ArticleBiophysical journal2003
The conformation of myosin head domains in rigor muscle determined by X-ray interference.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- Mechanics of blunting of actin-myosin interaction dynamics by the actinopathy-causing mutation E334Q in cytoskeletal γ-actin.The Journal of physiology · 2026Article
- Anisotropic Elasticity of the Myosin Motor in Muscle.International journal of molecular sciences · 2022Article
- Analysis methods and quality criteria for investigating muscle physiology using x-ray diffraction.The Journal of general physiology · 2021Article
- Myosin lever arm orientation in muscle determined with high angular resolution using bifunctional spin labels.The Journal of general physiology · 2019Article
- Different Myosin Head Conformations in Bony Fish Muscles Put into Rigor at Different Sarcomere Lengths.International journal of molecular sciences · 2018Article
- Impact of familial hypertrophic cardiomyopathy-linked mutations in the NH2 terminus of the RLC on β-myosin cross-bridge mechanics.Journal of applied physiology (Bethesda, Md. : 1985) · 2014Article
- The contributions of filaments and cross-bridges to sarcomere compliance in skeletal muscle.The Journal of physiology · 2014Article
- Sarcomere-length dependence of myosin filament structure in skeletal muscle fibres of the frog.The Journal of physiology · 2014Article
- Difference in hydration structures between F-actin and myosin subfragment-1 detected by small-angle X-ray and neutron scattering.Biophysics (Nagoya-shi, Japan) · 2013Article
- Stiffness and fraction of Myosin motors responsible for active force in permeabilized muscle fibers from rabbit psoas.Biophysical journal · 2007Article
- RECENT IMPROVEMENTS IN SMALL ANGLE X-RAY DIFFRACTION FOR THE STUDY OF MUSCLE PHYSIOLOGY.Reports on progress in physics. Physical Society (Great Britain) · 2006Article
- New techniques in linear and non-linear laser optics in muscle research.Journal of muscle research and cell motility · 2006Review
- The structural basis of the increase in isometric force production with temperature in frog skeletal muscle.The Journal of physiology · 2005Article
- Strong binding of myosin heads stretches and twists the actin helix.Biophysical journal · 2005Article
- X-ray diffraction studies of the contractile mechanism in single muscle fibres.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004Review
- Recent X-ray diffraction studies of muscle contraction and their implications.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
In the absence of adenosine triphosphate, the head domains of myosin cross-bridges in muscle bind to actin filaments in a rigor conformation that is expected to mimic that following the working stroke during active contraction. We used x-ray interference between the two head arrays in opposite halves of each myosin filament to determine the rigor head conformation in single fibers from frog skeletal muscle. During isometric contraction (force T(0)), the interference effect splits the M3 x-ray reflection from the axial repeat of the heads into two peaks with relative intensity (higher angle/lower angle peak) 0.76. In demembranated fibers in rigor at low force (<0.05 T(0)), the relative intensity was 4.0, showing that the center of mass of the heads had moved 4.5 nm closer to the midpoint of the myosin filament. When rigor fibers were stretched, increasing the force to 0.55 T(0), the heads' center of mass moved back by 1.1-1.6 nm. These motions can be explained by tilting of the light chain domain of the head so that the mean angle between the Cys(707)-Lys(843) vector and the filament axis increases by approximately 36 degrees between isometric contraction and low-force rigor, and decreases by 7-10 degrees when the rigor fiber is stretched to 0.55 T(0).
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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.