The conformation of bombesin in solution as determined by two‐dimensional 1H‐NMR techniques

Abstract

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. Copyright © 1987, Wiley Blackwell. All rights reserved