The preferred conformations of peptides heavily based on the currently extensively exploited
achiral and chiral α‐amino acids with a quaternary α‐carbon atom, as determined by …

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 α-helix is pre-eminent in structural biology and widely exploited in protein folding,
design and engineering. Although other helical peptide conformations do exist near to the α …

1. Introduction 3517 2. Diastereoselective alkylation of α-amino acids. Self-reproduction of
chirality 3518 3. Diastereoselective alkylation of chiral amino acid enolates 3535 4. Chiral β …

Along with polyisoprenoids, polypeptides, polysaccharides, and polynucleotides, Nature
contains a further group of biopolymers, the poly (hydroxyalkanoates). The commonest …

In nature, α-helical peptides adopt right-handed conformations that are dictated by L-amino
acids. Isolating one-handed α-helical peptides composed of only achiral components …

The secondary structure of poly (amino acids) is an excellent tool for controlling and
understanding the functionality and properties of proteins. In this perspective article the …

Helicity is a widespread characteristic of the secondary structure of peptides: those built of L-
amino acids typically adopt right-handed helical structures, even when most of the chain is …

The review article summarizes the most relevant solid state structural and conformational
results obtained in the laboratories involved in Italy in the studies of synthetic and natural …

We have carried out a comparative study of five ab initio electrostatic frequency maps and a
semiempirical model for the amide-I and-II modes. Unrestrained molecular dynamics …