500 MHz 1 H-NMR study of the N-terminal N -trimethylalanine residue of LC-1 and LC-2 light chains m rabbit fast skeletal myosin solutions
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(84)81125-4/fullpdf
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1. Muscle Contraction
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4. The Amino-Acid Sequence of the Alkali Light Chains of Rabbit Skeletal-Muscle Myosin
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1. Muscle Proteins;Encyclopedia of Magnetic Resonance;2007-03-15
2. The proteolytic susceptibility of specific sites in myosin light chains is modulated by the filament conformation;European Journal of Biochemistry;1993-08
3. Refined conditions for selective modifications of rabbit skeletal myosin light chains;Biochimie;1992-12
4. Probing myosin light chain 1 structure with monoclonal antibodies;Journal of Muscle Research & Cell Motility;1992-06
5. High protein mobility in skinned rabbit muscle fibres observed by 1 H NMR spectroscopy;FEBS Letters;1992-02-24
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