Covering: up to June 2020 Ribosomally-synthesized and post-translationally modified
peptides (RiPPs) are a large group of natural products. A community-driven review in 2013 …

Our understanding of the complex molecular processes of living organisms at the molecular
level is growing exponentially. This knowledge, together with a powerful arsenal of tools for …

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 …

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

The development of new orthogonal aminoacyl-tRNA synthetase/tRNA pairs has led to the
addition of approximately 70 unnatural amino acids (UAAs) to the genetic codes of …

Site-specific incorporation of unnatural amino acids (Uaas) in living cells relies on
engineered aminoacyl-transfer RNA synthetase–tRNA pairs borrowed from a distant domain …

Site-specific modification of proteins is a major challenge in modern chemical biology due to
the large number of reactive functional groups typically present in polypeptides. Because of …

The ability to genetically encode unnatural amino acids beyond the common 20 has allowed
unprecedented control over the chemical structures of recombinantly expressed proteins …

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 …

Escherichia coli is a widely used host organism for recombinant technology and the
bacterial incorporation of non-natural amino acids promises the efficient synthesis of …