… structure of an oligoproline adopting an all-trans polyproline … This unique property is a reason
for PPII conformation to … The compactness and inherent flexibility of the PPII conformation is …

… structure consists of 6 PPII-helices that are stacked in two sets of three and form a compact
brick-like structure… α-helices have unique preference for amino acids at various positions, …

… ) is the third type of the protein backbone structure. This conformation universally exists in
fibrous, globular proteins, and biologically active peptides. It has unique physical and chemical …

… Proline is unique among the 20 genetically coded amino acids. (1) The … structures known
as poly proline helices of type-I (all-cis right handed, PP-I) or type-II (all-trans left handed, PP-II), …

… unique conformational behaviors. First, it is known that oligo- and poly-(l-proline) form two
unique helices, named polyproline… charge-dipole interaction in the compact structure of PP-I. …

… non-local interactions within compact or globular conformations or … state rather than the
secondary structure of the entire or a … ensembles of glycine residues are rare. Graf et al. explored …

… structure of an oligoproline adopting an all-trans polyproline … This unique property is a reason
for PPII conformation to … The compactness and inherent flexibility of the PPII conformation is …

… structural and thermodynamic properties of Zn 2+ - and Cu 2+ -complexes with the AaFEcR
domain, based on peptide models of its two … structure, but result in protein compaction. (6) …

… polypeptide with unusually high polyproline type II helix propensity… with an unusually high
propensity for PPII structure. … Another unusual feature of PGR was that both AUC and DLS data …

… such as trifluoroethanol but prefers a more compact right-handed PPI helical geometry in
less-… were unique PPII helical chains of different lengths (Figure 5A). The structural parameters …