BIOL 49 |
| Proline residues, or non-canonical imino acid analogues can have a critical effect on the structural and functional properties of proteins. We have developed a system for the multiple site-specific incorporation of proline analogues into elastin-mimetic polypeptides using a genetic engineering approach. The inherent codon bias observed for an Escherichia coli bacterial cell host can be exploited to create an orthogonal prolyl-tRNA synthetase/prolyl-tRNA pair that decodes the rarely utilized proline CCC codon. The ProRS/tRNAPro pair from M. jannaschii was shown to be orthogonal to the native E. coli translational machinery. This pair could be used to capture the rarely used CCC codon, which was introduced at positions encoding proline residues in a synthetic elastin-mimetic protein. We hypothesize that this in vivo approach might be employed to control protein structure through the site-specific incorporation of imino acid analogues, which would enable the creation of novel protein-based materials. |
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Protein Structure and Folding
4:30 PM-6:30 PM, Sunday, 10 September 2006 Moscone Center -- Hall D, Poster
Sci-Mix
Division of Biological Chemistry |