Protein design has come of age, but how will it mature? In the 1980s and the 1990s, the
primary motivation for de novo protein design was to test our understanding of the …

Proteins are molecular machines whose function depends on their ability to achieve
complex folds with precisely defined structural and dynamic properties. The rational design …

The primary sequence of a biopolymer encodes the essential information for folding,
permitting to carry out sophisticated functions. Inspired by natural biopolymers, peptide and …

1.1 Background In his historic review titled “Polymerization” in Chemical Reviews of 1931,
Wallace H. Carothers described his brilliant ideas about the rapidly develo** field of …

The construction of bioactive peptides using β-amino acid-containing sequence patterns is a
very promising strategy to obtain analogues that exhibit properties of high interest for …

Truncation and mutation of a poorly folded 39-residue peptide has produced 20-residue
constructs that are> 95% folded in water at physiological pH. These constructs optimize a …

A structural motif, the tryptophan zipper (trpzip), greatly stabilizes the β-hairpin conformation
in short peptides. Peptides (12 or 16 aa in length) with four different turn sequences are …

Molecular dynamics simulation techniques have been used to investigate the effect of 2, 2, 2-
trifluoroethanol (TFE) as a cosolvent on the stability of three different secondary structure …

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 …

Rational peptide design and large-scale prediction of peptide structure from sequence
remain a challenge for chemical biologists. We present PEP-FOLD, an online service, aimed …