Solution conformation of Forssman antigen probed by NOE and exchange interactions.
The conformation of Forssman glycolipid, GalNAc alpha 1-3GalNAc beta 1-3Gal alpha 1-4Gal beta 1-4Glc beta 1-1ceramide, was analysed with the aid of the rotating frame NOE and Hartmann-Hahn spectroscopy. NOE contacts between C-, O-, and N-linked protons were used for distance mapping. The glycosidic bonds that are common to globotriaosylceramide and globoside showed a similar flexibility as found for these compounds [Poppe et al., (1990) Eur. J. Biochem. 189, 313-325; J. Am. Chem. Soc. 112, 7762-7771]. In contrast, the conformational mobility of the terminal GalNAc alpha 1-3GalNAc beta linkage appears to be restrained. A new approach, based on 2D exchange spectroscopy, was proposed for revealing of spatial proximities between exchangeable protons in Me2SO solution.
Poppe
L
L
Max-Planck-Institut für Medizinische Forschung, Heidelberg, Germany.
Dabrowski
J
J
von der Lieth
C W
CW
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D005577:Forssman Antigen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data
D005577:Forssman Antigen