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The myosin filament XIV backbone structure.

F T Ashton1, J Weisel, F A Pepe

  • 1Department of Anatomy, School of Medicine, University of Pennsylvania, Philadelphia 19104-6058.

Biophysical Journal
|June 1, 1992
PubMed
Summary
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Investigating chicken muscle thick filaments revealed threefold symmetry in myosin filaments using electron microscopy. Three distinct arrangements of nine subfilaments were identified, influencing filament structure and orientation.

Area of Science:

  • Muscle physiology
  • Biophysics
  • Electron microscopy

Background:

  • Thick filaments are crucial for muscle contraction, composed primarily of myosin.
  • Understanding the substructure of myosin filaments provides insights into muscle mechanics.

Purpose of the Study:

  • To investigate the substructure of thick filaments in chicken pectoralis muscle.
  • To determine the arrangement and symmetry of myosin subfilaments.

Main Methods:

  • Electron microscopy was used to image transverse sections of chemically skinned chicken pectoralis muscle.
  • Cross-correlation analysis determined the rotational symmetry of myosin filaments.
  • Phase residual tests assessed the resolution of the images.

Main Results:

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  • Myosin filaments exhibited threefold symmetry with a resolution between 3.2 and 3.6 nm.
  • Three distinct arrangements of nine subfilaments were observed, varying in central vs. surface distribution of mass.
  • A transitional arrangement was more frequent at higher ionic strength (200 mM).
  • Subfilaments were generally parallel to the filament axis, with specific rotational orientations observed relative to the hexagonal lattice.

Conclusions:

  • The substructure of chicken muscle thick filaments is complex, with multiple observed arrangements of myosin subfilaments.
  • These arrangements and their orientations likely contribute to the functional properties of muscle contraction.
  • Further research can explore the dynamic nature and functional implications of these substructural variations.