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- 8Carbohydrates
- 6Norovirus
- 4Affinity
- 4Library screening
- 4Lipids
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Identifying carbohydrate ligands of a norovirus P particle using a catch and release electrospray ionization mass spectrometry assay
Download2014
Jiang, Xi, Kitova, Elena N., Klassen, John S., Tan, Ming, Han, Ling
Noroviruses (NoVs), the major cause of epidemic acute gastroenteritis, recognize human histo-blood group antigens (HBGAs), which are present as free oligosaccharides in bodily fluid or glycolipids and glycoproteins on the surfaces of cells. The subviral P particle formed by the protruding (P)...
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Identifying carbohydrate ligands of a norovirus P particle using a catch and release electrospray ionization mass spectrometry assay
Download2014
Jiang, Xi, Kitova, Elena N., Klassen, John S., Tan, Ming, Han, Ling
Noroviruses (NoVs), the major cause of epidemic acute gastroenteritis, recognize human histo-blood group antigens (HBGAs), which are present as free oligosaccharides in bodily fluid or glycolipids and glycoproteins on the surfaces of cells. The subviral P particle formed by the protruding (P)...
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Measuring positive cooperativity using the direct ESI-MS assay: Cholera toxin B subunit homopentamer binding to GM1 pentasaccharide
Download2014
Lin, Hong, Klassen, John S., Kitova, Elena N.
Direct electrospray ionization mass spectrometry (ESI-MS) assay was used to investigate the stepwise binding of the GM1 pentasaccharide β-D-Galp-(1→3)-β-D-GalpNAc-(1→4)[α-D-Neu5Ac-(2→3)]-β-D-Galp-(1→4)-β-D-Glcp (GM1os) to the cholera toxin B subunit homopentamer (CTB5) and to establish...
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Measuring positive cooperativity using the direct ESI-MS assay: Cholera toxin B subunit homopentamer binding to GM1 pentasaccharide
Download2014
Kitova, Elena N., Lin, Hong, Klassen, John S.
Direct electrospray ionization mass spectrometry (ESI-MS) assay was used to investigate the stepwise binding of the GM1 pentasaccharide β-D-Galp-(1→3)-β-D-GalpNAc-(1→4)[α-D-Neu5Ac-(2→3)]-β-D-Galp-(1→4)-β-D-Glcp (GM1os) to the cholera toxin B subunit homopentamer (CTB5) and to establish...
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Quantifying protein-fatty acid interactions using electrospray ionization mass spectrometry
Download2011
Liu, Lan, Kitova, Elena N., Klassen, John S.
The application of the direct electrospray ionization mass spectrometry (ESI-MS) assay to quantify interactions between bovine β-lactoglobulin (Lg) and a series of fatty acids (FA), CH3(CH2)xCOOH, where x = 6 (caprylic acid, CpA), 8 (capric acid, CA), 10 (lauric acid, LA), 12 (myristic acid, MA),...
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Quantifying protein-fatty acid interactions using electrospray ionization mass spectrometry
Download2011
Klassen, John S., Kitova, Elena N., Liu, Lan
The application of the direct electrospray ionization mass spectrometry (ESI-MS) assay to quantify interactions between bovine β-lactoglobulin (Lg) and a series of fatty acids (FA), CH3(CH2)xCOOH, where x = 6 (caprylic acid, CpA), 8 (capric acid, CA), 10 (lauric acid, LA), 12 (myristic acid, MA),...
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Reliable determinations of protein-ligand interactions by direct ESI-MS measurements: Are we there yet?
Download2012
El-Hawiet, Amr, Klassen, John S., Kitova, Elena N., Schnier, Paul D.
The association-dissociation of noncovalent interactions between protein and ligands, such as other proteins, carbohydrates, lipids, DNA, or small molecules, are critical events in many biological processes. The discovery and characterization of these interactions is essential to a complete...
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Reliable determinations of protein-ligand interactions by direct ESI-MS measurements: Are we there yet?
Download2012
Klassen, John S., Kitova, Elena N., Schnier, Paul D., El-Hawiet, Amr
The association-dissociation of noncovalent interactions between protein and ligands, such as other proteins, carbohydrates, lipids, DNA, or small molecules, are critical events in many biological processes. The discovery and characterization of these interactions is essential to a complete...
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Screening carbohydrate libraries for protein interactions using the direct ESI-MS assay: Applications to libraries of unknown concentration
Download2014
El-Hawiet, Amr, Klassen, John S., Kitova, Elena N.
A semiquantitative electrospray ionization mass spectrometry (ESI-MS) binding assay suitable for analyzing mixtures of oligosaccharides, at unknown concentrations, for interactions with target proteins is described. The assay relies on the differences in the ratio of the relative abundances of...
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Screening carbohydrate libraries for protein interactions using the direct ESI-MS assay: Applications to libraries of unknown concentration
Download2014
El-Hawiet, Amr, Klassen, John S., Kitova, Elena N.
A semiquantitative electrospray ionization mass spectrometry (ESI-MS) binding assay suitable for analyzing mixtures of oligosaccharides, at unknown concentrations, for interactions with target proteins is described. The assay relies on the differences in the ratio of the relative abundances of...