Dieter G. Söll

This study examines how E. coli's genetic code tolerates tRNA mutations that increase codon size, finding that while many tRNAs can be converted to quadruplet tRNAs, only nine aminoacyl tRNA synthetases tolerate quadruplet anticodons, limiting the chemical alphabet of a synthetic quadruplet code.

The paper demonstrates a triply orthogonal system that reassigns three stop codons to encode three distinct noncanonical amino acids in proteins.

This paper introduces a method called Post-Translational Proofreading (PTP) to improve the accuracy of detecting non-standard amino acid incorporation into proteins by leveraging the N-end rule pathway.

The paper replaces rare arginine codons in E. coli with synonymous alternatives, identifying rules for codon choice based on mRNA structure and ribosomal binding motifs.