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Journal of Muscle Research & Cell Motility

, Volume 6, Issue 1, pp 43–52 | Cite as

Angle of active site of myosin heads in contracting muscle during sudden length changes

  • Toshio Yanagida
Papers

Summary

The change in orientation of myosin crossbridges in contracting muscle during sudden length changes was examined by fluorescence polarization. This study used a fluorescent ATP analogue, 1,N6-etheno-2-aza-ATP(ε-2-aza-ATP) as a probe. Its fluorescence is considerably enhanced upon binding with myosin and is dependent on the chemical state of the myosin-nucleotide complex in muscle. The results showed that nucleotides bound to crossbridges in the intermediate attached state (presumably AM-ε-2-aza-ADP-Pi) during isometric contraction are highly oriented at the same angle as that of AM in rigor with bound ε-2-aza-ADP. Furthermore the orientation of nucleotides bound to crossbridges in the attached state is not altered during sudden changes in length of isometrically contracting muscle. The results of this time-resolved measurement support the conclusion obtained from a previous steady-state experiment that change in axial orientation of the active site of the myosin head is not involved in force generation.

Keywords

Nucleotide Chemical State Sudden Change Force Generation Isometric Contraction 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Chapman and Hall Ltd 1985

Authors and Affiliations

  • Toshio Yanagida
    • 1
  1. 1.Department of Biophysical Engineering, Faculty of Engineering ScienceOsaka UniversityToyonaka, OsakaJapan

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