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- W2061632152 abstract "Muscular force is generated by molecular interactions between the contractile proteins actin and myosin. The myosin filaments in the sarcomere of vertebrate muscle pack on a triangular array into which the actin filaments are interdigitated. High resolution studies of the actin-myosin interactions are performed by x-ray fiber diffraction analysis of whole muscle fibers. In most vertebrate muscles however, the myosin filaments pack in a so-called “superlattice” arrangement that involves a semi-random distribution of two filament rotations. The unknown effects of this disorder on diffraction by muscle fibres have so far prevented a rigorous analysis of x-ray fiber diffraction patterns in terms of the structure of this complex system. We report a quantitative model of the disorder and its incorporation into calculations of x-ray fiber diffraction patterns from model structures. This allows rapid calculation of the diffraction and does not involve numerical averaging over the disorder. Calculations show that the disorder modulates the Bragg reflections in diffraction patterns and introduces diffuse diffraction. The results of this analysis will allow the effects of the disorder to be included in muscle structure refinement programs, allowing more accurate structure determination from x-ray fiber diffraction data." @default.
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- W2061632152 date "2009-02-01" @default.
- W2061632152 modified "2023-09-30" @default.
- W2061632152 title "Modelling X-ray Diffraction From The Myosin Superlattice Of Vertebrate Muscle" @default.
- W2061632152 doi "https://doi.org/10.1016/j.bpj.2008.12.3255" @default.
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