biostudies-literaturePatgiri ANIGMS NIH HHS11495-502https://www.ebi.ac.uk/biostudies/studies/S-EPMC3399945biostudies-literatureUnknown134(28)Oligomers composed of β(3)-amino acid residues and a mixture of α- and β(3)-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 β(3)-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 than the corresponding homogeneous α-peptide helices, with the macrocycle templating the helical conformation having a significant influence.Journal of the American Chemical SocietyNucleation effects in peptide foldamers.PMC3399945R01 GM073943GM073943Joy STArora PSPatgiri AfalseNucleation effects in peptide foldamers.Oligomers composed of β(3)-amino acid residues and a mixture of α- and β(3)-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 β(3)-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 than the corresponding homogeneous α-peptide helices, with the macrocycle templating the helical conformation having a significant influence.2012-01-01T00:00:00Z2012 Jul2024-11-09T14:39:41.881Z2019-03-27T00:55:43ZS-EPMC33999452271598210.1021/ja301953j