ArticleBiophysical journal2000
Characterization of single actomyosin rigor bonds: load dependence of lifetime and mechanical properties.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- Mechanics of blunting of actin-myosin interaction dynamics by the actinopathy-causing mutation E334Q in cytoskeletal γ-actin.The Journal of physiology · 2026Article
- Delayed phosphate release can highly improve energy efficiency of muscle contraction.Biophysical journal · 2025Article
- A reverse stroke characterizes the force generation of cardiac myofilaments, leading to an understanding of heart function.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Single-molecule pull-out manipulation of the shaft of the rotary motor FScientific reports · 2019Article
- Nonlinear Actomyosin Elasticity in Muscle?Biophysical journal · 2019Article
- Functional significance of HCM mutants of tropomyosin, V95A and D175N, studied withBiophysics and physicobiology · 2019Article
- 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
- Electron Microscopic Recording of the Power and Recovery Strokes of Individual Myosin Heads Coupled with ATP Hydrolysis: Facts and Implications.International journal of molecular sciences · 2018Review
- Single-molecule measurements of the effect of force on Thy-1/αvβ3-integrin interaction using nonpurified proteins.Molecular biology of the cell · 2018Article
- Radial stiffness characteristics of the overlap regions of sarcomeres in isolated skeletal myofibrils in pre-force generating state.Biophysics and physicobiology · 2017Article
- Actomyosin based contraction: one mechanokinetic model from single molecules to muscle?Journal of muscle research and cell motility · 2016Article
- A Restrictive Cardiomyopathy Mutation in an Invariant Proline at the Myosin Head/Rod Junction Enhances Head Flexibility and Function, Yielding Muscle Defects in Drosophila.Journal of molecular biology · 2016Article
- Probing fibronectin-antibody interactions using AFM force spectroscopy and lateral force microscopy.Beilstein journal of nanotechnology · 2015Article
- Unitary step of gliding machinery in Mycoplasma mobile.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Nonlinear cross-bridge elasticity and post-power-stroke events in fast skeletal muscle actomyosin.Biophysical journal · 2013Article
- A cross-bridge cycle with two tension-generating steps simulates skeletal muscle mechanics.Biophysical journal · 2013Article
- Radial stability of the actomyosin filament lattice in isolated skeletal myofibrils studied using atomic force microscopy.The journal of physiological sciences : JPS · 2013Article
- Emergent complexity of the cytoskeleton: from single filaments to tissue.Advances in physics · 2013Review
- The role of tropomyosin domains in cooperative activation of the actin-myosin interaction.Journal of molecular biology · 2011Article
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Authors and funding
5 authors.
Funding
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Abstract
Load dependence of the lifetime of the rigor bonds formed between a single myosin molecule (either heavy meromyosin, HMM, or myosin subfragment-1, S1) and actin filament was examined in the absence of nucleotide by pulling the barbed end of the actin filament with optical tweezers. For S1, the relationship between the lifetime (tau) and the externally imposed load (F) at absolute temperature T could be expressed as tau(F) = tau(0).exp(-F.d/k(B)T) with tau(0) of 67 s and an apparent interaction distance d of 2.4 nm (k(B) is the Boltzmann constant). The relationship for HMM was expressed by the sum of two exponentials, with two sets of tau(0) and d being, respectively, 62 s and 2.7 nm, and 950 s and 1.4 nm. The fast component of HMM coincides with tau(F) for S1, suggesting that the fast component corresponds to single-headed binding and the slow component to double-headed binding. These large interaction distances, which may be a common characteristic of motor proteins, are attributed to the geometry for applying an external load. The pulling experiment has also allowed direct estimation of the number of myosin molecules interacting with an actin filament. Actin filaments tethered to a single HMM molecule underwent extensive rotational Brownian motion, indicating a low torsional stiffness for HMM. From these results, we discuss the characteristics of interaction between actin and myosin, with the focus on the manner of binding of myosin.
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