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Peptides as Probes in Muscle Research pp 15–31Cite as

Interaction of Actin 1–28 with Myosin and Troponin I and the Importance of These Interactions to Muscle Regulation

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Abstract

Muscle contraction involves the regulation of the interaction between actin and myosin (acto-myosin) by the regulatory protein complex, troponin-tropomyosin (Tn-TM). The troponin (Tn) subunits (TnC, TnI, TnT) interact with each other and work in concert with actin-TM to produce conformational changes which alter the acto-myosin interaction. When F-actin binds the myosin head, activation of the ATP hydrolysis rate occurs causing an increase in the release of Pi, thereby increasing the rate of cross-bridge cycling.

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Authors and Affiliations

  1. Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada, T6G 2H7

    J. E. Van Eyk, F. D. Sönnichsen, B. D. Sykes & R. S. Hodges

Authors
  1. J. E. Van Eyk
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  2. F. D. Sönnichsen
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  3. B. D. Sykes
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  4. R. S. Hodges
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Editor information

Editors and Affiliations

  1. Department of Physiology II, University of Heidelberg, Im Neuenheimer Feld 326, 6900, Heidelberg, Germany

    Johann Caspar Rüegg

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© 1991 Springer-Verlag Berlin Heidelberg

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Van Eyk, J.E., Sönnichsen, F.D., Sykes, B.D., Hodges, R.S. (1991). Interaction of Actin 1–28 with Myosin and Troponin I and the Importance of These Interactions to Muscle Regulation. In: Rüegg, J.C. (eds) Peptides as Probes in Muscle Research. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76409-7_3

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  • DOI: https://doi.org/10.1007/978-3-642-76409-7_3

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-76411-0

  • Online ISBN: 978-3-642-76409-7

  • eBook Packages: Springer Book Archive

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