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- W2013306005 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." @default.
- W2013306005 created "2016-06-24" @default.
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- W2013306005 date "2002-08-01" @default.
- W2013306005 modified "2023-10-12" @default.
- W2013306005 title "Direct Modeling of X-Ray Diffraction Pattern from Skeletal Muscle in Rigor" @default.
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- W2013306005 doi "https://doi.org/10.1016/s0006-3495(02)75232-6" @default.
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