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• W4205564102 endingPage "49" @default.
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• W4205564102 abstract "A mutant aminoacyl-tRNA synthetase identified by a library selection system affords site-specific incorporation of 7-fluoro-L-tryptophan in response to an amber stop codon. The enzyme allows the production of proteins with a single hydrogen atom replaced by a fluorine atom as a sensitive nuclear magnetic resonance (NMR) probe. The substitution of a single hydrogen atom by another element that is as closely similar in size and hydrophobicity as possible minimizes possible perturbations in the structure, stability, and solubility of the protein. The fluorine atom enables site-selective monitoring of the protein response to ligand binding by 19F NMR spectroscopy, as demonstrated with the Zika virus NS2B-NS3 protease." @default.
• W4205564102 created "2022-01-25" @default.
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• W4205564102 date "2022-01-10" @default.
• W4205564102 modified "2023-10-14" @default.
• W4205564102 title "Site-Specific Incorporation of 7-Fluoro-<scp>L</scp>-tryptophan into Proteins by Genetic Encoding to Monitor Ligand Binding by ¹⁹F NMR Spectroscopy" @default.
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• W4205564102 doi "https://doi.org/10.1021/acssensors.1c02467" @default.
• W4205564102 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35005899" @default.
• W4205564102 hasPublicationYear "2022" @default.
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