ANYL 153 |
| Red fluorescent protein (DsRed) has become a popular fusion tag in biochemical studies. It is better suited for cellular and tissue studies, compared to GFP, because of its excitation and emission in the red region of the spectrum, high quantum yield, and tissue translucency. Several genetic modifications have been performed on this protein to overcome drawbacks such as obligate oligomerization and slow fluorescence maturation. In addition to this traditional way of preparing protein variants, non-natural amino acids can also be incorporated into proteins, imparting unprecedented properties. The effect of non-natural amino acid incorporation on the structure and properties of DsRed will be presented here. Specifically, properties of DsRed variants with incorporated non-natural amino acids 3-fluoro-L-tyrosine and 3-amino-L-tyrosine will be evaluated. A strategy of forced biochemical incorporation of non-natural amino acids will be utilized to create the variants. The non-natural analogues of the amino acid tyrosine are incorporated because tyrosine is involved in chromophore formation. |
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General Papers
7:00 PM-9:00 PM, Sunday, 10 September 2006 Moscone Center -- Hall D, Poster
Division of Analytical Chemistry |