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Conformation and dynamics of glycoprotein oligosaccharides as studied by 1 H NMR spectroscopy
Author(s) -
Van Halbeek Herman,
Poppe Leszek
Publication year - 1992
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1260301316
Subject(s) - chemistry , oligosaccharide , nuclear magnetic resonance spectroscopy , relaxation (psychology) , spectroscopy , glycoprotein , nmr spectra database , crystallography , spectral line , stereochemistry , biochemistry , physics , quantum mechanics , psychology , social psychology , astronomy
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,1 H NMR spectra of this oligosaccharide in D 2 O and H 2 O were completely assigned by the combination of TOCSY, ROESY and triple‐quantum spectroscopy experiments. Specific { 1 H, 1 H} cross‐relaxation rates and 1 H 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.