The poly-l-proline type II (PPII) helix in recent years has emerged clearly as a structural class
not only of fibrillar proteins (in collagen, PPII is a dominant conformation) but also of the …

Abstract The Database of Antimicrobial Activity and Structure of Peptides (DBAASP) is an
open-access, comprehensive database containing information on amino acid sequences …

The main-chain conformations of 80 proteins were analyzed to identify helical structures that
commonly occur but do not fall into the known classes of α-helix, 3 10-helix and β-sheet. The …

The “random coil” conformational problem is examined by comparison of vibrational CD
(VCD) spectra of various polypeptide model systems with that of proline oligomers [(Pro) n] …

In this chapter, the basic phenomenon of circular dichroism (CD) will be described. The
central theoretical parameter of rotational strength will then be defined. The mechanisms by …

The striking similarity between observed circular dichroism spectra of nonprolyl
homopolymers and that of regular left-handed polyproline II (PII) helices prompted Tiffany …

Circular dichroism (CD) is widely used in protein science to elucidate protein secondary
structure, to monitor protein folding, to detect conformational changes, and to measure …

The use of Lennard-Jones potentials gives rise to an expected energydistribution for main-
chain polypeptide conformations in the Ramachandran plot that matches well the observed …

Antiviral peptides (AVPs) are bioactive peptides that exhibit the inhibitory activity against
viruses through a range of mechanisms. Virus entry inhibitory peptides (VEIPs) make up a …

Translation of consecutive prolines causes ribosome stalling, which is alleviated but cannot
be fully compensated by the elongation factor P. However, the presence of polyproline …