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.
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Holmes, K.C. (1972). Molecular Structure of the Actomyosin System in Cross-striated Muscle. In: Weber, H.H. (eds) Molecular Bioenergetics and Macromolecular Biochemistry. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-65309-4_11
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DOI: https://doi.org/10.1007/978-3-642-65309-4_11
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