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 …

What I cannot create, I do not understand. Richard P. Feynman β-Sheets consist of
extended polypeptide strands (β-strands) connected by a network of hydrogen bonds and …

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 …

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 …

Protein folding barriers result from a combination of factors including unavoidable energetic
frustration from nonnative interactions, natural variation and selection of the amino acid …

What is the smallest protein? This is actually not such a simple question to answer, because
there is no established consensus among scientists as to the definition of a protein. We …

Phage display of peptide libraries has become a powerful tool for the evolution of novel
ligands that bind virtually any protein target. However, the rules governing conformational …

Ab initio based calculations of force fields and atomic polar tensors are used to simulate
amide I infrared absorption spectra for a series of isotopically substituted (Ac-A12-NH-CH3) …

A model β-hairpin peptide has been used to investigate the context-dependent contribution
of cross-strand Lys− Glu interactions to hairpin stability. We have mutated two Ser− Lys …

Amino acid structural propensities measured in “host− guest” model studies are often used
in protein structure prediction or to choose appropriate residues in de novo protein design …