【摘 要】
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Dear Editor,Among many of biophysical methods,19F NMR spectroscopy has emerged as a powerful tool for characterizing protein structure,dynamics and function pro
【机 构】
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Hefei National Laboratory for Physical Science at the Microscale School of Life Science, University
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Dear Editor,Among many of biophysical methods,19F NMR spectroscopy has emerged as a powerful tool for characterizing protein structure,dynamics and function properties due to high intrinsic sensitivities of fluorine,100％ natural abundance of the NMR-active spin,the absence of any natural background in cells,and exquisite sensitivities of 19F chemical shift to environment (Shi et al.,2011;Shi et al.,2010).With evolved aminoacyl-tRNA synthase specifically recognizing the 19F containing unnatural amino acids,and suppressed amber stop codon by tRNAcuA,several 19F containing unnatural amino acids were incorporated into proteins in bacteria (Hammill et al.,2007;Jackson et al.,2007).Achievements of the protein-specific and site-specific 19F incorporation provided great opportunities for in cell or in situ protein structure,dynamic and function studies.
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