The construction of complex protein folds relies on the precise conversion of a linear
polypeptide chain into a compact 3-dimensional structure. The interplay of forces that link …

The α‐aminoisobutyric (Aib) residue has generally been considered to be a strongly
helicogenic residue as evidenced by its ability to promote helical folding in synthetic and …

We have determined the N‐and C‐cap** preferences of all 20 amino acids by substituting
residue X in the peptides NH2‐XAKAAAAKAAAAKAAGY‐CONH2 and in Ac …

A predictive rule for protein folding is presented that involves two recurrent glycine-based
motifs that cap the carboxyl termini of α helices. In proteins, helices that terminated in glycine …

Beta-Hairpins with short connecting loops (1-5 residues) have been identified from a data
set of 250 non-homologous, high resolution (< or= 2.0 A) protein crystal structures. The …

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

An analysis on the nature of α-helix stop signals has been carried out, using a dataset of
1057 helices identified from 250 high resolution (⩽ 2.0 Å), non-homologous, protein crystal …

A comprehensive database analysis of C H… O hydrogen bonds in 3124 α‐helices and
their corresponding helix termini has been carried out from a nonredundant data set of high …

Insertion of achiral ω-amino acids into peptide sequences results in replacement of scissile
peptide bonds by proteolytically stable C− C bonds. This provides a convenient means of …

Loops are regions of nonrepetitive conformation connecting regular secondary structures.
We identified 2,024 loops of one to eight residues in length, with acceptable main‐chain …