Nuclear magnetic resonance (NMR) methods are widely used to determine the three-dimensional structures of proteins, to estimate protein folding, and to discover high-affinity ligands for proteins. However, one of the problems to apply such NMR methods to proteins is that we should obtain mg quantities of (15)N and/or (13)C labeled pure proteins of interest. Here, we describe the method to produce dual amino acid-selective (13)C-(15)N labeled proteins for NMR study using the improved wheat germ cell-free system, which enables sequence-specific assignments of amide signals simply even for very large protein.
CITATION STYLE
Kohno, T. (2010). NMR assignment method for amide signals with cell-free protein synthesis system. Methods in Molecular Biology (Clifton, N.J.), 607, 113–126. https://doi.org/10.1007/978-1-60327-331-2_11
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