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• W2065379121 abstract "It has previously been demonstrated that the unnatural amino acid p-Cl-phenylalanine can be attached to tRNA(Phe) by a modified phenylalanyl-tRNA synthetase with relaxed amino acid substrate specificity. We show that this modification to the translational machinery of Escherichia coli is the only requirement for the incorporation of either p-Cl- or p-Br-phenylalanine into full-length luciferase in vitro. The incorporation of p-Cl-phenylalanine was also demonstrated in vivo using a suitably modified host strain. These results represent the first description of the incorporation into a protein in vivo of an unnatural amino acid which is normally rejected by the cellular translational machinery." @default.
• W2065379121 created "2016-06-24" @default.
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• W2065379121 date "1995-05-15" @default.
• W2065379121 modified "2023-10-14" @default.
• W2065379121 title "Relaxing the substrate specificity of an aminoacyl‐tRNA synthetase allows in vitro and in vivo synthesis of proteins containing unnatural amino acids" @default.
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• W2065379121 doi "https://doi.org/10.1016/0014-5793(95)00408-2" @default.
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