A genetically encoded fluorescent amino acid Export

@article{citeulike:5663824, abstract = {10.1073/pnas.0603965103 The ability to introduce fluorophores selectively into proteins provides a powerful tool to study protein structure, dynamics, localization, and biomolecular interactions both and . Here, we report a strategy for the selective and efficient biosynthetic incorporation of a low-molecular-weight fluorophore into proteins at defined sites. The fluorescent amino acid 2-amino-3-(5-(dimethylamino)naphthalene-1-sulfonamide)propanoic acid (dansylalanine) was genetically encoded in by using an amber nonsense codon and corresponding orthogonal tRNA/aminoacyl-tRNA synthetase pair. This environmentally sensitive fluorophore was selectively introduced into human superoxide dismutase and used to monitor unfolding of the protein in the presence of guanidinium chloride. The strategy described here should be applicable to a number of different fluorophores in both prokaryotic and eukaryotic organisms, and it should facilitate both biochemical and cellular studies of protein structure and function.}, author = {Summerer, Daniel and Chen, Shuo and Wu, Ning and Deiters, Alexander and Chin, Jason W. and Schultz, Peter G.}, citeulike-article-id = {5663824}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0603965103}, citeulike-linkout-1 = {http://www.pnas.org/content/103/26/9785.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/103/26/9785.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/16785423}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=16785423}, day = {27}, doi = {10.1073/pnas.0603965103}, journal = {Proceedings of the National Academy of Sciences}, keywords = {acid, amino, encoded, fluorescence, fluorescent, genetically}, month = {June}, number = {26}, pages = {9785--9789}, posted-at = {2009-08-28 17:45:45}, priority = {2}, title = {A genetically encoded fluorescent amino acid}, url = {http://dx.doi.org/10.1073/pnas.0603965103}, volume = {103}, year = {2006} }

TY - JOUR ID - citeulike:5663824 L3 - citeulike-article-id:5663824 N2 - 10.1073/pnas.0603965103 The ability to introduce fluorophores selectively into proteins provides a powerful tool to study protein structure, dynamics, localization, and biomolecular interactions both and . Here, we report a strategy for the selective and efficient biosynthetic incorporation of a low-molecular-weight fluorophore into proteins at defined sites. The fluorescent amino acid 2-amino-3-(5-(dimethylamino)naphthalene-1-sulfonamide)propanoic acid (dansylalanine) was genetically encoded in by using an amber nonsense codon and corresponding orthogonal tRNA/aminoacyl-tRNA synthetase pair. This environmentally sensitive fluorophore was selectively introduced into human superoxide dismutase and used to monitor unfolding of the protein in the presence of guanidinium chloride. The strategy described here should be applicable to a number of different fluorophores in both prokaryotic and eukaryotic organisms, and it should facilitate both biochemical and cellular studies of protein structure and function. IS - 26 JF - Proceedings of the National Academy of Sciences EP - 9789 TI - A genetically encoded fluorescent amino acid VL - 103 SP - 9785 KW - acid KW - amino KW - encoded KW - fluorescence KW - fluorescent KW - genetically AU - Summerer, Daniel AU - Chen, Shuo AU - Wu, Ning AU - Deiters, Alexander AU - Chin, Jason AU - Schultz, Peter PY - 2006/06/27/ UR - http://dx.doi.org/10.1073/pnas.0603965103 ER -