| Autor: |
Jones DH; Genomics Institute of the Novartis Research Foundation, San Diego, CA 92121-1125, USA., Cellitti SE, Hao X, Zhang Q, Jahnz M, Summerer D, Schultz PG, Uno T, Geierstanger BH |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of biomolecular NMR [J Biomol NMR] 2010 Jan; Vol. 46 (1), pp. 89-100. Date of Electronic Publication: 2009 Aug 09. |
| DOI: |
10.1007/s10858-009-9365-4 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
Full text from SpringerLink