Search
Skip to Search Results- 16Electrospray ionization mass spectrometry
- 11Complexes
- 8Affinity
- 8Carbohydrates
- 7Affinities
- 6Binding
-
Mapping protein-ligand interactions in the gas phase using a functional group replacement strategy: Comparison of CID and BIRD activation methods
Download2013
Klassen, John S., Deng, Lu, Kitova, Elena N.
Intermolecular interactions in the gaseous ions of two protein–ligand complexes, a single chain antibody (scFv) and its trisaccharide ligand (α-D-Galp-(1→2)-[α-D-Abep-(1→3)]-α-Manp-OCH3, L1) and streptavidin homotetramer (S4) and biotin (B), were investigated using a collision-induced...
-
Mapping protein-ligand interactions in the gas phase using a functional group replacement strategy: Comparison of CID and BIRD activation methods
Download2013
Klassen, John S., Kitova, Elena N., Deng, Lu
Intermolecular interactions in the gaseous ions of two protein–ligand complexes, a single chain antibody (scFv) and its trisaccharide ligand (α-D-Galp-(1→2)-[α-D-Abep-(1→3)]-α-Manp-OCH3, L1) and streptavidin homotetramer (S4) and biotin (B), were investigated using a collision-induced...
-
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...
-
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...
-
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...
-
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...
-
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...
-
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...
-
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...
-
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...