500 MHz NMR characterization of synthetic bombesin and related peptides in DMSO-d6 by two-dimensional techniques

FEBS Lett. 1988 Sep 12;237(1-2):85-90. doi: 10.1016/0014-5793(88)80177-7.

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 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.

MeSH terms

  • Amino Acid Sequence
  • Bombesin* / chemical synthesis
  • Deuterium
  • Dimethyl Sulfoxide
  • Magnetic Resonance Spectroscopy / methods
  • Protein Conformation

Substances

  • Deuterium
  • Bombesin
  • Dimethyl Sulfoxide