ArticleBiophysical journal2008
Direct modeling of X-ray diffraction pattern from contracting skeletal muscle.
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 19 papers.
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Who cites it
19 citing papers in PubMed.
- Distinct distributions of myosin motor conformations during contraction of slow and fast skeletal muscle.The Journal of physiology · 2026Article
- The Structural Role of Tropomyosin in Regulating Thin Filament Activation of Actin-Myosin Interaction.Sub-cellular biochemistry · 2026Review
- Dual-filament regulation of relaxation in mammalian fast skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Using Multiscale Simulations as a Tool to Interpret Equatorial X-ray Fiber Diffraction Patterns from Skeletal Muscle.International journal of molecular sciences · 2023Article
- Small Angle X-ray Diffraction as a Tool for Structural Characterization of Muscle Disease.International journal of molecular sciences · 2022Review
- Myosin filament-based regulation of the dynamics of contraction in heart muscle.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Low temperature traps myosin motors of mammalian muscle in a refractory state that prevents activation.The Journal of general physiology · 2019Article
- High-speed AFM reveals subsecond dynamics of cardiac thin filaments upon CaProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Comparing models with one versus multiple myosin-binding sites per actin target zone: The power of simplicity.The Journal of general physiology · 2019Article
- 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
- The intriguing dual lattices of the Myosin filaments in vertebrate striated muscles: evolution and advantage.Biology · 2014Review
- Why muscle is an efficient shock absorber.PloS one · 2014Article
- Pre-power-stroke cross-bridges contribute to force transients during imposed shortening in isolated muscle fibers.PloS one · 2012Article
- The fraction of myosin motors that participate in isometric contraction of rabbit muscle fibers at near-physiological temperature.Biophysical journal · 2011Article
- FRET characterisation for cross-bridge dynamics in single-skinned rigor muscle fibres.European biophysics journal : EBJ · 2011Article
- X-ray fiber diffraction modeling of structural changes of the thin filament upon activation of live vertebrate skeletal muscles.Biophysics (Nagoya-shi, Japan) · 2010Article
- Force-generating cross-bridges during ramp-shaped releases: evidence for a new structural state.Biophysical journal · 2009Article
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4 authors.
Funding
Abstract
A direct modeling approach was used to quantitatively interpret the two-dimensional x-ray diffraction patterns obtained from contracting mammalian skeletal muscle. The dependence of the calculated layer line intensities on the number of myosin heads bound to the thin filaments, on the conformation of these heads and on their mode of attachment to actin, was studied systematically. Results of modeling are compared to experimental data collected from permeabilized fibers from rabbit skeletal muscle contracting at 5 degrees C and 30 degrees C and developing low and high isometric tension, respectively. The results of the modeling show that: i), the intensity of the first actin layer line is independent of the tilt of the light chain domains of myosin heads and can be used as a measure of the fraction of myosin heads stereospecifically attached to actin; ii), during isometric contraction at near physiological temperature, the fraction of these heads is approximately 40% and the light chain domains of the majority of them are more perpendicular to the filament axis than in rigor; and iii), at low temperature, when isometric tension is low, a majority of the attached myosin heads are bound to actin nonstereospecifically whereas at high temperature and tension they are bound stereospecifically.
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