F., 1957; Huxley H. E., 1969). The energy for contraction is supplied by ATP hydrolysis. Since the ATPase activity and actin binding site are localized in the S-l region of myosin, S-l is commonly believed to play a major role in muscle contraction. In fact, in vitro motility assay experiments have shown that S-l alone is sufficient to produce force and move actin filaments. However, the ATP-dependent actin-myosin sliding observed in the assay systems is not the same as that actually taking place in muscle.
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