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Secondary structure from chemical shifts:
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Disordered proteins:
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Old 05-12-2016, 09:30 PM
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Default NMR Structural Biology of Sulfated Glycans.

NMR Structural Biology of Sulfated Glycans.

Related Articles NMR Structural Biology of Sulfated Glycans.

J Biomol Struct Dyn. 2016 May 11;:1-45

Authors: Soares PA, Queiroz IN, Pomin VH

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 in the field 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.


PMID: 27166778 [PubMed - as supplied by publisher]



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