Abstract
X-ray diffraction and electron microscopy show that the myosin molecules in relaxed thick filaments of striated muscle have a helical arrangement, in which the heads of each molecule interact with each other to form the interacting heads motif (IHM). in relaxed mammalian skeletal muscle this helical ordering occurs only at temperatures higher than 20°C and is disrupted when temperature is decreased. Recent X-ray studies of live tarantula muscle have suggested that the two heads (blocked, BH, and free, FH) have very different roles and dynamics during contraction.
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