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BL
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| Record Number
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860086
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| Main Entry
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Aitchison Smith, David
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| Title & Author
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The sliding-filament theory of muscle contraction /\ David Aitchison Smith.
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| Publication Statement
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Cham, Switzerland :: Springer,, [2019]
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| Page. NO
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1 online resource (xv, 426 pages)
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| ISBN
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3030035263
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: 9783030035266
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9783030035259
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| Notes
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5.4.2 A Simple Quantitative Theory of Isotonic Oscillations
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| Bibliographies/Indexes
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Includes bibliographical references and index.
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| Contents
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Intro; Preface; Acknowledgements; Contents; Chapter 1: Introduction; 1.1 Historical Perspectives; 1.1.1 The Sliding Filament Model; 1.1.2 New Experimental Techniques; 1.1.3 Models of Contractility; 1.2 A Short Guide to Contractile Behaviour; 1.3 The Structure of Skeletal Muscle; 1.3.1 Muscle Ultrastructure; References; Chapter 2: Of Sliding Filaments and Swinging Lever-Arms; 2.1 Contractile Empiricism: Hillś Equations; 2.2 How Myosin Heads Find Actin Sites; 2.2.1 Head-Site Matching for Vernier Models; 2.2.2 Lattice Models: Target Zones, Layer Lines and Azimuthal Matching
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2.3 The First Sliding-Filament Model2.4 The Swinging-Lever-Arm Mechanism; 2.4.1 Mechanokinetics of the Working Stroke; 2.4.2 Theory of the Rapid Length-Step Response; References; Chapter 3: Actin-Myosin Biochemistry and Structure; 3.1 How Myosin and Actin Hydrolyze ATP; 3.1.1 Myosin is an ATPase; 3.1.2 Actomyosin is a Better ATPase; 3.1.3 Steady-State ATP Hydrolysis by Actin-Myosin; 3.2 The Biochemical Contraction Cycle; 3.2.1 Actin Binding Versus Nucleotide Binding; 3.2.2 A Biochemical Cycle for Myosin-S1; 3.2.3 Evidence for Two A.M. ADP States; 3.2.4 Evidence for Two M. ATP States
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3.3 Coordinating Lever-Arm Movements with Biochemical Events3.3.1 What Biochemical Event Triggers the Working Stroke?; 3.3.2 The Location of the Repriming Stroke; 3.3.3 An Amalgated Mechanochemical Cycle; 3.4 The Atomic Structure of Myosin Complexes; 3.4.1 Actin Binding; 3.4.2 Phosphate Release and the Working Stroke; 3.4.3 An ADP-Release Stroke; 3.4.4 ATP Binding and Actin Affinity; 3.4.5 The Repriming Stroke and Hydrolysis; 3.4.6 Hydrolysis on Actomyosin?; 3.4.7 The Pathway of the Stroke; References; Chapter 4: Models for Fully-Activated Muscle; 4.1 Strain-Dependent Kinetics
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4.1.1 Kramers ́Method for Reaction Rates4.1.2 Actin Binding: Swing, Roll and Lock; 4.1.3 The Kinetics of the Working Stroke; 4.1.4 An ADP-Release Stroke; 4.2 The Evolution of Contraction Models; 4.2.1 A Two-State Stroking Model; 4.2.2 The Search for a Simple Vernier Model; 4.2.3 Lattice Models; 4.3 Computational Methods; 4.3.1 Probabilistic Methods; 4.3.2 Monte-Carlo Simulation; 4.4 The Effects of Filament Elasticity; 4.4.1 The Equivalent Lumped Filament Compliance; 4.4.2 Experimental Consequences; 4.5 Target Zones, Dimeric Myosins and Buckling Rods
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4.5.1 Calculations with Target Zones and Dimeric Myosins4.5.2 An Updated 5-State Vernier Model; 4.5.3 Buckling Rods; 4.6 Adding Phosphate, ADP or ATP; 4.6.1 Added Phosphate; 4.6.2 Changing ADP or ATP; 4.7 The Effects of Temperature; References; Chapter 5: Transients, Stability and Oscillations; 5.1 Chemical Jumps and Temperature Jumps; 5.1.1 The Activation Jump; 5.1.2 Pi Jumps; 5.1.3 ATP Jumps; 5.1.4 Temperature Jumps; 5.2 Length Steps; 5.2.1 The Length-Step Response; 5.2.2 Repeated Length Steps; 5.3 Sinusoidal Length Changes; 5.4 Force Steps; 5.4.1 Isotonic Oscillations
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| Subject
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Muscle contraction.
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| Subject
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Muscle Contraction.
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| Subject
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Muscle contraction.
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| Dewey Classification
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573.7/5
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| LC Classification
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QP321.A38 2019
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| NLM classification
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WE 504
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