Issue Date: December 21, 2009
Fluorine NMR Opens A Window Into Cells
With the help of a few 19F labels to boost sensitivity, spectroscopists have used NMR to study the structural and dynamic properties of proteins inside live bacteria (J. Am. Chem. Soc., DOI: 10.1021/ja907966n). In-cell NMR experiments promise better understanding of how proteins function in their native environments, note Gary J. Pielak of the University of North Carolina, Chapel Hill, and coworkers. But such experiments, which almost exclusively rely on 15N labeling, typically require that the cells produce copious quantities of the protein to be studied—and even then the proteins are often not detectable, Pielak says. In addition, protein overexpression could undermine the biological significance of the data. Seeking to sidestep these potential problems, Pielak’s team labeled small 10-kDa proteins with 3-fluorotyrosine and demonstrated in-cell detection with 19F NMR. By incorporating trifluoromethyl-l-phenylalanine, they observed proteins as large as 100 kDa at physiologically relevant cellular concentrations. Notably, they find that the strategy can be used to study both well-structured and intrinsically disordered proteins.
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