The sliding-filament theory of muscle contraction. ([2019])
- Record Type:
- Book
- Title:
- The sliding-filament theory of muscle contraction. ([2019])
- Main Title:
- The sliding-filament theory of muscle contraction
- Further Information:
- Note: David Aitchison Smith.
- Authors:
- Aitchison Smith, David
- Contents:
- 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 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 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 AnIntro; 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 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 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 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 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 … (more)
- Publisher Details:
- Cham, Switzerland : Springer
- Publication Date:
- 2019
- Extent:
- 1 online resource (xv, 426 pages)
- Subjects:
- 573.7/5
Muscle contraction
Muscle contraction
Electronic books - Languages:
- English
- ISBNs:
- 9783030035266
3030035263 - Related ISBNs:
- 9783030035259
- Notes:
- Note: Includes bibliographical references and index.
Note: Description based on online resource; title from digital title page (viewed on March 07, 2019). - Access Rights:
- Legal Deposit; Only available on premises controlled by the deposit library and to one user at any one time; The Legal Deposit Libraries (Non-Print Works) Regulations (UK).
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- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library HMNTS - ELD.DS.386036
- Ingest File:
- 02_374.xml