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Site-specific labeling of proteins with NMR-active unnatural amino acids

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Abstract

A large number of amino acids other than the canonical amino acids can now be easily incorporated in vivo into proteins at genetically encoded positions. The technology requires an orthogonal tRNA/aminoacyl-tRNA synthetase pair specific for the unnatural amino acid that is added to the media while a TAG amber or frame shift codon specifies the incorporation site in the protein to be studied. These unnatural amino acids can be isotopically labeled and provide unique opportunities for site-specific labeling of proteins for NMR studies. In this perspective, we discuss these opportunities including new photocaged unnatural amino acids, outline usage of metal chelating and spin-labeled unnatural amino acids and expand the approach to in-cell NMR experiments.

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Acknowledgments

We thank Huiyong Hu for the synthesis of 15N-labeled o-NBTyr, and Hyun Soo Lee for samples of HQ-Ala.

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  1. Genomics Institute of the Novartis Research Foundation, 10675 John Jay Hopkins Drive, San Diego, CA, 92121-1125, USA

    David H. Jones, Susan E. Cellitti, Xueshi Hao, Qiong Zhang, Peter G. Schultz, Tetsuo Uno & Bernhard H. Geierstanger

  2. Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA, 92037, USA

    Michael Jahnz, Daniel Summerer & Peter G. Schultz

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  1. David H. Jones
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Jones, D.H., Cellitti, S.E., Hao, X. et al. Site-specific labeling of proteins with NMR-active unnatural amino acids. J Biomol NMR 46, 89–100 (2010). https://doi.org/10.1007/s10858-009-9365-4

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