Interpretation of the X-ray diffraction pattern from relaxed skeletal muscle and modelling of the thick filament structure

1992 ◽  
Vol 13 (4) ◽  
pp. 406-419 ◽  
Author(s):  
S. B. Malinchik ◽  
V. V. Lednev
Keyword(s):  
Skeletal Muscle ◽  
Diffraction Pattern ◽  
Thick Filament ◽  
X Ray Diffraction ◽  
X Ray ◽  
Filament Structure

An ultrastructural study of crossbridge arrangement in the fish skeletal muscle thick filament

1989 ◽  
Vol 94 (3) ◽  
pp. 391-401
Author(s):  
R.W. Kensler ◽  
M. Stewart
Keyword(s):  
Skeletal Muscle ◽  
Fourier Transforms ◽  
Thick Filament ◽  
Fish Muscle ◽  
X Ray Diffraction ◽  
X Ray ◽  
Thick Filaments ◽  
Gold Fish ◽  
Diffraction Patterns ◽  
Cross Bridges

A procedure has been developed for isolating gold-fish skeletal muscle thick filaments that preserves the near-helical arrangement of the myosin cross-bridges under relaxing conditions. These filaments have been examined by electron microscopy and computer image analysis. Electron micrographs of the negatively stained filaments showed a clear periodicity associated with the crossbridges, with an axial repeat every 42.9 nm. Computed Fourier transforms of the negatively stained filaments showed a series of layer lines confirming this periodicity, and were similar to the X-ray diffraction patterns of fish muscle obtained by J. Hartford and J. Squire. Analysis of the computed transform data and filtered images of the isolated fish filaments demonstrated that the myosin crossbridges lie along three strands. Platinum shadowing demonstrated that the strands have a right-handed orientation, and computed transforms and filtered images of the shadowed filaments suggest that the crossbridges are perturbed both axially and azimuthally from an ideal helical arrangement.

scholarly journals Direct Modeling of X-Ray Diffraction Pattern from Contracting Skeletal Muscle

2008 ◽  
Vol 95 (6) ◽  
pp. 2880-2894 ◽  
Author(s):  
Natalia A. Koubassova ◽  
Sergey Y. Bershitsky ◽  
Michael A. Ferenczi ◽  
Andrey K. Tsaturyan
Keyword(s):  
Skeletal Muscle ◽  
Diffraction Pattern ◽  
X Ray Diffraction ◽  
X Ray ◽  
Direct Modeling

scholarly journals Changes in Thick Filament Structure of Isolated Intact Rat Cardiac Muscle During Contraction Determined by 2-D X-ray Diffraction Analysis

2009 ◽  
Vol 96 (3) ◽  
pp. 619a
Author(s):  
Gerrie P. Farman ◽  
Edward J. Allen ◽  
Kelly Q. Schoenfelt ◽  
David Gore ◽  
Peter H. Backx ◽  
...  
Keyword(s):  
Diffraction Analysis ◽  
Cardiac Muscle ◽  
Thick Filament ◽  
X Ray Diffraction ◽  
X Ray ◽  
Filament Structure

scholarly journals Dependence of thick filament structure in relaxed mammalian skeletal muscle on temperature and interfilament spacing

2021 ◽  
Vol 153 (3) ◽  
Author(s):  
Marco Caremani ◽  
Luca Fusi ◽  
Marco Linari ◽  
Massimo Reconditi ◽  
Gabriella Piazzesi ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Thick Filament ◽  
Structural Basis ◽  
Mammalian Skeletal Muscle ◽  
X Ray ◽  
Physiological Temperature ◽  
Thick Filaments ◽  
Filament Structure ◽  
Intact Muscle ◽  
Resting Muscle

