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Heliyon
2020 Oct 01;610:e05140. doi: 10.1016/j.heliyon.2020.e05140.
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A rationally designed orthogonal synthetase for genetically encoded fluorescent amino acids.
Steinberg X
,
Galpin J
,
Nasir G
,
Sepúlveda RV
,
Ladron de Guevara E
,
Gonzalez-Nilo F
,
Islas LD
,
Ahern CA
,
Brauchi SE
.
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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.
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