title: Muscle contraction as a Markov process. I: Energetics of the process.
abstract: Force generation during muscle contraction can be understood in terms of cyclical length changes in segments of actin thin filaments moving through the three-dimensional lattice of myosin thick filaments. Recent anomalies discovered in connection with analysis of myosin step sizes in in vitro motility assays and with skinned fibres can be rationalized by assuming that ATP hydrolysis on actin accompanies these length changes. The paradoxically rapid regeneration of tension in quick release experiments, as well as classical energetic relationships, such as Hill's force-velocity curve, the Fenn effect, and the unexplained enthalpy of shortening, can be given mutually self-consistent explanations with this model. When muscle is viewed as a Markov process, the vectorial process of chemomechanical transduction can be understood in terms of lattice dependent transitions, wherein the phosphate release steps of the myosin and actin ATPases depend only on occurrence of allosteric changes in neighbouring molecules. Tropomyosin has a central role in coordinating the steady progression of these cooperative transitions along actin filaments and in gearing up the system in response to higher imposed loads.
authors.affiliation: Department of Chemistry, Princeton University, NJ 08544, USA.
authors.forename: C E
authors.initials: CE
authors.lastname: Schutt
authors.forename: U
authors.initials: U
authors.lastname: Lindberg
mesh_terms: D000199:Actins / Q000502:physiology; D000818:Animals; D004734:Energy Metabolism / Q000502:physiology*; D008954:Models, Biological; D009119:Muscle Contraction / Q000502:physiology*; D009132:Muscles / Q000378:metabolism / Q000502:physiology*; D009218:Myosins / Q000502:physiology
chemical_list: D000199:Actins; D009218:Myosins