Publisher Summary This chapter focuses on contemporary approaches to the design of
structurally defined peptides and proteins with special emphasis being given to the ways in …

The structural preferences of synthetic peptides containing α, β‐dehydroamino acid
residues, as determined by theoretical studies, x‐ray diffraction analyses, and spectroscopic …

The de novo design of peptides and proteins has emerged as an approach for investigating
protein structure and function. The success relies heavily on the ability to design relatively …

In this second part of our review article on the preferred screw sense and interconversion of
peptide helices, we discuss the most significant computational and experimental data …

Incorporation of α, β‐dehydrophenylalanine (ΔPhe) residue in peptides induces folded
conformations: β‐turns in short peptides and 310‐helices in larger ones. A few exceptions …

The confornlational preferences of amino acid side chains are of fundamental importance in
determining the interactions that govern the preferred conformations of polypeptides and …

The crystal and molecular structure of the pentapeptide Boc‐d‐Ala‐ΔPhe‐Gly‐ΔPhe‐d‐Ala‐
OMe, containing two dehydrophenylalanine residues, was determined by x‐ray diffraction …

The aspartic proteinase, endothiapepsin (EC 3.4. 23.6), was complexed with a highly potent
renin inhibitor, H-261 (t-Boc-His-Pro-Phe-His-Leu OH Val-Ile-His), where OH denotes a …

Abstract α, β‐Dehydroamino acids are expected to provide conformational constraint to the
peptide backbone. A pentapeptide containing two dehydrophenylalanines (ΔZPhe) …

The peptide N‐Boc‐l‐Pro‐dehydro‐Phe‐l‐Gly‐OH was synthesized by the usual workup
procedure and finally coupling the N‐Boc‐l‐Pro‐dehydro‐Phe to glycine. The peptide …