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Related Experiment Videos

Changes in the X-ray diffraction pattern from rigor muscles by application of external length changes.

H Tanaka1, K Wakabayashi, Y Amemiya

  • 1Department of Physiology, School of Medicine, Teikyo University, Tokyo, Japan.

Advances in Biophysics
|January 1, 1991
PubMed
Summary

External force alters X-ray patterns in frog muscles during rigor. Applying sinusoidal length changes specifically affected the 14.3 nm reflection, indicating myosin

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Area of Science:

  • Muscle physiology
  • Biophysics
  • X-ray diffraction

Background:

  • Understanding muscle contraction mechanisms requires analyzing structural changes during force generation.
  • X-ray diffraction provides insights into the arrangement of muscle filaments.
  • Previous studies have explored muscle mechanics, but the precise structural basis of force transmission remains debated.

Purpose of the Study:

  • To investigate the effect of external force on the X-ray diffraction pattern of frog muscles in rigor.
  • To identify which structural components within the muscle are responsible for observed changes during length oscillations.

Main Methods:

  • Time-resolved X-ray diffraction technique applied to frog muscles.
  • Sinusoidal length changes (1.5-3% of muscle length at 5 Hz) were imposed on rigor and relaxed muscles.

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  • Analysis of intensity changes in specific X-ray reflections (14.3 nm, 5.9 nm, 5.1 nm, and equatorial reflections).

    • Main Results:

    • The 14.3 nm reflection intensity decreased during muscle release and increased during stretching in rigor muscles.
    • No significant changes were observed in other reflections (5.9 nm, 5.1 nm, equatorial) or in relaxed muscles.
    • The 14.3 nm intensity change was suppressed when muscles were stretched beyond filament overlap and showed a delay related to tension changes.

    Conclusions:

    • The 14.3 nm intensity change is dependent on rigor crossbridges, suggesting their involvement in force transmission.
    • Large conformational changes in the distal myosin head or actin filament are unlikely.
    • The proximal portion of myosin heads, including S-2, likely contributes to the observed intensity changes, with potential involvement of other structures.