Search
Skip to Search Results- 8Electrospray ionization mass spectrometry
- 6Carbohydrates
- 4Affinity
- 4Human milk oligosaccharide
- 4Library screening
- 4Lipids
-
2011
Dingle, Tanis C., Szpacenko, Adam, Ng, Kenneth K.S., Kitov, Pavel, Klassen, John S., El-Hawiet, Amr, Kitova,Elena N., Mulvey, George L., Eugenio, Luiz, Armstrong, Glen D.
The binding of recombinant fragments of the C-terminal cell-binding domains of the two large exotoxins, toxin A (TcdA) and toxin B (TcdB), expressed by Clostridium difficile and a library consisting of the most abundant neutral and acidic human milk oligosaccharides (HMOs) was examined...
-
2011
El-Hawiet, Amr, Klassen, John S., Armstrong, Glen D., Dingle, Tanis C., Eugenio, Luiz, Mulvey, George L., Szpacenko, Adam, Ng, Kenneth K.S., Kitova,Elena N., Kitov, Pavel
The binding of recombinant fragments of the C-terminal cell-binding domains of the two large exotoxins, toxin A (TcdA) and toxin B (TcdB), expressed by Clostridium difficile and a library consisting of the most abundant neutral and acidic human milk oligosaccharides (HMOs) was examined...
-
Carbohydrate-lipid interactions: Affinities of methylmannose polysaccharides for lipids in aqueous solution
Download2012
Sun, Nian, Klassen, John S., Bai, Yu, Liu, Lan, Xia, Li, Lowary, Todd L.
The interactions between 3-O-methyl-mannose polysaccharides (MMPs), extracted from Mycobacterium smegmatis (consisting of a mixture of MMP-10, -11, -12 and -13) or obtained by chemical synthesis (MMP-5s, -8s, -11s and -14s), and linear saturated and unsaturated fatty acids (FAs), and a commercial...
-
Carbohydrate-lipid interactions: Affinities of methylmannose polysaccharides for lipids in aqueous solution
Download2012
Xia, Li, Sun, Nian, Klassen, John S., Liu, Lan, Bai, Yu, Lowary, Todd L.
The interactions between 3-O-methyl-mannose polysaccharides (MMPs), extracted from Mycobacterium smegmatis (consisting of a mixture of MMP-10, -11, -12 and -13) or obtained by chemical synthesis (MMP-5s, -8s, -11s and -14s), and linear saturated and unsaturated fatty acids (FAs), and a commercial...
-
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):...
-
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):...
-
2014
Klassen, John S., Derda, Ratmir, Ng, Simon, Bailey, Justin, Baergen, Alyson, Liu, Lan, Jalili, Nobar
This paper reports on the first experimental study of the energies of noncovalent fluorine bonding in a protein-ligand complex in the absence of solvent. Arrhenius parameters were measured for the dissociation of gaseous deprotonated ions of complexes of bovine β-lactoglobulin (Lg), a model...
-
2014
Klassen, John S., Ng, Simon, Liu, Lan, Bailey, Justin, Derda, Ratmir, Baergen, Alyson, Jalili, Nobar
This paper reports on the first experimental study of the energies of noncovalent fluorine bonding in a protein-ligand complex in the absence of solvent. Arrhenius parameters were measured for the dissociation of gaseous deprotonated ions of complexes of bovine β-lactoglobulin (Lg), a model...
-
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...
-
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...