ArticleBiophysical journal2002
Direct modeling of x-ray diffraction pattern from skeletal muscle in rigor.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- Destabilization of cardiac myosin acetylation and sequestration with type 2 diabetes mellitus.Cardiovascular diabetology · 2026Article
- Comparison of Predicted X-Ray Fiber Diffraction Patterns from All-Atom and Coarse-Grained Actin Filament Models Under Nonuniform Strain.International journal of molecular sciences · 2025Article
- Annotating the x-ray diffraction pattern of vertebrate striated muscle.Biophysical journal · 2025Article
- Interacting-heads motif explains the X-ray diffraction pattern of relaxed vertebrate skeletal muscle.Biophysical journal · 2022Article
- Anisotropic Elasticity of the Myosin Motor in Muscle.International journal of molecular sciences · 2022Article
- Geometric frustration in the myosin superlattice of vertebrate muscle.Journal of the Royal Society, Interface · 2021Article
- The myosin interacting-heads motif present in live tarantula muscle explains tetanic and posttetanic phosphorylation mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Different Myosin Head Conformations in Bony Fish Muscles Put into Rigor at Different Sarcomere Lengths.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
- Direct observation of tropomyosin binding to actin filaments.Cytoskeleton (Hoboken, N.J.) · 2015Article
- The intriguing dual lattices of the Myosin filaments in vertebrate striated muscles: evolution and advantage.Biology · 2014Review
- The fraction of myosin motors that participate in isometric contraction of rabbit muscle fibers at near-physiological temperature.Biophysical journal · 2011Article
- Myosin heads contribute to the maintenance of filament order in relaxed rabbit muscle.Biophysical journal · 2010Article
- Force-generating cross-bridges during ramp-shaped releases: evidence for a new structural state.Biophysical journal · 2009Article
- Dynamics of thin-filament activation in rabbit skeletal muscle fibers examined by time-resolved x-ray diffraction.Biophysical journal · 2009Article
- Direct modeling of X-ray diffraction pattern from contracting skeletal muscle.Biophysical journal · 2008Article
- RECENT IMPROVEMENTS IN SMALL ANGLE X-RAY DIFFRACTION FOR THE STUDY OF MUSCLE PHYSIOLOGY.Reports on progress in physics. Physical Society (Great Britain) · 2006Article
- Structural changes of actin-bound myosin heads after a quick length change in frog skeletal muscle.Biophysical journal · 2005Article
- Structural transients of contractile proteins upon sudden ATP liberation in skeletal muscle fibers.Biophysical journal · 2004Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Available high-resolution structures of F-actin, myosin subfragment 1 (S1), and their complex, actin-S1, were used to calculate a 2D x-ray diffraction pattern from skeletal muscle in rigor. Actin sites occupied by myosin heads were chosen using a "principle of minimal elastic distortion energy" so that the 3D actin labeling pattern in the A-band of a sarcomere was determined by a single parameter. Computer calculations demonstrate that the total off-meridional intensity of a layer line does not depend on disorder of the filament lattice. The intensity of the first actin layer A1 line is independent of tilting of the "lever arm" region of the myosin heads. Myosin-based modulation of actin labeling pattern leads not only to the appearance of the myosin and "beating" actin-myosin layer lines in rigor diffraction patterns, but also to changes in the intensities of some actin layer lines compared to random labeling. Results of the modeling were compared to experimental data obtained from small bundles of rabbit muscle fibers. A good fit of the data was obtained without recourse to global parameter search. The approach developed here provides a background for quantitative interpretation of the x-ray diffraction data from contracting muscle and understanding structural changes underlying muscle contraction.
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