title: NMR structural biology of sulfated glycans.
abstract: Sulfated fucans, sulfated galactans, and glycosaminoglycans are extensively studied worldwide in terms of both structure and biomedical functions. Liquid-state nuclear magnetic resonance (NMR) spectroscopy is the most employed analytical technique in structural analysis of these sulfated glycans. This is due to the fact that NMR-based analyses enable a series of achievements such as (i) accurate structure characterization/determination; (ii) measurements of parameters regarding molecular motion (dynamics); (iii) assessment of the 3D structures (usually assisted by computational techniques of Molecular Modeling and/or Molecular Dynamics) of the composing monosaccharides (ring conformers) and the overall conformational states of the glycan chains either free in solution or bound to proteins; and (iv) analysis of the resultant intermolecular complexes with functional proteins through either the protein or the carbohydrate perspective. In this review, after a general introduction about the principal NMR parameters utilized for achieving this set of structural information, discussion is given on NMR-based studies of some representative sulfated fucans, sulfated galactans, and glycosaminoglycans. Due to the growing number of studies concerning both structure and function of sulfated glycans and the widely use of NMR spectroscopy in such studies, a review paper discussing (i) the most experiments employed for analysis, (ii) procedures used in data interpretation, and (iii) the general aspects of the sulfated glycans, is timely in the literature.
authors.affiliation: a Program of Glycobiology , Institute of Medical Biochemistry Leopoldo de Meis, and University Hospital Clementino Fraga Filho, Federal University of Rio de Janeiro , Rio de Janeiro , RJ 21941-913 , Brazil.
authors.forename: Paulo A G
authors.initials: PA
authors.lastname: Soares
authors.affiliation: a Program of Glycobiology , Institute of Medical Biochemistry Leopoldo de Meis, and University Hospital Clementino Fraga Filho, Federal University of Rio de Janeiro , Rio de Janeiro , RJ 21941-913 , Brazil.
authors.forename: Ismael N L
authors.initials: IN
authors.lastname: Queiroz
authors.affiliation: a Program of Glycobiology , Institute of Medical Biochemistry Leopoldo de Meis, and University Hospital Clementino Fraga Filho, Federal University of Rio de Janeiro , Rio de Janeiro , RJ 21941-913 , Brazil.
authors.forename: Vitor H
authors.initials: VH
authors.lastname: Pomin
mesh_terms: D002241:Carbohydrates / Q000737:chemistry; D046911:Macromolecular Substances / Q000737:chemistry / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D056004:Molecular Dynamics Simulation; D011134:Polysaccharides / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D002241:Carbohydrates; D046911:Macromolecular Substances; D011134:Polysaccharides; D011506:Proteins; C007789:fucoidan
keywords: NOE; glycosaminoglycans; spin relaxation; sulfated fucan; sulfated galactan