2-DIMENSIONAL NMR SPECTRAL STUDY (AT 500 MHZ) OF A GLYCOOCTAPEPTIDE DERIVED FROM GLYCOPHORIN AM

One-dimensional and two-dimensional spectral data are presented for the N -terminal glycooctapeptide derived from the transmembrane glycoprotein, glycophorin A M . Two-dimensional homonuclear Hartmann-Hahn spectroscopy (2D-HOHAHA) and two-dimensional rotating frame nuclear Overhauser enhancement spectroscopy (2D-ROESY) were used to assign many of the resonances present in the spectra, with specific emphasis placed upon the oligosaccharide units. Not only were intra residue NOE's detected, but also inter residue NOE's involving two linked carbohydrates [p-Gal(l-->3)a-GalNAc] and also between the α-GalNac—>Thr linkage pair (between GalNAc H-l and Thr Hβ) indicating restricted motion about this glycosidic bond. Moreover, the H-l/H-2 cross-peaks in the 2D-ROESY spectra appear to be well resolved indicating some chemical shift differences for H-l and H-2 of the three linkage GalNAc residues found in this glycooctapeptide. © 1990, Taylor & Francis Group, LLC. All rights reserved.