Fig. 3: tRNA-binding domain mutations generally improved the incorporation efficiency of various ncAAs. | Nature Communications

Fig. 3: tRNA-binding domain mutations generally improved the incorporation efficiency of various ncAAs.

From: Machine learning-guided evolution of pyrrolysyl-tRNA synthetase for improved incorporation efficiency of diverse noncanonical amino acids

Fig. 3

a The SCS activity of IFRS, Com1-IFRS, and Com2-IFRS toward various substrates. b The SCS activity of combinatorial variants against various ncAAs. Light purple, absence of ncAAs in growth medium; Dark purple, presence of ncAAs in growth medium. Error bars represent ±standard deviation of the mean over 4 independent replicates. NcAAs include 3-fluoro-L-phenylalanine (3FF), 2,3-difluoro-L-phenylalanine (23FF), 2,4-difluoro-L-phenylalanine (24FF), 2,5-difluoro-L-phenylalanine (25FF), 3,4,5-trifluoro-L-phenylalanine (345FF), 2,3,6-trifluoro-L-phenylalanine (236FF), 2,3,4,5,6-pentafluoro-L-phenylalanine (PFF), 5-bromo-2-chloro-L-phenylalanine (5Br2ClF), 2-chloro-L-phenylalanine (2ClF), 3,4-dichloro-L-phenylalanine (34ClF), 3-(2-thienyl)-L-alanine (2ThiA), 2-(5-bromothienyl)-L-alanine (BrThiA), N6-(tert-butoxycarbonyl)-L-lysine (BocK), N6-((allyloxy)carbonyl)-L-lysine (AlocK), N-epsilon-Acetyl-L-lysine (AcK), 3-L-phenyllactic acid (PLA), 3-bromo-L-tyrosine (3BrY), 3-chloro-L-tyrosine (3ClY), 3-iodo-L-tyrosine (3IY), 3-benzothienyl-L-alanine (Bta), 3-(1-naphthyl)-L-alanine (1NaA), S-allyl-L-cysteine (Sac), 3-methyl-L-histidine (3MeH). Source data are provided as a Source Data file.

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