ArticleBiophysical journal2011
The fraction of myosin motors that participate in isometric contraction of rabbit muscle fibers at near-physiological temperature.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Thick filament activation is different in fast- and slow-twitch skeletal muscle.The Journal of physiology · 2022Article
- Anisotropic Elasticity of the Myosin Motor in Muscle.International journal of molecular sciences · 2022Article
- Changes in the Viscoelastic Properties of theFrontiers in physiology · 2020Article
- Myosin Head Configurations in Resting and Contracting Murine Skeletal Muscle.International journal of molecular sciences · 2018Article
- Tropomyosin movement is described by a quantitative high-resolution model of X-ray diffraction of contracting muscle.European biophysics journal : EBJ · 2017Article
- The Closed State of the Thin Filament Is Not Occupied in Fully Activated Skeletal Muscle.Biophysical journal · 2017Article
- Force per cross-sectional area from molecules to muscles: a general property of biological motors.Royal Society open science · 2016Article
- The lifetime of the actomyosin complex in vitro under load corresponding to stretch of contracting muscle.European biophysics journal : EBJ · 2015Article
- Non-channel mechanosensors working at focal adhesion-stress fiber complex.Pflugers Archiv : European journal of physiology · 2015Review
- Why muscle is an efficient shock absorber.PloS one · 2014Article
- Stiffness, working stroke, and force of single-myosin molecules in skeletal muscle: elucidation of these mechanical properties via nonlinear elasticity evaluation.Cellular and molecular life sciences : CMLS · 2013Review
- A cross-bridge cycle with two tension-generating steps simulates skeletal muscle mechanics.Biophysical journal · 2013Article
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6 authors.
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Abstract
The duty ratio, or the part of the working cycle in which a myosin molecule is strongly attached to actin, determines motor processivity and is required to evaluate the force generated by each molecule. In muscle, it is equal to the fraction of myosin heads that are strongly, or stereospecifically, bound to the thin filaments. Estimates of this fraction during isometric contraction based on stiffness measurements or the intensities of the equatorial or meridional x-ray reflections vary significantly. Here, we determined this value using the intensity of the first actin layer line, A1, in the low-angle x-ray diffraction patterns of permeable fibers from rabbit skeletal muscle. We calibrated the A1 intensity by considering that the intensity in the relaxed and rigor states corresponds to 0% and 100% of myosin heads bound to actin, respectively. The fibers maximally activated with Ca(2+) at 4°C were heated to 31-34°C with a Joule temperature jump (T-jump). Rigor and relaxed-state measurements were obtained on the same fibers. The intensity of the inner part of A1 during isometric contraction compared with that in rigor corresponds to 41-43% stereospecifically bound myosin heads at near-physiological temperature, or an average force produced by a head of ~6.3 pN.
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