Bending motions and internal motions in myosin rod.
Depolarized light scattering and high-resolution 1H NMR measurements were made on solutions of light meromyosin (LMM) and myosin rod in 0.6 M KCl-0.010 M pyrophosphate, pH 9.5, at 20 degrees C. The light scattering data indicated LMM is a rigid molecule. Myosin rod is best described as a once-broken rod with domains that can freely diffuse in conical volumes. The maximum angle that the cone surface makes with the myosin rod axis is 128 degrees, indicating the bending motion of the domains is largely unrestrained. NMR data indicated the fraction of the structure that could be in a random-coil configuration was equal and less than 0.04 for both hydrodynamically rigid LMM and bending myosin rod. Thus, the flexible bending of myosin rod appears to not be due to a random-coil structure.
D000818:Animals; D008027:Light; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D009132:Muscles / Q000032:analysis; D009218:Myosins / Q000032:analysis*; D009904:Optical Rotation; D011487:Protein Conformation; D011817:Rabbits; D012542:Scattering, Radiation
D009218:Myosins