title: The stiffness of myosin subfragment-1 changes with the physiological state of muscle.
abstract: The anisotropy decay of the spin-labelled myosin subfragment-1, takes place with different rates depending on the physiological state of muscle: relaxation, isometric contraction and rigor. The decay is mostly explained by the rotation of myosin subfragment-1. This rotation is promoted by thermal energy and is opposed by the viscous and by the elastic reactions. A model is proposed that relates the amplitude of the rotation of myosin subfragment-1 to its stiffness. It is found that the amplitude of the rotation is inversely proportional to the stiffness assigned to the structure. It is concluded that, in relaxed myofibrils, the stiffness of myosin subfragment-1 is much lower than that in myosin subfragment-1 - F-actin. The consequences of this finding on modeling of muscle contraction are discussed.
authors.affiliation: Dept. of Biochemistry and Molecular Biology, Ferrara University, Via Borsari 46, 44121 Ferrara, Italy. enrico.grazi@unife.it
authors.forename: Enrico
authors.initials: E
authors.lastname: Grazi
mesh_terms: D001696:Biomechanical Phenomena; D006244:Hardness; D055595:Mechanical Phenomena; D008954:Models, Biological; D009068:Movement; D009132:Muscles / Q000378:metabolism / Q000502:physiology*; D009210:Myofibrils / Q000378:metabolism / Q000502:physiology; D015879:Myosin Subfragments / Q000737:chemistry / Q000378:metabolism*; D018583:Pliability; D012399:Rotation
chemical_list: D015879:Myosin Subfragments