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Related Experiment Videos

The myosin molecule--charge response to nucleotide binding

E M Bartels1, P H Cooke, G F Elliott

  • 1Biophysics Group, Open University Oxford Research Unit, Boars Hill, UK.

Biochimica Et Biophysica Acta
|May 7, 1993
PubMed
Summary

Adenosine triphosphate (ATP) initiates a decrease in muscle A-band net electric charge, localized to myosin, not light meromyosin. This charge reduction is linked to ligand interactions with myosin sites.

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Area of Science:

  • Muscle physiology
  • Biochemistry
  • Protein electrostatics

Background:

  • Muscle contraction involves changes in electric charge.
  • Previous work observed charge decrease in muscle A-bands during relaxation.

Purpose of the Study:

  • To pinpoint the source of charge decrease in muscle A-bands.
  • To investigate the role of adenosine triphosphate (ATP) in charge dynamics.

Main Methods:

  • Studied net charge on myosin, myosin rod, and light meromyosin (LMM) gels with varying ATP concentrations.
  • Examined muscle A-bands under identical ATP variations.
  • Compared effects of ATP, pyrophosphate (PPi), and adenosine diphosphate (ADP).

Main Results:

Related Experiment Videos

  • A small amount of ATP (100-200 microns) triggers the charge decrease.
  • ATP affects muscle A-bands, myosin, and myosin rod gels, but not LMM gels.
  • PPi mimics ATP's charge effect, while ADP does not.

    • Conclusions:

    • ATP-induced charge decrease originates from myosin.
    • The effect is due to ligand interaction at specific myosin sites.
    • This interaction alters protein charge, possibly by affecting anion or cation absorption.