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Related Experiment Videos

Calcium-dependent structural changes in scallop heavy meromyosin.

W F Stafford1, M P Jacobsen, J Woodhead

  • 1Boston Biomedical Research Institute, Watertown, MA 02472, USA.

Journal of Molecular Biology
|March 13, 2001
PubMed
Summary
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Calcium binding causes scallop myosin heads to separate, increasing muscle contraction. This study reveals how calcium regulation works in scallop heavy meromyosin (HMM) by examining head interactions.

Area of Science:

  • Muscle contraction
  • Biochemistry
  • Molecular biology

Background:

  • Scallop myosin head interaction and calcium regulation are not fully understood.
  • Both myosin heads are known to be essential for muscle contraction.

Purpose of the Study:

  • To investigate the interaction between heavy meromyosin (HMM) heads in scallop myosin.
  • To elucidate the role of calcium and nucleotides in regulating HMM structure and activity.

Main Methods:

  • Sedimentation velocity studies to assess molecular asymmetry.
  • Electron microscopy of crosslinked, rotary shadowed specimens.
  • Biochemical assays to measure ATPase activity.

Main Results:

  • Calcium binding significantly increased HMM ATPase activity.

Related Experiment Videos

  • Calcium induced a conformational change in HMM, increasing molecular asymmetry in the presence of nucleotides.
  • Electron microscopy showed that in the absence of calcium, HMM heads associate, forming a rigid structure, while calcium binding promotes head separation.

    • Conclusions:

    • Scallop myosin heads interact in an "off" state, reducing ATPase activity.
    • Calcium binding to scallop myosin "switches on" the molecule by causing head separation, facilitating actin interaction and muscle contraction.