Conformation and dynamics of glycoprotein oligosaccharides as studied by 1H NMR spectroscopy

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Abstract
Most complex carbohydrates can take a large number of shapes in solution. Determining the favored solution conformations and characterizing the internal motions of complex carbohydrates is essential to understanding their biological function, particularly their interactions with proteins. This paper describes an NMR spectroscopic study of the internal dynamics of a mucin glycoprotein‐derived di‐antennary octasaccharide, equation image 1H NMR spectra of this oligosaccharide in D2O and H2O were completely assigned by the combination of TOCSY, ROESY and triple‐quantum spectroscopy experiments. Specific {1H,1H} cross‐relaxation rates and 1H longitudinal relaxation times were measured at various temperatures and magnetic field strengths. The data show that the NeuAcα(2 → 3)Galβ arm of the octasaccharide can adopt two conformations around the (2 → 3)‐bond. Most important, the NeuAcα(2 → 3)Galβ and Galα(1 → 4)Galβ linkages both have pronounced conformational flexibility; their rearrangements are fast on the time scale of the overall molecular tumbling.

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