title: Conformation of uteroglobin fragments.
abstract: The conformation of three fragments of uteroglobin in aqueous solution and in the presence of SDS micelles is described. Two of these fragments correspond to helix II and helix III of uteroglobin, the crystal structure of which is made of four helices. The third peptide comprises helices II and III, with the connecting beta-turn. While helix II does not interact strongly with the micelles, helix III adopts a rather clear alpha-helix in this system. The elongation of helix III with the addition of helix II at the N-terminus somewhat stabilizes the ordered structure. It is possible that the beta-turn found in the crystal is also present in solution.
authors.affiliation: Department of Organic Chemistry, University of Padova, Italy.
authors.forename: S
authors.initials: S
authors.lastname: Mammi
authors.forename: M T
authors.initials: MT
authors.lastname: Foffani
authors.forename: S
authors.initials: S
authors.lastname: Improta
authors.forename: M
authors.initials: M
authors.lastname: Tessari
authors.forename: E
authors.initials: E
authors.lastname: Schievano
authors.forename: E
authors.initials: E
authors.lastname: Peggion
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D011487:Protein Conformation; D014598:Uteroglobin / Q000737:chemistry*
chemical_list: D010446:Peptide Fragments; D014598:Uteroglobin