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- 4Cholera-toxin binding
- 4Ionization mass-spectrometry
- 4Membranes
- 4Phospholipid-bilayer nanodiscs
- 4Recognition
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2016
Richards, Michele R., Campuzano, Iain D. G., Kitova, Elena N., Klassen, John S., Li, Jun, Privé, Gilbert G., Xiong, Zi Jian, Bagal, Dhanashri
Saposin A (SapA) lipoprotein discs, also known as picodiscs (PDs), represent an attractive method to solubilize glycolipids for protein interaction studies in aqueous solution. Recent electrospray ionization mass spectrometry (ESI-MS) data suggest that the size and composition of...
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2016
Klassen, John S., Campuzano, Iain D. G., Bagal, Dhanashri, Privé, Gilbert G., Kitova, Elena N., Xiong, Zi Jian, Richards, Michele R., Li, Jun
Saposin A (SapA) lipoprotein discs, also known as picodiscs (PDs), represent an attractive method to solubilize glycolipids for protein interaction studies in aqueous solution. Recent electrospray ionization mass spectrometry (ESI-MS) data suggest that the size and composition of...
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Localizing carbohydrate binding sites in proteins using hydrogen/deuterium exchange mass spectrometry
Download2016
Kitova, Elena N., Klassen, John S., Eugenio, Luiz, Li, Jun, Ng, Kenneth, Zhang, Jingjing
The application of hydrogen/deuterium exchange mass spectrometry (HDX-MS) to localize ligand binding sites in carbohydrate-binding proteins is described. Proteins from three bacterial toxins, the B subunit homopentamers of Cholera toxin and Shiga toxin type 1 and a fragment of Clostridium...
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Localizing carbohydrate binding sites in proteins using hydrogen/deuterium exchange mass spectrometry
Download2016
Klassen, John S., Kitova, Elena N., Li, Jun, Zhang, Jingjing, Ng, Kenneth, Eugenio, Luiz
The application of hydrogen/deuterium exchange mass spectrometry (HDX-MS) to localize ligand binding sites in carbohydrate-binding proteins is described. Proteins from three bacterial toxins, the B subunit homopentamers of Cholera toxin and Shiga toxin type 1 and a fragment of Clostridium...
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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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Screening oligosaccharide libraries against lectins using the proxy protein electrospray ionization mass spectrometry assay
Download2016
Kitova, Elena N., Klassen, John S., Fan, Xuxin, Privé, Gilbert G., Cairo, Christopher W., Xiong, Zi Jian, Ng, Kenneth K. S., Zou, Chunxia, Eugenio, Luiz, Li, Jun
An electrospray ionization mass spectrometry (ESI-MS) assay for screening carbohydrate libraries against lectins is described. The assay is based on the proxy protein ESI-MS method, which combines direct ESI-MS protein–ligand binding measurements and competitive protein binding, to simultaneously...
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Screening oligosaccharide libraries against lectins using the proxy protein electrospray ionization mass spectrometry assay
Download2016
Privé, Gilbert G., Ng, Kenneth K. S., Xiong, Zi Jian, Klassen, John S., Kitova, Elena N., Fan, Xuxin, Li, Jun, Zou, Chunxia, Eugenio, Luiz, Cairo, Christopher W.
An electrospray ionization mass spectrometry (ESI-MS) assay for screening carbohydrate libraries against lectins is described. The assay is based on the proxy protein ESI-MS method, which combines direct ESI-MS protein–ligand binding measurements and competitive protein binding, to simultaneously...