Exploiting Uniformly (13)C-Labeled Carbohydrates for Probing Carbohydrate-Protein Interactions by NMR Spectroscopy.
J Am Chem Soc. 2017 Apr 13;:
Authors: Nestor G, Anderson T, Oscarson S, Gronenborn AM
Abstract
NMR of a uniformly (13)C-labeled carbohydrate was used to elucidate the atomic details of a sugar-protein complex. The structure of the (13)C-labeled Man?(1-2)Man?(1-2)Man?OMe trisaccharide ligand when bound to cyanovirin-N was characterized and revealed that in the complex the glycosidic linkage torsion angles between the two reducing-end mannoses are different from the free trisaccharide. Distances within the carbohydrate were employed for conformational analysis, and NOE-based distance mapping between sugar and protein revealed that Man?(1-2)Man?(1-2)Man?OMe is bound more intimately with its two reducing-end mannoses into the domain A binding site of CV-N than with the non-reducing end unit. Taking advantage of the (13)C spectral dispersion of (13)C-labeled carbohydrates in isotope-filtered experiments is a versatile means for a simultaneous mapping of the binding interactions on both, the carbohydrate and the protein.
PMID: 28406013 [PubMed - as supplied by publisher]
NMR structure analysis of uniformly 13C-labeled carbohydrates
NMR structure analysis of uniformly 13C-labeled carbohydrates
Abstract
In this study, a set of nuclear magnetic resonance experiments, some of them commonly used in the study of 13C-labeled proteins and/or nucleic acids, is applied for the structure determination of uniformly 13C-enriched carbohydrates. Two model substances were employed: one compound of low molecular weight and one compound of medium molecular weight (13C-enriched O-antigenic polysaccharide isolated from Escherichia coli O142, ~10Â*kDa). The first step in this approach involves...
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[NMR paper] NMR structure analysis of uniformly (13)C-labeled carbohydrates.
NMR structure analysis of uniformly (13)C-labeled carbohydrates.
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J Biomol NMR. 2014 Apr 26;
Authors: Fontana C, Kovacs H, Widmalm G
Abstract
In this study, a set of nuclear magnetic resonance experiments, some of them commonly used in the study of (13)C-labeled proteins and/or nucleic acids, is applied for the structure determination of uniformly (13)C-enriched carbohydrates. Two model substances were employed: one compound of low molecular weight ...
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04-29-2014 12:04 PM
[NMR paper] Fluorinated Carbohydrates as Lectin Ligands: Dissecting Glycan-Cyanovirin Interactions by Using 19 F NMR Spectroscopy.
Fluorinated Carbohydrates as Lectin Ligands: Dissecting Glycan-Cyanovirin Interactions by Using 19 F NMR Spectroscopy.
Fluorinated Carbohydrates as Lectin Ligands: Dissecting Glycan-Cyanovirin Interactions by Using 19 F NMR Spectroscopy.
Chemistry. 2013 Feb 28;
Authors: Matei E, André S, Glinschert A, Infantino AS, Oscarson S, Gabius HJ, Gronenborn AM
Abstract
NMR spectroscopy and isothermal titration calorimetry (ITC) are powerful methods to investigate ligand-protein interactions. Here, we present a versatile and sensitive fluorine NMR...
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03-01-2013 09:57 PM
[NMR paper] Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
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J Am Chem Soc. 2005 Aug 31;127(34):11946-7
Authors: Wylie BJ, Franks WT, Graesser DT, Rienstra CM
In this Communication, we introduce a 3D magic-angle spinning recoupling experiment that correlates chemical shift...
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12-01-2010 06:56 PM
[NMR paper] New structural insights into carbohydrate-protein interactions from NMR spectroscopy.
New structural insights into carbohydrate-protein interactions from NMR spectroscopy.
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Curr Opin Struct Biol. 2003 Oct;13(5):646-53
Authors: Kogelberg H, Solís D, Jiménez-Barbero J
Recently developed NMR methods have been applied to discover carbohydrate ligands for proteins and to identify their binding epitopes. The structural details of carbohydrate-protein complexes have also been examined by NMR, providing site-specific information on the...
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11-24-2010 09:16 PM
[NMR paper] NMR and molecular modeling of complex carbohydrates and carbohydrate-protein interact
NMR and molecular modeling of complex carbohydrates and carbohydrate-protein interactions. Applications to anti-bacteria vaccines.
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Adv Exp Med Biol. 2001;491:543-50
Authors: Brisson JR, Jennings HJ
In order to characterize the conformational epitope of the group B meningococcal polysaccharide and of the type III group B Streptococcus capsular polysaccharide NMR measurements were done on a wide...
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11-19-2010 08:32 PM
[NMR paper] Probing carbohydrate-protein interactions by high-resolution NMR spectroscopy.
Probing carbohydrate-protein interactions by high-resolution NMR spectroscopy.
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Adv Exp Med Biol. 1998;435:29-38
Authors: Homans SW, Field RA, Milton MJ, Probert M, Richardson JM
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Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively 13C labeled samples
Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively 13C labeled samples
Patrik Lundström, D. Flemming Hansen and Lewis E. Kay
Journal of Biomolecular NMR; 2008; 42(1); pp 35 - 47
Abstract: Carr–Purcell–Meiboom–Gill (CPMG) relaxation dispersion nuclear magnetic resonance (NMR) spectroscopy has emerged as a powerful method for quantifying chemical shifts of excited protein states. For many applications of the technique that involve the measurement of relaxation rates of carbon...
Exploiting Uniformly (13)C-Labeled Carbohydrates for Probing Carbohydrate-Protein Interactions by NMR Spectroscopy.
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