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Prog Biophys Mol Biol. 2014 Apr;114(2):61-8. doi: 10.1016/j.pbiomolbio.2014.01.001. Epub 2014 Feb 19.

Solution NMR conformation of glycosaminoglycans.

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1
Program of Glycobiology, Institute of Medical Biochemistry Leopoldo de Meis, University Hospital Clementino Fraga Filho, Federal University of Rio de Janeiro, 255, HUCFF 4A01, Ilha do Fundão, Rio de Janeiro, RJ 21941-913, Brazil. Electronic address: pominvh@bioqmed.ufrj.br.

Abstract

Nuclear magnetic resonance (NMR) spectroscopy has been giving a pivotal contribution to the progress of glycomics, mostly by elucidating the structural, dynamical, conformational and intermolecular binding aspects of carbohydrates. Particularly in the field of conformation, NOE resonances, scalar couplings, residual dipolar couplings, and chemical shift anisotropy offsets have been the principal NMR parameters utilized. Molecular dynamics calculations restrained by NMR-data input are usually employed in conjunction to generate glycosidic bond dihedral angles. Glycosaminoglycans (GAGs) are a special class of sulfated polysaccharides extensively studied worldwide. Besides regulating innumerous physiological processes, these glycans are also widely explored in the global market as either clinical or nutraceutical agents. The conformational aspects of GAGs are key regulators to the quality of interactions with the functional proteins involved in biological events. This report discusses the solution conformation of each GAG type analyzed by one or more of the above-mentioned methods.

KEYWORDS:

Chemical shift anisotropy; Glycosaminoglycans; Nuclear Overhauser effect; Residual dipolar coupling; Scalar coupling

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