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 …

Nature uses a limited, conservative set of amino acids to synthesize proteins. The ability to
genetically encode an expanded set of building blocks with new chemical and physical …

Oxazole compounds containing nitrogen and oxygen atoms in the five-membered aromatic
ring are readily able to bind with a variety of enzymes and receptors in biological systems …

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

Orthogonal ribosomes are unnatural ribosomes that are directed towards orthogonal
messenger RNAs in Escherichia coli, through an altered version of the 16S ribosomal RNA …

The introduction of noncanonical amino acids into proteins and peptides has been of great
interest for many years and has facilitated the detailed study of peptide/protein structure and …

Exploration of the full potential of thioamide substitution as a tool in the chemical biology of
peptides and proteins has been hampered by insufficient synthetic strategies for the site …

Entire reconstitution of tRNAs for active protein production in a cell-free system brings
flexibility into the genetic code engineering. It can also contribute to the field of cell-free …

Using directed evolution, aminoacyl-tRNA synthetases (aaRSs) have been engineered to
incorporate numerous noncanonical amino acids (ncAAs). Until now, the selection of such …

It has recently been reported that ribosomes from erythromycin-resistant Escherichia coli
strains, when isolated in S30 extracts and incubated with chemically mis-acylated tRNA, can …