Publikation: Site-specific labeling of proteins with NMR-active unnatural amino acids
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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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JONES, David H., Susan E. CELLITTI, Xueshi HAO, Qiong ZHANG, Michael JAHNZ, Daniel SUMMERER, Peter G. SCHULTZ, Tetsuo UNO, Bernhard H. GEIERSTANGER, 2010. Site-specific labeling of proteins with NMR-active unnatural amino acids. In: Journal of Biomolecular NMR. 2010, 46(1), pp. 89-100. ISSN 0925-2738. eISSN 1573-5001. Available under: doi: 10.1007/s10858-009-9365-4BibTex
@article{Jones2010-01Sites-13747, year={2010}, doi={10.1007/s10858-009-9365-4}, title={Site-specific labeling of proteins with NMR-active unnatural amino acids}, number={1}, volume={46}, issn={0925-2738}, journal={Journal of Biomolecular NMR}, pages={89--100}, author={Jones, David H. and Cellitti, Susan E. and Hao, Xueshi and Zhang, Qiong and Jahnz, Michael and Summerer, Daniel and Schultz, Peter G. and Uno, Tetsuo and Geierstanger, Bernhard H.} }
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