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 JαCH-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.

500 MHZ NMR CHARACTERIZATION OF SYNTHETIC BOMBESIN AND RELATED PEPTIDES IN DMSO-D6 BY TWO-DIMENSIONAL TECHNIQUES

D'AURIA, GABRIELLA;PAOLILLO, LIVIO;
1988

Abstract

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 JαCH-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.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/404557
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