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This volume presents the entire proceedings of the symposium organized by one of us (H. S. ) on November 11 to 15, 1991 at Hakone, Japan, under the title of "Mechanism of Myofllament Sliding in Muscle Contraction. " Among various kinds of energy transduction mechanisms in biological systems, the mechanism of muscle contraction has been studied most intensively and extensively over many years. Since the monumental discovery by the two Huxleys and coworkers that muscle contraction results from relative sliding between the thick and thin myofilaments, attention of muscle investigators has been focused on the question, what makes the fllaments slide past one another. In response to the above question, A. F. Huxley and Simmons put forward a contraction model in 1971, in which globular heads of myosin (cross-bridges) extending from the thick fllament first attach to actin on the thin fllament, and then change their angle of attachment to actin (power stroke) leading to force generation or myofilament sliding until they detach from the thin fllament. The rocking cross-bridge contraction model seemed to be entirely consistent with the kinetic scheme of actomyosin ATPase published by Lymn and Taylor at the same time, thus giving a strong impression to the people concerned that the muscle contraction mechanism would soon be sorted out. In his review lecture in 1974, however, A. F.
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Contenuti
Structural Basis of Myofilament Sliding: A New Crystal Form of Tropomyosin; A. Miegel, et al. Regulatory Mechanisms of Contraction: Activation and Relaxation Mechanisms in Single Muscle Fibers; C.C. Ashley, et al. Biochemical Aspects of Actin-Myosin Interaction: Interaction Between Two Myosin Heads in Acto-Smooth Muscle Heavy Meromyosin Rigor Complex; H. Onishi Properties of Actin-Myosin Sliding Studied by In vitro Movement Assay Systems. Properties of Actin-Myosin Sliding and Force Generation Studied by In vitro Force Movement Assay Systems. Structural Changes During Contraction Studied by X-Ray Diffraction: Kinetic Properties of Actin-Myosin Sliding in Muscle Studied by Flash Photolysis of Caged Substances and Temperature Jump. Kinetic Properties of Actin-Myosin Sliding Studied with Demembranated Systems. Kinetic Properties of Actin-Myosin Sliding Studied with Intact Muscle Fibers. Kinetic Properties of Actin-Myosin Sliding Studied by Energetics Experiments. Concluding Discussions. 83 additional articles. Index.
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Condizione: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Proceedings of a Symposium held in Hakone, Japan, November 11-15, 1991 This volume presents the entire proceedings of the symposium organized by one of us (H. S. ) on November 11 to 15, 1991 at Hakone, Japan, under the title of Mechanism of Myofllamen. Codice articolo 4194437
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Taschenbuch. Condizione: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -This volume presents the entire proceedings of the symposium organized by one of us (H. S. ) on November 11 to 15, 1991 at Hakone, Japan, under the title of 'Mechanism of Myofllament Sliding in Muscle Contraction. ' Among various kinds of energy transduction mechanisms in biological systems, the mechanism of muscle contraction has been studied most intensively and extensively over many years. Since the monumental discovery by the two Huxleys and coworkers that muscle contraction results from relative sliding between the thick and thin myofilaments, attention of muscle investigators has been focused on the question, what makes the fllaments slide past one another. In response to the above question, A. F. Huxley and Simmons put forward a contraction model in 1971, in which globular heads of myosin (cross-bridges) extending from the thick fllament first attach to actin on the thin fllament, and then change their angle of attachment to actin (power stroke) leading to force generation or myofilament sliding until they detach from the thin fllament. The rocking cross-bridge contraction model seemed to be entirely consistent with the kinetic scheme of actomyosin ATPase published by Lymn and Taylor at the same time, thus giving a strong impression to the people concerned that the muscle contraction mechanism would soon be sorted out. In his review lecture in 1974, however, A. F. 908 pp. Englisch. Codice articolo 9781461362456
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Taschenbuch. Condizione: Neu. This item is printed on demand - Print on Demand Titel. Neuware -This volume presents the entire proceedings of the symposium organized by one of us (H. S. ) on November 11 to 15, 1991 at Hakone, Japan, under the title of 'Mechanism of Myofllament Sliding in Muscle Contraction. ' Among various kinds of energy transduction mechanisms in biological systems, the mechanism of muscle contraction has been studied most intensively and extensively over many years. Since the monumental discovery by the two Huxleys and coworkers that muscle contraction results from relative sliding between the thick and thin myofilaments, attention of muscle investigators has been focused on the question, what makes the fllaments slide past one another. In response to the above question, A. F. Huxley and Simmons put forward a contraction model in 1971, in which globular heads of myosin (cross-bridges) extending from the thick fllament first attach to actin on the thin fllament, and then change their angle of attachment to actin (power stroke) leading to force generation or myofilament sliding until they detach from the thin fllament. The rocking cross-bridge contraction model seemed to be entirely consistent with the kinetic scheme of actomyosin ATPase published by Lymn and Taylor at the same time, thus giving a strong impression to the people concerned that the muscle contraction mechanism would soon be sorted out. In his review lecture in 1974, however, A. F.Springer-Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg 908 pp. Englisch. Codice articolo 9781461362456
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Taschenbuch. Condizione: Neu. Druck auf Anfrage Neuware - Printed after ordering - This volume presents the entire proceedings of the symposium organized by one of us (H. S. ) on November 11 to 15, 1991 at Hakone, Japan, under the title of 'Mechanism of Myofllament Sliding in Muscle Contraction. ' Among various kinds of energy transduction mechanisms in biological systems, the mechanism of muscle contraction has been studied most intensively and extensively over many years. Since the monumental discovery by the two Huxleys and coworkers that muscle contraction results from relative sliding between the thick and thin myofilaments, attention of muscle investigators has been focused on the question, what makes the fllaments slide past one another. In response to the above question, A. F. Huxley and Simmons put forward a contraction model in 1971, in which globular heads of myosin (cross-bridges) extending from the thick fllament first attach to actin on the thin fllament, and then change their angle of attachment to actin (power stroke) leading to force generation or myofilament sliding until they detach from the thin fllament. The rocking cross-bridge contraction model seemed to be entirely consistent with the kinetic scheme of actomyosin ATPase published by Lymn and Taylor at the same time, thus giving a strong impression to the people concerned that the muscle contraction mechanism would soon be sorted out. In his review lecture in 1974, however, A. F. Codice articolo 9781461362456
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Mechanism of Myofilament Sliding in Muscle Contraction (Advances in Experimental Medicine and Biology, 332)
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