The conformation of bombesin in solution as determined by two-dimensional 1H-NMR techniques.
The 1H nuclear magnetic resonance spectrum of the tetradecapeptide, bombesin, has been assigned in (2H6)dimethyl sulphoxide solution and aqueous solution using two-dimensional techniques. The chemical shifts in both solvents indicate that the molecule has little secondary structure and adopts a random coil conformation. A comparison is made between the spectra of various smaller bombesin fragments and the intact polypeptide.
Carver
J A
JA
Department of Biochemistry, University of Adelaide, South Australia.
D001839:Bombesin; D004735:Energy Transfer; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D012996:Solutions; D013696:Temperature
D010446:Peptide Fragments; D012996:Solutions; D001839:Bombesin