A rationally designed orthogonal synthetase for genetically encoded fluorescent amino acids
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Fecha
2020-10
Profesor/a Guía
Facultad/escuela
Idioma
en
Título de la revista
ISSN de la revista
Título del volumen
Editor
Elsevier Ltd
Nombre de Curso
Licencia CC
Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
Licencia CC
https://creativecommons.org/licenses/by-nc-nd/4.0/
Resumen
The incorporation of non-canonical amino acids into proteins has emerged as a promising strategy to manipulate and study protein structure-function relationships with superior precision in vitro and in vivo. To date, fluorescent non-canonical amino acids (f-ncAA) have been successfully incorporated in proteins expressed in bacterial systems, Xenopus oocytes, and HEK-293T cells. Here, we describe the rational generation of a novel orthogonal aminoacyl-tRNA synthetase based on the E. coli tyrosine synthetase that is capable of encoding the f-ncAA tyr-coumarin in HEK-293T cells. © 2020Bioorganic Chemistry; Bioinformatics; Proteins; Biochemistry; Molecular Biology; Unnatural amino acids, aminoacyl-tRNA synthetase, coumarin, fluorescence. © 2020
Notas
Indexación: Scopus.
Palabras clave
Aminoacyl-tRNA synthetase, Biochemistry, Bioinformatics, Bioorganic chemistry, Coumarin, Fluorescence, Molecular biology, Proteins, Unnatural amino acids
Citación
HeliyonOpen AccessVolume 6, Issue 10October 2020 Article number e05140
DOI
10.1016/j.heliyon.2020.e05140