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 …

Since the establishment of site-specific mutagenesis of single amino acids to interrogate
protein function in the 1970s, biochemists have sought to tailor protein structure in the native …

It is widely hypothesized that removing cellular transfer RNAs (tRNAs)—making their
cognate codons unreadable—might create a genetic firewall to viral infection and enable …

The genetic code of living cells has been reprogrammed to enable the site-specific
incorporation of hundreds of non-canonical amino acids into proteins, and the encoded …

The direct genetically encoded cell-based synthesis of non-natural peptide and
depsipeptide macrocycles is an outstanding challenge. Here we programme the encoded …

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 …

Orthogonal (O) ribosome-mediated translation of O-mRNAs enables the incorporation of up
to three distinct non-canonical amino acids (ncAAs) into proteins in Escherichia coli (E. coli) …

Ribosome-mediated polymerization of backbone-extended monomers into polypeptides is
challenging due to their poor compatibility with the translation apparatus, which evolved to …

A central challenge in expanding the genetic code of cells to incorporate noncanonical
amino acids into proteins is the scalable discovery of aminoacyl-tRNA synthetase (aaRS) …

The site-specific incorporation of noncanonical monomers into polypeptides through genetic
code reprogramming permits synthesis of bio-based products that extend beyond natural …