title: Opioid peptides in micellar systems: conformational analysis by CD and by one-dimensional and two-dimensional 1H-NMR spectroscopy.
abstract: beta-Endorphin has been studied in SDS micelles by one- and two-dimensional nmr spectroscopy (1D and 2D nmr), and to explore the influence of peptide length and composition on the polypeptide structure, the investigation was extended to a number of fragments. The nmr results are compared with those obtained from CD experiments and discussed in terms of a secondary structure that involves the central region of beta-endorphin.
authors.affiliation: Istituto di Chimica delle Macromolecole del CNR, Milano, Italy.
authors.forename: L
authors.initials: L
authors.lastname: Zetta
authors.forename: R
authors.initials: R
authors.lastname: Consonni
authors.forename: A
authors.initials: A
authors.lastname: De Marco
authors.forename: R
authors.initials: R
authors.lastname: Longhi
authors.forename: E
authors.initials: E
authors.lastname: Manera
authors.forename: G
authors.initials: G
authors.lastname: Vecchio
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D008969:Molecular Sequence Data; D001615:beta-Endorphin / Q000737:chemistry*
chemical_list: D008823:Micelles; D001615:beta-Endorphin