Opioid peptides in micellar systems: conformational analysis by CD and by one-dimensional and two-dimensional 1H-NMR spectroscopy.
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.
Zetta
L
L
Istituto di Chimica delle Macromolecole del CNR, Milano, Italy.
Consonni
R
R
De Marco
A
A
Longhi
R
R
Manera
E
E
Vecchio
G
G
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D008969:Molecular Sequence Data; D001615:beta-Endorphin / Q000737:chemistry*
D008823:Micelles; D001615:beta-Endorphin