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  High protein mobility in skinned rabbit muscle fibres observed by 1H NMR spectroscopy

Kalbitzer, H. R., Schrumpf, M., & Wray, J. (1992). High protein mobility in skinned rabbit muscle fibres observed by 1H NMR spectroscopy. FEBS Letters, 298(2), 226-228. doi:10.1016/0014-5793(92)80063-M.

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FEBSLett_298_1992_226.pdf (Any fulltext), 244KB
 
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 Creators:
Kalbitzer, Hans Robert1, Author           
Schrumpf, Matthias1, Author           
Wray, John1, 2, Author           
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1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: Muscle; Myosin; NMR; Skinned fibres; Mobility
 Abstract: 1H NMR spectra of skinned rabbit muscle fibers show a group of relatively sharp resonance lines which presumably originate from highly mobile protein domains. Comparison with the spectrum of myosin subfragment 1 suggests that these signals may come at least partly from mobile regions of the myosin head. NMR could possibly be used to characterize the movements of crossbridges in force generation.

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Language(s): eng - English
 Dates: 1991-12-091992-01-081992-02-24
 Publication Status: Issued
 Pages: 3
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 Rev. Type: Peer
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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 298 (2) Sequence Number: - Start / End Page: 226 - 228 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501