Abstract
Designer amino acids, beyond the canonical 20 that are normally used by cells, can now be site-specifically encoded into proteins in cells and organisms. This is achieved using 'orthogonal' aminoacyl-tRNA synthetase-tRNA pairs that direct amino acid incorporation in response to an amber stop codon (UAG) placed in a gene of interest. Using this approach, it is now possible to study biology in vitro and in vivo with an increased level of molecular precision. This has allowed new biological insights into protein conformational changes, protein interactions, elementary processes in signal transduction and the role of post-translational modifications.
Original language | English |
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Pages (from-to) | 168-82 |
Number of pages | 15 |
Journal | Nature reviews Molecular cell biology |
Volume | 13 |
Issue number | 3 |
DOIs | |
Publication status | Published - Mar 2012 |
Keywords / Materials (for Non-textual outputs)
- Animals
- Genetic Code
- Humans
- Models, Molecular
- Protein Binding
- Protein Conformation
- Protein Engineering
- Protein Interaction Mapping
- Protein Processing, Post-Translational
- Recombinant Proteins
- Signal Transduction