title: Spectroscopic studies on elastin-like synthetic polypeptides.
abstract: Spectroscopic studies on synthetic polypeptides containing the unit-X-G-G (X=V or L) are reported. The sequences, constituting either fragments or model of elastin, were shown to adopt type II beta-turns together with an ensemble of unordered conformations. Furthermore, it was found that the stability of the beta-turns was depending on the nature of the X residue, on the hydration of the chain and, in the case of the sequence G-V-G-G-L, was decreasing by increasing the length of the chain.
authors.affiliation: Department of Chemistry, Università della Basilicata, Potenza, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Castiglione-Morelli
authors.forename: A
authors.initials: A
authors.lastname: Scopa
authors.forename: A M
authors.initials: AM
authors.lastname: Tamburro
authors.forename: V
authors.initials: V
authors.lastname: Guantieri
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D004549:Elastin / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D013696:Temperature
chemical_list: D010455:Peptides; D004549:Elastin