title: Characterization of collagen-like heterotrimers: implications for triple-helix stability.
abstract: This article deals with the effects of proline hydroxylation on collagen triple-helix stability, an issue that is still under discussion. To investigate the structural determinants of triple-helix stabilization by hydroxyproline (Hyp), we here characterized spectroscopically triple-helix heterotrimers containing both chains of (Pro-Pro-Gly)10 and (Pro-Hyp-Gly)10. Results are discussed in relation to the various triple-helix stabilization mechanisms.
authors.affiliation: Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 6, I-80134 Napoli, Italy.
authors.forename: Rita
authors.initials: R
authors.lastname: Berisio
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Granata
authors.forename: Luigi
authors.initials: L
authors.lastname: Vitagliano
authors.forename: Adriana
authors.initials: A
authors.lastname: Zagari
mesh_terms: D000595:Amino Acid Sequence; D003094:Collagen / Q000737:chemistry*; D006358:Hot Temperature; D006909:Hydroxyproline / Q000737:chemistry; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011392:Proline / Q000737:chemistry; D011489:Protein Denaturation; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides; D003094:Collagen; D011392:Proline; D006909:Hydroxyproline