The ribosome is an ancient molecular fossil that provides a telescope to the origins of life.
Made from RNA and protein, the ribosome translates mRNA to coded protein in all living …

Genetic code reprogramming has enabled us to ribosomally incorporate various
nonproteinogenic amino acids (npAAs) into peptides in vitro. The repertoire of usable npAAs …

Peptides that contain β-amino acids display stable secondary structures, such as helices
and sheets, and are often referred to as foldamers. Cyclic β2, 3-amino acids (cβAAs), such …

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

The compatibility of β-amino acids with ribosomal translation was studied for decades, but it
has been still unclear whether the ribosome can accept various β-amino acids, and whether …

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 …

Due to their unique characteristics, which are not shared by canonical α-peptides, peptides
that contain stretches of consecutive β-amino acids are attractive scaffolds for novel peptide …

More than two decades ago a general method to genetically encode noncanonical or
unnatural amino acids (NAAs) with diverse physical, chemical, or biological properties in …

Synthesis of proteins with non-canonical amino acids via genetic code expansion is at the
forefront of synthetic biology. Progress in this field has enabled site-specific incorporation of …

Current textbook knowledge holds that the structural scope of ribosomal biosynthesis is
based exclusively on α-amino acid backbone topology. Here we report the genome-guided …