title: Synthetic fragments and analogues of elastin. II. Conformational studies.
abstract: Conformational studies on synthetic repetitive sequences and analogues of elastin are described. CD and nmr measurements gave evidence of flexible beta-turns as the dominant structural feature whose stability was found to decrease by increasing the number of repetitive units. The sequences comprised the structural unit Gly-X-Gly (X = Val, Leu, Ala), with X-Gly or Gly-Gly located at the corners of the bend. Based on that, it is proposed that these regions of elastin, unlike the proline-containing sequences, contribute to the elasticity of the protein through a classical mechanism in terms of the rotational isomeric state theory.
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: L
authors.initials: L
authors.lastname: Pandolfo
authors.forename: A
authors.initials: A
authors.lastname: Scopa
mesh_terms: D000595:Amino Acid Sequence; D004549:Elastin / Q000031:analogs & derivatives*; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D011487:Protein Conformation
chemical_list: D010446:Peptide Fragments; D004549:Elastin