Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Heliyon October 1, 2020; 6 (10): e05140.

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 .

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.

PubMed ID: 33083608
Article link: Heliyon

References [+] :
Bae, Expansion of the genetic code enables design of a novel "gold" class of green fluorescent proteins. 2003, Pubmed