Abstract 1528 A mutation to the exit tunnel of the E. coli ribosome improves translation of polyproline sequences with implications for incorporation of cyclic β-amino acids

Incorporation of β-amino acids into peptides imparts proteolytic stability, unique architectures, and membrane permeability as demonstrated by β-amino acid containing natural products. Additionally, cyclic β-amino acids can act as turn inducers, and multiple incorporations can generate foldamers with rigid helical structures. However, incorporation efficiency and number of residues incorporated is highly dependent on the stereochemistry of the cyclic β-amino acid. We sought to improve incorporation of cyclic β-amino acids through structure guided mutations of the E.