[NMR paper] Unraveling the interaction between the LPS O-antigen of Burkholderia anthina and the 5D8 monoclonal antibody by using a multidisciplinary chemical approach, with synthesis, NMR, and molecular modeling methods.
Unraveling the interaction between the LPS O-antigen of Burkholderia anthina and the 5D8 monoclonal antibody by using a multidisciplinary chemical approach, with synthesis, NMR, and molecular modeling methods.
Related ArticlesUnraveling the interaction between the LPS O-antigen of Burkholderia anthina and the 5D8 monoclonal antibody by using a multidisciplinary chemical approach, with synthesis, NMR, and molecular modeling methods.
Chembiochem. 2013 Aug 19;14(12):1485-93
Authors: Marchetti R, Canales A, Lanzetta R, Nilsson I, Vogel C, Reed DE, Aucoin DP, Jiménez-Barbero J, Molinaro A, Silipo A
Abstract
The interaction between the O-chain from the lipopolysaccharide from Burkholderia anthina and a lipopolysaccharide-specific monoclonal antibody (5D8) has been studied at high resolution by NMR spectroscopy. In particular, the 5D8-bound epitope of the saccharide entity has been unraveled by a combination of saturation transfer difference (STD) and transferred NOESY (tr-NOESY) experiments performed on the 5D8/polysaccharide complex. To dissect the fine details of the molecular recognition events, further experiments with simpler carbohydrate ligands were carried out. Thus, experiments were also performed with ad hoc synthesized trisaccharide and hexasaccharide O-antigen repeating units. By using this multidisciplinary approach (chemical synthesis, NMR spectroscopy and molecular dynamics simulation), determination of the binding epitope and the contribution to the binding of the sugar units composing the O-chain have been determined.
[NMR paper] Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
J Biochem. 2013 Oct 4;
Authors: Yuasa N, Koyama T, Subedi GP, Yamaguchi Y, Matsushita M, Fujita-Yamaguchi Y
Abstract
T-antigen (Gal?1-3GalNAc?-1-Ser/Thr), also known as...
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Unraveling the 13C NMR Chemical Shiftsin Single-Walled Carbon Nanotubes: Dependence on Diameter and ElectronicStructure
Unraveling the 13C NMR Chemical Shiftsin Single-Walled Carbon Nanotubes: Dependence on Diameter and ElectronicStructure
Chaiwat Engtrakul, Veronica M. Irurzun, Erica L. Gjersing, Josh M. Holt, Brian A. Larsen, Daniel E. Resasco and Jeffrey L. Blackburn
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja211181q/aop/images/medium/ja-2011-11181q_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja211181q
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http://feeds.feedburner.com/~r/acs/jacsat/~4/k6jE1qN8glA
[NMR paper] NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimen
NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides.
Related Articles NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides.
Chembiochem. 2004 Sep 6;5(9):1245-55
Authors: Aboitiz N, Vila-Perelló M, Groves P, Asensio JL, Andreu D, Cañada FJ, Jiménez-Barbero...
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[NMR paper] NMR and molecular modeling studies of the interaction between wheat germ agglutinin a
NMR and molecular modeling studies of the interaction between wheat germ agglutinin and the beta-D-GlcpNAc-(1-->6)-alpha-D-Manp epitope present in glycoproteins of tumor cells.
Related Articles NMR and molecular modeling studies of the interaction between wheat germ agglutinin and the beta-D-GlcpNAc-(1-->6)-alpha-D-Manp epitope present in glycoproteins of tumor cells.
Biochemistry. 2004 Aug 3;43(30):9647-54
Authors: Lycknert K, Edblad M, Imberty A, Widmalm G
The beta-D-GlcpNAc-(1-->6)-alpha-D-Manp disaccharide is a constituent of highly...
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[NMR paper] Epitope mapping of gibberellin to the anti-gibberellin A(4) monoclonal antibody by sa
Epitope mapping of gibberellin to the anti-gibberellin A(4) monoclonal antibody by saturation transfer difference NMR spectroscopy.
Related Articles Epitope mapping of gibberellin to the anti-gibberellin A(4) monoclonal antibody by saturation transfer difference NMR spectroscopy.
Biochem Biophys Res Commun. 2003 Aug 1;307(3):498-502
Authors: Murata T, Hemmi H, Nakajima M, Yoshida M, Yamaguchi I
Saturation transfer difference (STD) NMR spectroscopy is a promising tool for rapid screening, identifying ligands that interact with a target protein,...
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[NMR paper] NMR study on the interaction between MHC class I protein and its antigen peptide.
NMR study on the interaction between MHC class I protein and its antigen peptide.
Related Articles NMR study on the interaction between MHC class I protein and its antigen peptide.
Biochem Biophys Res Commun. 2000 Nov 30;278(3):609-13
Authors: Nakagawa M, Chiba-Kamoshida K, Udaka K, Nakanishi H
A major histcompatibility complex (MHC) class I protein H-2K(b) was expressed in a large scale as a fusion protein with thioredoxin and hexahistidine at the N-terminus to analyze the interaction with the antigen peptide SIYRYYGL. NMR spectra of the...
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[NMR paper] NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
Related Articles NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
J Mol Biol. 1998 Aug 7;281(1):61-7
Authors: Huang X, Yang X, Luft BJ, Koide S
Outer surface protein A (OspA) from the Lyme disease spirochete Borrelia burgdorferi has been a focus of vaccine development. We have identified epitopes of OspA to two monoclonal antibodies (mAbs) by comparing NMR chemical shifts of free OspA and those in Fab complexes....
Unraveling the interaction between the LPS O-antigen of Burkholderia anthina and the 5D8 monoclonal antibody by using a multidisciplinary chemical approach, with synthesis, NMR, and molecular modeling methods.
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