Contraction of skeletal muscle is regulated by structural changes in both actin-containing thin filaments and myosin-containing thick filaments, but myosin-based regulation is unlikely to be preserved after thick filament isolation, and its structural basis remains poorly characterized. Here, we describe the periodic features of the thick filament structure in situ by high-resolution small-angle x-ray diffraction and interference. We used both relaxed demembranated fibers and resting intact muscle preparations to assess whether thick filament regulation is preserved in demembranated fibers, which have been widely used for previous studies. We show that the thick filaments in both preparations exhibit two closely spaced axial periodicities, 43.1 nm and 45.5 nm, at near-physiological temperature. The shorter periodicity matches that of the myosin helix, and x-ray interference between the two arrays of myosin in the bipolar filament shows that all zones of the filament follow this periodicity. The 45.5-nm repeat has no helical component and originates from myosin layers closer to the filament midpoint associated with the titin super-repeat in that region. Cooling relaxed or resting muscle, which partially mimics the effects of calcium activation on thick filament structure, disrupts the helical order of the myosin motors, and they move out from the filament backbone. Compression of the filament lattice of demembranated fibers by 5% Dextran, which restores interfilament spacing to that in intact muscle, stabilizes the higher-temperature structure. The axial periodicity of the filament backbone increases on cooling, but in lattice-compressed fibers the periodicity of the myosin heads does not follow the extension of the backbone. Thick filament structure in lattice-compressed demembranated fibers at near-physiological temperature is similar to that in intact resting muscle, suggesting that the native structure of the thick filament is largely preserved after demembranation in these conditions, although not in the conditions used for most previous studies with this preparation.

scholarly journals 1P184 The effect of muscle length changes on the x-ray diffraction pattern from tetanized frog skeletal muscle

2004 ◽  
Vol 44 (supplement) ◽  
pp. S75
Author(s):  
H. Tanaka ◽  
T. Kobayashi ◽  
Y. Takezawa ◽  
Y. Sugimoto ◽  
K. Oshima ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Diffraction Pattern ◽  
Muscle Length ◽  
Frog Skeletal Muscle ◽  
X Ray Diffraction ◽  
X Ray ◽  
Length Changes

scholarly journals Direct Modeling of X-Ray Diffraction Pattern from Skeletal Muscle in Rigor

2002 ◽  
Vol 83 (2) ◽  
pp. 1082-1097 ◽  
Author(s):  
Natalia A. Koubassova ◽  
A.K. Tsaturyan
Keyword(s):  
Skeletal Muscle ◽  
Diffraction Pattern ◽  
X Ray Diffraction ◽  
X Ray ◽  
Direct Modeling

scholarly journals The effect of successive stretches on the X-ray diffraction pattern in tetanized frog skeletal muscle

2003 ◽  
Vol 43 (supplement) ◽  
pp. S130
Author(s):  
T. Kobayashi ◽  
H. Tanaka ◽  
K. Wakabayashi ◽  
Y. Takezawa ◽  
Y. Sugimoto ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Diffraction Pattern ◽  
Frog Skeletal Muscle ◽  
X Ray Diffraction ◽  
X Ray

scholarly journals Lattice arrangement of myosin filaments correlates with fiber type in rat skeletal muscle

2019 ◽  
Vol 151 (12) ◽  
pp. 1404-1412 ◽  
Author(s):  
Weikang Ma ◽  
Kyoung Hwan Lee ◽  
Shixin Yang ◽  
Thomas C. Irving ◽  
Roger Craig
Keyword(s):  
Skeletal Muscle ◽  
Fiber Type ◽  
Hexagonal Lattice ◽  
Thick Filament ◽  
Fiber Types ◽  
X Ray Diffraction ◽  
X Ray ◽  
Lattice Disorder ◽  
Simple Lattice ◽  
Lattice Arrangement

The thick (myosin-containing) filaments of vertebrate skeletal muscle are arranged in a hexagonal lattice, interleaved with an array of thin (actin-containing) filaments with which they interact to produce contraction. X-ray diffraction and EM have shown that there are two types of thick filament lattice. In the simple lattice, all filaments have the same orientation about their long axis, while in the superlattice, nearest neighbors have rotations differing by 0° or 60°. Tetrapods (amphibians, reptiles, birds, and mammals) typically have only a superlattice, while the simple lattice is confined to fish. We have performed x-ray diffraction and electron microscopy of the soleus (SOL) and extensor digitorum longus (EDL) muscles of the rat and found that while the EDL has a superlattice as expected, the SOL has a simple lattice. The EDL and SOL of the rat are unusual in being essentially pure fast and slow muscles, respectively. The mixed fiber content of most tetrapod muscles and/or lattice disorder may explain why the simple lattice has not been apparent in these vertebrates before. This is supported by only weak simple lattice diffraction in the x-ray pattern of mouse SOL, which has a greater mix of fiber types than rat SOL. We conclude that the simple lattice might be common in tetrapods. The correlation between fiber type and filament lattice arrangement suggests that the lattice arrangement may contribute to the functional properties of a muscle.

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