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 …

Tryptophan plays important roles in protein stability and recognition despite its scarcity in
proteins. Except as fluorescent groups, they have been used rarely in peptide design …

Minimized β hairpins have provided additional data on the geometric preferences of Trp
interactions in TW-loop-WT motifs. This motif imparts significant fold stability to peptides as …

Proteins involved in immune checkpoint pathways, such as CTLA4, PD1, and PD-L1, have
become important targets for cancer immunotherapy; however, development of small …

A series of β-hairpin peptides based on variations of the TrpZip2 sequence,
SWTWENGKWTWK, of Cochran and co-workers were studied using electronic circular …

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 …

Although much has been learned about the design of models of β-sheets during the last
decade, modest fold stabilities in water and terminal fraying remain a feature of most β …

Thioamides are sterically almost identical to their oxoamide counterparts, but they are
weaker hydrogen bond acceptors. Therefore, thioamide amino acids are excellent …

Motivation: The solvent accessibility of amino acid residues plays an important role in tertiary
structure prediction, especially in the absence of significant sequence similarity of a query …

Peptide β-sheet systems have emerged as context-independent models for probing
secondary structure propensities, the nature and magnitude of stabilizing weak interactions …