title: Polypeptide models of elastin: CD and NMR studies on synthetic poly(X-Gly-Gly).
abstract: Poly(X-Gly-Gly), simple structural models for the hydrophobic, proline-devoid, regions of elastin, have been synthesized and studied by circular dichroism and NMR spectroscopies. The results gave evidence of type II beta-turns as the only ordered structure present in the polymers. The stability of the turns has been shown to decrease on hydration and to increase in the series Leu less than Ala less than Val less than Ile.
authors.affiliation: Department of Chemistry, University of Basilicata, Potenza, Italy.
authors.forename: A M
authors.initials: AM
authors.lastname: Tamburro
authors.forename: V
authors.initials: V
authors.lastname: Guantieri
authors.forename: A
authors.initials: A
authors.lastname: Scopa
authors.forename: J M
authors.initials: JM
authors.lastname: Drabble
mesh_terms: D002942:Circular Dichroism; D004549:Elastin / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008961:Models, Structural; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D010455:Peptides; D004549:Elastin