title: Synthesis and circular dichroism study of the human salivary proline-rich protein IB7.
abstract: The solid phase synthesis of a 59 amino acid human salivary protein IB7 has been accomplished using Fmoc strategy. Because the protein contains 25 proline, 13 glycine and 9 glutamine residues the coupling time, piperidine delivery and acetic anhydride reaction time were increased. Yield after HPLC purification was 35%. Circular dichroism studies revealed that about one third of IB7 residues adopted a type II helix secondary structure, as found in collagen helices. The rest of the sequence adopts a random coil secondary structure.
authors.affiliation: Institut Européen de Chimie et Biologie, FRE CNRS 2247, Pessac, France.
authors.forename: Cécile
authors.initials: C
authors.lastname: Simon
authors.forename: Isabelle
authors.initials: I
authors.lastname: Pianet
authors.forename: Erick J
authors.initials: EJ
authors.lastname: Dufourc
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry* / Q000302:isolation & purification; D055232:Proline-Rich Protein Domains; D017433:Protein Structure, Secondary; D012471:Salivary Proteins and Peptides / Q000138:chemical synthesis* / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D010455:Peptides; D012471:Salivary Proteins and Peptides