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Book Chapter

Molecular structure of the actomyosin system in cross-striated muscle

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Holmes,  Kenneth C.
Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Muscle Research, Max Planck Institute for Medical Research, Max Planck Society;

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https://link.springer.com/content/pdf/10.1007%2F978-3-642-65309-4_11.pdf
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https://doi.org/10.1007/978-3-642-65309-4_11
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Citation

Holmes, K. C. (1972). Molecular structure of the actomyosin system in cross-striated muscle. In H. H. Weber (Ed.), Molecular Bioenergetics and Macromolecular Biochemistry (pp. 90-110). Heidelberg / Berlin: Springer.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-B19D-E
Abstract
The present dogma of muscle contraction is founded principally on two tenets: (1) that contraction is the result of an interaction between actin, myosin and adenosine triphosphate (ATP), and (2) that contraction proceeds by a sliding mechanism which does not involve permanent change in the length or configuration of the component protein molecules. Actomyosin is an ATPase needing Mg++ ion as a co-factor but not Ca++ ion. The Ca++ concentration on the other hand plays a vital role in switching the muscle from a resting to an active state. I wish to acknowledge at the outset the debt we owe to Dr. H. E. Huxley for his unique role in the development of the structural ideas underlying this hypothesis.