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  Identification of the transitory complex myosin-ATP by the use of α,β-methylene-ATP

Mannherz, H. G., Barrington Leigh, J., Holmes, K. C., & Rosenbaum, G. (1973). Identification of the transitory complex myosin-ATP by the use of α,β-methylene-ATP. Nature, 241, 226-229. doi:10.1038/newbio241226a0.

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 Creators:
Mannherz, Hans Georg1, Author           
Barrington Leigh, J.2, Author           
Holmes, Kenneth C.3, Author           
Rosenbaum, G.2, Author           
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1Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753289              
2Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              
3Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: FROM structural studies on glycerinated Lethocerus flight muscle Ready, Holmes and Tregear1 showed that the cross-bridges of insect flight muscle take on recognizably different configurations in the presence and absence of ATP. In the presence of excess ATP (relaxed) the bridges are approximately at right-angles to the myosin thick filament and in its absence (rigor state, with formation of the actomyosin complex) they make a chevron-like structure by binding at an angle of about 45° to the actin filaments. Coupled with studies on living frog muscle2 this led to proposals by Huxley3 and Pringle4 that the cross-bridges move the actin filament past the myosin filament by a kind of rowing action; a model which has been generally accepted as a working hypothesis.

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Language(s): eng - English
 Dates: 1972-05-191972-10-021973-02-21
 Publication Status: Published in print
 Pages: 4
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/newbio241226a0
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Title: Nature
  Abbreviation : Nature
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 241 Sequence Number: - Start / End Page: 226 - 229 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238