Site-specific labeling of proteins with NMR-active unnatural amino acids |
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Authors: | David H Jones Susan E Cellitti Xueshi Hao Qiong Zhang Michael Jahnz Daniel Summerer Peter G Schultz Tetsuo Uno Bernhard H Geierstanger |
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Institution: | (1) Genomics Institute of the Novartis Research Foundation, 10675 John Jay Hopkins Drive, San Diego, CA 92121-1125, USA;(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; |
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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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