title: Investigation of the membrane-active peptides melittin and glucagon by photochemically induced dynamic-nuclear-polarization (photo-CIDNP) NMR.
abstract: The photochemically induced dynamic-nuclear-polarization (photo-CIDNP) NMR technique was used to investigate the membrane-active peptides melittin and glucagon. The experiments were performed both in the absence and presence of phospholipid vesicles in order to study the topography of the membrane-bound state. From the results it can be concluded that the melittin peptide chain is oriented in such a way that the single tryptophan residue (Trp19) reaches into the membrane. In the case of glucagon, a binding interaction with vesicle membranes is indicated within the pH range 2-10, whereby the single tryptophan residue (Trp25) is buried in the lipid bilayer and the tyrosine and histidine residues are exposed to the aqueous solvent.
authors.affiliation: Institut für Biophysikalische Chemie, Universität Frankfurt, Federal Republic of Germany.
authors.forename: T
authors.initials: T
authors.lastname: Maurer
authors.forename: C
authors.initials: C
authors.lastname: Lücke
authors.forename: H
authors.initials: H
authors.lastname: Rüterjans
mesh_terms: D000595:Amino Acid Sequence; D005934:Glucagon / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008555:Melitten / Q000737:chemistry*; D008969:Molecular Sequence Data; D010777:Photochemistry
chemical_list: D008555:Melitten; D005934:Glucagon