The encoded biosynthesis of proteins provides the ultimate paradigm for high-fidelity
synthesis of long polymers of defined sequence and composition, but it is limited to …

Over the past 16 years, genetic code expansion and reprogramming in living organisms has
been transformed by advances that leverage the unique properties of pyrrolysyl-tRNA …

Directed evolution of orthogonal aminoacyl-tRNA synthetases (AARSs) enables site-specific
installation of noncanonical amino acids (ncAAs) into proteins. Traditional evolution …

The absence of orthogonal aminoacyl-transfer RNA (tRNA) synthetases that accept non-l-α-
amino acids is a primary bottleneck hindering the in vivo translation of sequence-defined …

Expanding and reprogramming the genetic code of cells for the incorporation of multiple
distinct non-canonical amino acids (ncAAs), and the encoded biosynthesis of non-canonical …

Genetically encoding distinct non-canonical amino acids (ncAAs) into proteins synthesized
in cells requires mutually orthogonal aminoacyl-tRNA synthetase (aaRS)/tRNA pairs. The …

Virtually all natural proteins are built from only 20 amino acids, and while this makes
possible all the functions they perform, the ability to encode other amino acids selected for …

Abstract Pyrrolysine (Pyl), the 22nd natural amino acid, is genetically encoded by UAG and
inserted into proteins by the unique suppressor tRNAPyl (ref.). The Methanosarcinaceae …

Pyrrolysyl-tRNA synthetase (PylRS) is a major tool in genetic code expansion using
noncanonical amino acids, yet its structure and function are not completely understood …

Protein translation is orchestrated through tRNA aminoacylation and ribosomal elongation.
Among the highly conserved structure of tRNAs, they have distinguishing features which …