title: 1H-NMR conformational study of a synthetic peptide derived from the consensus sequence of annexins.
abstract: The solution conformation of a synthetic 18 amino acid peptide derived from a consensus sequence of Annexins has been investigated by 1H NMR. Full sequential assignment has been achieved. Conformational properties of the peptide were deduced from the analysis of J(NH-CH alpha) coupling constants, amide proton exchange, 2D NOESY connectivities and computer modeling.
authors.affiliation: SBPM and URA CNRS 1290, Department of Cell and Molecular Biology, CEN Saclay, Gif sur Yvette, France.
authors.forename: F
authors.initials: F
authors.lastname: Macquaire
authors.forename: F
authors.initials: F
authors.lastname: Baleux
authors.forename: T
authors.initials: T
authors.lastname: Huynh-Dinh
authors.forename: J M
authors.initials: JM
authors.lastname: Neumann
authors.forename: A
authors.initials: A
authors.lastname: Sanson
mesh_terms: D000595:Amino Acid Sequence; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D013696:Temperature
chemical_list: D002135:Calcium-Binding Proteins; D010455:Peptides