Abstract
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 15N and/or 13C labeled pure proteins of interest.
Here, we describe the method to produce dual amino acid-selective 13C–15N 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.
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Kohno, T. (2010). NMR Assignment Method for Amide Signals with Cell-Free Protein Synthesis System. In: Endo, Y., Takai, K., Ueda, T. (eds) Cell-Free Protein Production. Methods in Molecular Biology, vol 607. Humana Press. https://doi.org/10.1007/978-1-60327-331-2_11
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DOI: https://doi.org/10.1007/978-1-60327-331-2_11
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