Open AccessThe conformation of bombesin in solution as determined by two‐dimensional 1 H‐NMR techniques
Author(s) -
CARVER John A.
Publication year - 1987
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1987.tb13404.x
Subject(s) - random coil , bombesin , aqueous solution , chemistry , molecule , chemical shift , nuclear magnetic resonance , proton nmr , spectral line , nuclear magnetic resonance spectroscopy , nmr spectra database , crystallography , stereochemistry , organic chemistry , circular dichroism , biochemistry , physics , neuropeptide , receptor , astronomy
The 1 H nuclear magnetic resonance spectrum of the tetradecapeptide, bombesin, has been assigned in ( 2 H 6 )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.