Examinando por Autor "Brauchi, S.E."

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    A rationally designed orthogonal synthetase for genetically encoded fluorescent amino acids
    (Elsevier Ltd, 2020-10) Steinberg, X.; Galpin, J.; Nasir, G.; Sepulveda, R.V.; Ladron de Guevara, E.; Gonzalez-Nilo, F.; Islas, L.D.; Ahern, C.A.; Brauchi, S.E.
    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