Oligomers composed of β3-amino acid residues and a mixture of α-and β3-residues have
emerged as proteolytically stable structural mimics of α-helices. An attractive feature of these
oligomers is that they adopt defined conformations in short sequences. In this manuscript,
we evaluate the impact of β3-residues as compared to their α-amino acid analogs in
prenucleated helices. Our hydrogen–deuterium exchange results suggest that
heterogeneous sequences composed of “αααβ” repeats are conformationally more rigid …