The secondary structures of oligomeric organic molecules are known to reveal fascinating
architectures that can be responsible for their aesthetic beauty as well as their biological …

Interest in unnatural oligomers (“foldamers”) with discrete conformational propensities akin
to those of proteins has led to numerous recent explorations of peptides constructed from-, γ …

α, γ-and β, γ-hybrid peptides, which are composed of two different homologous amino acid
constituents in alternate order, are suggested as novel classes of peptide foldamers. On the …

The de novo design of peptides and proteins has provided an approach to critically assess
the features that are responsible for the folding and function of proteins. 1 Recent successes …

Biological systems rely on peptides and proteins for a wide variety of functions, but
designing new activities into short, linear R-amino acid oligomers is difficult because of high …

Oligomers that contain both α-and β-amino acid residues in a 1: 1 alternating pattern have
recently been shown by several groups to adopt helical secondary structures in solution …

Naturally occurring peptides and proteins are polymers of R-amino acids. The kind and
grouping of R-amino acid side chains determine protein secondary structures such as R …

Hybrid oligomeric sequences derived from both aliphatic and aromatic units are shown to
adopt a folded conformation with an unprecedented architecture. Specifically, a δ-amino …

The β-turn represents a particularly favorable way for R-amino acid backbones to reverse
direction, as required for compact folding of proteins. 1, 2 Identification of unnatural polymer …

We report the first high-resolution structural data for the β/γ-peptide 13-helix (i, i+ 3 C O···
H N H-bonds), a secondary structure that is formed by oligomers with a 1: 1 alternation of β …