ArticleBiophysical journal2010
Myosin heads contribute to the maintenance of filament order in relaxed rabbit muscle.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Predicting organoid morphology through a phase field model: Insights into cell division and lumenal pressure.PLoS computational biology · 2025Article
- Sarcomere, troponin, and myosin X-ray diffraction signals can be resolved in single cardiomyocytes.Biophysical journal · 2024Article
- Dependence of myosin filament structure on intracellular calcium concentration in skeletal muscle.The Journal of general physiology · 2023Article
- Using Multiscale Simulations as a Tool to Interpret Equatorial X-ray Fiber Diffraction Patterns from Skeletal Muscle.International journal of molecular sciences · 2023Article
- Dependence of thick filament structure in relaxed mammalian skeletal muscle on temperature and interfilament spacing.The Journal of general physiology · 2021Article
- Nebulin stiffens the thin filament and augments cross-bridge interaction in skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Myosin Head Configurations in Resting and Contracting Murine Skeletal Muscle.International journal of molecular sciences · 2018Article
- Effects of myosin inhibitors on the X-ray diffraction patterns of relaxed and calcium-activated rabbit skeletal muscle fibers.Biophysics and physicobiology · 2018Article
- Radial stability of the actomyosin filament lattice in isolated skeletal myofibrils studied using atomic force microscopy.The journal of physiological sciences : JPS · 2013Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Raising the temperature of rabbit skeletal muscle from ∼0°C to ∼20°C has been shown to enhance the helical organization of the myosin heads and to change the intensities of the 10 and 11 equatorial reflections. We show here by time-resolved x-ray diffraction combined with temperature jump that the movement of the heads to enhance the organized myosin helix occurs at the same fast rate as the change in the intensities of the equatorial reflections. However, model calculations indicate that the change in the equatorials cannot be explained simply in terms of the movement of myosin heads. Analysis of electron micrographs of transverse sections of relaxed muscle fibers cryofixed at ∼5°C and ∼35°C shows that in addition to the reorganization of the heads the thin and thick filaments are less constrained to their positions in the hexagonal filament lattice in the warm muscle than in the cold. Incorporating the changes in filament order in model calculations reconciles these with the observed changes in equatorial reflections. We suggest the thin filaments in the cold muscle are boxed into their positions by the thermal movement of the disordered myosin heads. In the warmer muscle, the packed-down heads leave the thin filaments more room to diffuse laterally.
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Registered trials
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