500 MHz NMR characterization of synthetic bombesin and related peptides in DMSO-d6 by two-dimensional techniques.
The proton NMR characterization of bombesin has been carried out at 500 MHz in DMSO-d6 using two-dimensional homo- and 1H-13C hetero-correlated techniques. All resonances in the NMR spectra have been assigned and several coupling constants have been measured. The backbone J alpha CH-NH coupling constants have constant values that vary between 7.8 and 8.2 Hz and indicate an unfolded structure in DMSO-d6. Discrepancies with data recently obtained at 300 MHz [(1987) Eur. J. Biochem. 168, 193-199] are discussed.
Di Bello
C
C
Institute of Industrial Chemistry, University of Padua, Italy.
Gozzini
L
L
Tonellato
M
M
Grazia Corradini
M
M
D'Auria
G
G
Paolillo
L
L
Trivellone
E
E
D000595:Amino Acid Sequence; D001839:Bombesin / Q000138:chemical synthesis; D003903:Deuterium; D004121:Dimethyl Sulfoxide; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D011487:Protein Conformation
D003903:Deuterium; D001839:Bombesin; D004121:Dimethyl Sulfoxide