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

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Kalbitzer,  Hans Robert
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Schrumpf,  Matthias
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Wray,  John
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

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.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-AB9E-7
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.