Stereochemically constrained amino acid residues that strongly favour specific backbone
conformations may be used to nucleate and stabilize specific secondary structures in …

α-Aminoisobutyric acid (Aib) is a Cα-tetrasubstituted amino acid that strongly favors helical
structure. Most of the conformational trends established for Aib-rich peptides have been …

Prediction of peptide secondary structure (R-helix,-sheet, 310-helix, etc.) a priori from amino
acid sequence is a primary goal of de noVo protein design and protein folding studies. 1 …

The undecamer of poly-l-leucine at the water− hexane interface is studied by molecular
dynamics simulations. This represents a simple model relevant to folding and insertion of …

The proposal by Pauling and his coworkers (1951) of an atomic model for the structure of the
alpha helix stimulated research in several areas of protein chemistry. It excited chemists as …

Free energy surfaces, or potentials of mean force, for the a-to 3io-helicalconformational
transition in polypeptides have been calculated in several solvents of differentdielectric. The …

An overview of the use of non-protein amino acids in the design of conformationally well-
defined peptides, based on work from the author's laboratory, is discussed. The crystal …

A structural transition from a 310‐helix to an α‐helix has been characterized at high
resolution for an octapeptide segment located in 3 different sequences. Three synthetic …

Oligopeptides based on protein (CR-trisubstituted) R-amino acids are known to undergo R-
helix a unordered conformation transitions under appropriate experimental conditions. 1 On …

The strong propensity of 2‐amino‐2‐methyl propanoic acid (Aib)‐rich peptides to form
stable helical structures is well documented. NMR analysis of the short peptide Z‐(Aib) 5‐l …