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Nonspecific interactions between proteins and charged biomolecules in electrospray ionization mass spectrometry
Download2010
Soya, Naoto, Klassen, John S., Kitova, Elena N., Sun, Nian
An investigation of the nonspecific association of small charged biomolecules and proteins in electrospray ionization mass spectrometry (ES-MS) is described. Aqueous solutions containing pairs of proteins and a small acidic or basic biomolecule that does not interact specifically with either of...
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Nonspecific interactions between proteins and charged biomolecules in electrospray ionization mass spectrometry
Download2010
Kitova, Elena N., Sun, Nian, Klassen, John S., Soya, Naoto
An investigation of the nonspecific association of small charged biomolecules and proteins in electrospray ionization mass spectrometry (ES-MS) is described. Aqueous solutions containing pairs of proteins and a small acidic or basic biomolecule that does not interact specifically with either 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...
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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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2015
Klassen, John S., Darestani, Reza Rezaei, Kitova, Elena N., Zou, Chunxia, Li, Jun, Leney, Aneika C., Cairo, Christopher W.Xiong, Zi Jian, Privé, Gilbert G., 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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Protein-glycolipid interactions studied in vitro using ESI-MS and nanodiscs: Insights into the mechanisms and energetics of binding
Download2015
Han, Ling Han, Kitova, Elena N., Klassen, John S., Pluvinage, Benjamin, Lin, Hong, Nikjah, Sanaz, Li, Jun, Boraston, Alisdair B.
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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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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Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry
Download2010
El-Hawiet, Amr, Klassen, John S., Kitova, Elena N., Liu, Lan
A new electrospray ionization mass spectrometry (ES-MS) approach for quantifying protein—ligand complexes that are prone to in-source (gas-phase) dissociation is described. The method, referred to here as the reference ligand ES-MS method, is based on the direct ES-MS assay and competitive ligand...
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Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry
Download2010
El-Hawiet, Amr, Liu, Lan, Klassen, John S., Kitova, Elena N.
A new electrospray ionization mass spectrometry (ES-MS) approach for quantifying protein—ligand complexes that are prone to in-source (gas-phase) dissociation is described. The method, referred to here as the reference ligand ES-MS method, is based on the direct ES-MS assay and competitive ligand...
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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...