The preferred conformations of peptides heavily based on the currently extensively exploited
achiral and chiral α‐amino acids with a quaternary α‐carbon atom, as determined by …

Fourier transform infrared spectroscopy (FTIR) can be used for conformational analysis of
peptides in a wide range of environments. Measurements can be performed in aqueous …

BESIDE THE CLASSICAL a-helix and pleated~-sneet conformation, the only other principal
structure that occurs significantly in globular proteins is the 3t0-helix. This structure was first …

Oligomers that adopt predictable conformations (“foldamers”) are subjects of increasing
interest from the perspectives of both fundamental research and applications.[1] The study of …

The secondary structure of poly (amino acids) is an excellent tool for controlling and
understanding the functionality and properties of proteins. In this perspective article the …

Numerous backbone constraints can be used to develop pseudopeptides or
pseudomimetics of biologically active peptides. Among those, N-and Cα-methyl amino acids …

A model for the solution structure of horse heart ferricytochrome c has been determined by
nuclear magnetic resonance spectroscopy combined with hybrid distance geometry …

The review article summarizes the most relevant solid state structural and conformational
results obtained in the laboratories involved in Italy in the studies of synthetic and natural …

α-Aminoisobutyric acid (Aib) is a Cα-tetrasubstituted amino acid that strongly favors helical
structure. Most of the conformational trends established for Aib-rich peptides have been …

Helices are among the predominant secondary structures in globular proteins. About 90% of
the residues in them are found to be in the α-helical conformation, and another 10% in the …