ArticleBiophysical journal2008
Single-molecule measurement of the stiffness of the rigor myosin head.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 85 citations in OpenAlex.
- Distinct distributions of myosin motor conformations during contraction of slow and fast skeletal muscle.The Journal of physiology · 2026Article
- Characterizing the concentration and load dependence of phosphate binding to rabbit fast skeletal actomyosin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Four phases of a force transient emerge from a binary mechanical system.Journal of muscle research and cell motility · 2024Article
- Single-Molecule Investigation of Load-Dependent Actomyosin Dissociation Kinetics for Cardiac and Slow Skeletal Myosin.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Modeling thick filament activation suggests a molecular basis for force depression.Biophysical journal · 2024Article
- Thermodynamics and Kinetics of a Binary Mechanical System: Mechanisms of Muscle Contraction.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- Cardiac ventricular myosin and slow skeletal myosin exhibit dissimilar chemomechanical properties despite bearing the same myosin heavy chain isoform.The Journal of biological chemistry · 2022Article
- High-Speed Optical Traps Address Dynamics of Processive and Non-Processive Molecular Motors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- RETRACTED: Human sperm uses asymmetric and anisotropic flagellar controls to regulate swimming symmetry and cell steering.Science advances · 2020Article
- Single-molecule analysis reveals that regulatory light chains fine-tune skeletal myosin II function.The Journal of biological chemistry · 2020Article
- Straightening Out the Elasticity of Myosin Cross-Bridges.Biophysical journal · 2020Review
- Single molecule mechanics resolves the earliest events in force generation by cardiac myosin.eLife · 2019Article
- Comparing models with one versus multiple myosin-binding sites per actin target zone: The power of simplicity.The Journal of general physiology · 2019Article
- Nonlinear Actomyosin Elasticity in Muscle?Biophysical journal · 2019Article
- Positive cardiac inotrope omecamtiv mecarbil activates muscle despite suppressing the myosin working stroke.Nature communications · 2018Article
- A myosin II nanomachine mimicking the striated muscle.Nature communications · 2018Article
- Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?International journal of molecular sciences · 2018Review
- Mechanical parameters of the molecular motor myosin II determined in permeabilised fibres from slow and fast skeletal muscles of the rabbit.The Journal of physiology · 2018Article
- Sarcomere Stiffness during Stretching and Shortening of Rigor Skeletal Myofibrils.Biophysical journal · 2017Article
- Measuring the Kinetic and Mechanical Properties of Non-processive Myosins Using Optical Tweezers.Methods in molecular biology (Clifton, N.J.) · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The force-extension curve of single myosin subfragment-1 molecules, interacting in the rigor state with an actin filament, has been investigated at low [ATP] by applying a slow triangle-wave movement to the optical traps holding a bead-actin-bead dumbbell. In combination with a measurement of the overall stiffness of the dumbbell, this allowed characterization of the three extensible elements, the actin-bead links and the myosin. Simultaneously, another method, based on an analysis of bead position covariance, gave satisfactory agreement. The mean covariance-based estimate for the myosin stiffness was 1.79 pN/nm (SD = 0.7 pN/nm; SE = 0.06 pN/nm (n = 166 myosin molecules)), consistent with a recent report (1.7 pN/nm) from rabbit muscle fibers. In the triangle-wave protocol, the motion of the trapped beads during interactions was linear within experimental error over the physiological range of force applied to myosin (+/-10 pN), consistent with a Hookean model; any nonlinear terms could not be characterized. Bound states subjected to forces that resisted the working stroke (i.e., positive forces) detached at a significantly lower force than when subjected to negative forces, which is indicative of a strain-dependent dissociation rate.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.