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Skip to Search Results- 20Electrospray ionization mass spectrometry
- 12Affinity
- 11Complexes
- 10Carbohydrates
- 7Affinities
- 6Binding
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Quantifying protein-carbohydrate interactions using liquid sample desorption electrospray ionization mass spectrometry
Download2015
N. Kitova, Elena N., Shams-Ud-Doha, Km, Yao, Yuyu, Klassen, John S., Daneshfar, Rambod
The application of liquid sample desorption electrospray ionization mass spectrometry (liquid sample DESI-MS) for quantifying protein–carbohydrate interactions in vitro is described. Association constants for the interactions between lysozyme and β-D-GlcNAc-(1 → 4)-β-D-GlcNAc-(1 → 4)-D-GlcNAc and...
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Protein-glycolipid interactions studied in vitro using ESI-MS and nanodiscs: Insights into the mechanisms and energetics of binding
Download2015
Nikjah, Sanaz, Boraston, Alisdair B., Lin, Hong, Kitova, Elena N., Li, Jun, Pluvinage, Benjamin, Han, Ling Han, Klassen, John S.
Electrospray ionization-mass spectrometry (ESI-MS) analysis combined with the use of nanodiscs (NDs) to solubilize glycolipids (GLs) has recently emerged as a promising analytical method for detecting protein–GL interactions in vitro and, when applied to libraries of GLs, ranking their...
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2015
Klassen, John S., Cairo, Christopher W.Xiong, Zi Jian, Li, Jun, Privé, Gilbert G., Leney, Aneika C., Kitova, Elena N., Darestani, Reza Rezaei, Zou, Chunxia, Nikjah, Sanaz
Protein interactions with glycolipids are implicated in diverse cellular processes. However, the study of protein–glycolipid complexes remains a significant experimental challenge. Here, we describe a powerful new assay that combines electrospray ionization mass spectrometry (ESI-MS) and...
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Quantifying protein-carbohydrate interactions using liquid sample desorption electrospray ionization mass spectrometry
Download2015
Klassen, John S., N. Kitova, Elena N., Yao, Yuyu, Shams-Ud-Doha, Km, Daneshfar, Rambod
The application of liquid sample desorption electrospray ionization mass spectrometry (liquid sample DESI-MS) for quantifying protein–carbohydrate interactions in vitro is described. Association constants for the interactions between lysozyme and β-D-GlcNAc-(1 → 4)-β-D-GlcNAc-(1 → 4)-D-GlcNAc and...
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2015
Tan, Ming, Jiang, Xi, Han, Ling, Kitova, Elena N., Klassen, John S., Boraston, Alisdair, B., Pluvinage, Benjamin
The binding profiles of many human noroviruses (huNoVs) for human histo-blood group antigens have been characterized. However, quantitative-binding data for these important virus–host interactions are lacking. Here, we report on the intrinsic (per binding site) affinities of HBGA oligosaccharides...
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2015
Zhong, Weiming, Quigley, Christina, Klassen, John S., Fang, Hao, Jiang, Xi, Wei, Chao, Tan, Ming, Xia, Ming, Huang, Pengwei, Fan, Qiang, Zhang, Xufu
The recent discovery that human noroviruses (huNoVs) recognize sialic acids (SAs) in addition to histo-blood group antigens (HBGAs) pointed to a new direction in studying virus-host interactions during calicivirus infection. HuNoVs remain difficult to study due to the lack of an effective cell...
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2014
Kitova, Elena N., Klassen, John S., Michelsen, Klaus, Liu, Lan, Schnier, Paul D., Baergen, Alyson
This work explores the energetics of intermolecular H-bonds inside a hydrophobic protein cavity. Kinetic measurements were performed on the gaseous deprotonated ions (at the −7 charge state) of complexes of bovine β-lactoglobulin (Lg) and three monohydroxylated analogs of palmitic acid (PA):...
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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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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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P. aeruginosa SGNH hydrolase-like proteins AlgJ and AlgX have similar topology but separate and distinct roles in alginate acetylation
Download2014
Howell, P. Lynne, Klassen, John S., Robinson, Howard, Kitova, Elena N., Dawson, Karen, Clarke, Anthony J., Little, Dustin J., Walvoort, Marthe T., Weadge, Joel T., Codee, Jeroen D. C., Baker, Perrin, Whitney, John C., Ohman, Dennis E., Ricer, Tyler, Moynihan, Patrick J.
The O-acetylation of polysaccharides is a common modification used by pathogenic organisms to protect against external forces. Pseudomonas aeruginosa secretes the anionic, O-acetylated exopolysaccharide alginate during chronic infection in the lungs of cystic fibrosis patients to form the major...