Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11: XN6P4 ]
 
NCBI PubMed ID: 36622423
Publication DOI: 10.1021/acs.chemrev.2c00580
Journal NLM ID: 2985134R
Publisher: Chem Rev
Correspondence: G. Widmalm <goran.widmalmsu.se>
Institutions: Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, S-106 91 Stockholm, Sweden, Departamento de Química del Litoral, CENUR Litoral Norte, Universidad de la República, Paysandú 60000, Uruguay

Glycans, carbohydrate molecules in the realm of biology, are present as biomedically important glycoconjugates and a characteristic aspect is that their structures in many instances are branched. In determining the primary structure of a glycan, the sugar components including the absolute configuration and ring form, anomeric configuration, linkage(s), sequence, and substituents should be elucidated. Solution state NMR spectroscopy offers a unique opportunity to resolve all these aspects at atomic resolution. During the last two decades, advancement of both NMR experiments and spectrometer hardware have made it possible to unravel carbohydrate structure more efficiently. These developments applicable to glycans include, inter alia, NMR experiments that reduce spectral overlap, use selective excitations, record tilted projections of multidimensional spectra, acquire spectra by multiple receivers, utilize polarization by fast-pulsing techniques, concatenate pulse-sequence modules to acquire several spectra in a single measurement, acquire pure shift correlated spectra devoid of scalar couplings, employ stable isotope labeling to efficiently obtain homo- and/or heteronuclear correlations, as well as those that rely on dipolar cross-correlated interactions for sequential information. Refined computer programs for NMR spin simulation and chemical shift prediction aid the structural elucidation of glycans, which are notorious for their limited spectral dispersion. Hardware developments include cryogenically cold probes and dynamic nuclear polarization techniques, both resulting in enhanced sensitivity as well as ultrahigh field NMR spectrometers with a 1H NMR resonance frequency higher than 1 GHz, thus improving resolution of resonances. Taken together, the developments have made and will in the future make it possible to elucidate carbohydrate structure in great detail, thereby forming the basis for understanding of how glycans interact with other molecules.

NMR, glycan

Structure type: suggested polymer biological repeating unit
Location inside paper: Fig. 38(a)
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130648,IEDB_130701,IEDB_136104,IEDB_137473,IEDB_137485,IEDB_1391961,IEDB_140116,IEDB_141584,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_885822,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72
 
Comments, role: review; structure of the deacylated R-LPS of B. melitensis Bm_wbkD
 
NCBI Taxonomy refs (TaxIDs): 562
Reference(s) to other database(s): GTC:G82509QD, GlycomeDB:3519
Show glycosyltransferases
 

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