01-09-2011, 12:46 PM
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Site-specific labeling of proteins with NMR-active unnatural amino acids
Site-specific labeling of proteins with NMR-active unnatural amino acids
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. - Content Type Journal Article
- Pages 89-100
- DOI 10.1007/s10858-009-9365-4
- Authors
- David H. Jones, Genomics Institute of the Novartis Research Foundation 10675 John Jay Hopkins Drive San Diego CA 92121-1125 USA
- Susan E. Cellitti, Genomics Institute of the Novartis Research Foundation 10675 John Jay Hopkins Drive San Diego CA 92121-1125 USA
- Xueshi Hao, Genomics Institute of the Novartis Research Foundation 10675 John Jay Hopkins Drive San Diego CA 92121-1125 USA
- Qiong Zhang, Genomics Institute of the Novartis Research Foundation 10675 John Jay Hopkins Drive San Diego CA 92121-1125 USA
- Michael Jahnz, The Scripps Research Institute Department of Chemistry and the Skaggs Institute for Chemical Biology 10550 North Torrey Pines Road La Jolla CA 92037 USA
- Daniel Summerer, The Scripps Research Institute Department of Chemistry and the Skaggs Institute for Chemical Biology 10550 North Torrey Pines Road La Jolla CA 92037 USA
- Peter G. Schultz, Genomics Institute of the Novartis Research Foundation 10675 John Jay Hopkins Drive San Diego CA 92121-1125 USA
- Tetsuo Uno, Genomics Institute of the Novartis Research Foundation 10675 John Jay Hopkins Drive San Diego CA 92121-1125 USA
- Bernhard H. Geierstanger, Genomics Institute of the Novartis Research Foundation 10675 John Jay Hopkins Drive San Diego CA 92121-1125 USA
Source: Journal of Biomolecular NMR
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