The breadth of structure and function displayed by the molecules of biology is remarkable.
Considering that there are only three major biopolymer backbones (proteins, ribonucleic …

In recent years, our understanding of protein structure and function has advanced rapidly,
providing a mechanistic understanding of a wide variety of biological processes. As an …

The origins of our nearly ten‐year research program of chemical and biological
investigations into peptides based on homologated proteinogenic amino acids are …

The remarkable complexity of globular protein structures was first revealed about half a
century ago, when the crystal structure of myoglobin was determined at 2.4 Å. 1 In the …

The principal secondary structural motifs adopted by peptides assembled from β‐amino acid
units are discussed: the 14‐, 12‐, 10‐, 12/10‐, and 8‐helices, as well as the hairpin turn …

Interplay between proteins, nucleic acids, carbohydrates and/or lipids is involved in almost
every process in life on earth. As a consequence, a wide range of diseases results from …

The field of drug discovery and development has seen tremendous activity over the past
decade to better tackle the increasing occurrence of drug‐resistant bacterial infections and …

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 …

As one of the most important families of non‐natural polymers with the propensity to form
well‐defined secondary structures, the β‐peptides are attracting increasing attention. The …

By using a simple repeating unit method, we have conducted a theoretical study which
delineates the preferences for β-strand, 27-ribbon, 310-helix, and α-helix formation for a …