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  Molecular structure of the actomyosin system in cross-striated muscle

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.

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 Creators:
Holmes, Kenneth C.1, 2, 3, Author           
Affiliations:
1Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society, ou_1497735              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
3Muscle Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497731              

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Free keywords: Actin Filament; Flight Muscle; Layer Line; Thick Filament; Myosin Filament
 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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Language(s): eng - English
 Dates: 1972
 Publication Status: Published in print
 Pages: 21
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/978-3-642-65309-4_11
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Title: Molecular Bioenergetics and Macromolecular Biochemistry
Source Genre: Book
 Creator(s):
Weber, H. H., Editor
Affiliations:
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Publ. Info: Heidelberg / Berlin : Springer
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 90 - 110 Identifier: ISBN: 978-3-642-65311-7