Abstract
Nuclear magnetic resonance (NMR) methods have been developed to determine the three-dimensional structures of proteins, to estimate protein folding, and to discover high-affinity ligands for proteins. However, one of the difficulties encountered in the application of such NMR methods to proteins is that we should obtain milligram quantities of 15N and/or 13C-labeled pure proteins of interest. Here, we describe the method to produce proteins for NMR experiments using the improved wheat germ cell-free system, which exhibits several attractive features for high-throughput NMR study of proteins.
Cite
CITATION STYLE
Kohno, T., & Endo, Y. (2007). Production of Protein for Nuclear Magnetic Resonance Study Using the Wheat Germ Cell-Free System. In In Vitro Transcription and Translation Protocols (pp. 257–272). Humana Press. https://doi.org/10.1007/978-1-59745-388-2_13
Register to see more suggestions
Mendeley helps you to discover research relevant for your work.
