Search
Skip to Search Results- 14Electrospray ionization mass spectrometry
- 6Norovirus
- 6Protein–ligand complexes
- 4Affinity
- 2Affinities
- 2Affinity measurement
-
Quantifying protein-fatty acid interactions using electrospray ionization mass spectrometry
Download2011
Liu, Lan, Kitova, Elena N., Klassen, John S.
The application of the direct electrospray ionization mass spectrometry (ESI-MS) assay to quantify interactions between bovine β-lactoglobulin (Lg) and a series of fatty acids (FA), CH3(CH2)xCOOH, where x = 6 (caprylic acid, CpA), 8 (capric acid, CA), 10 (lauric acid, LA), 12 (myristic acid, MA),...
-
Quantifying protein-fatty acid interactions using electrospray ionization mass spectrometry
Download2011
Klassen, John S., Kitova, Elena N., Liu, Lan
The application of the direct electrospray ionization mass spectrometry (ESI-MS) assay to quantify interactions between bovine β-lactoglobulin (Lg) and a series of fatty acids (FA), CH3(CH2)xCOOH, where x = 6 (caprylic acid, CpA), 8 (capric acid, CA), 10 (lauric acid, LA), 12 (myristic acid, MA),...
-
Reliable determinations of protein-ligand interactions by direct ESI-MS measurements: Are we there yet?
Download2012
El-Hawiet, Amr, Klassen, John S., Kitova, Elena N., Schnier, Paul D.
The association-dissociation of noncovalent interactions between protein and ligands, such as other proteins, carbohydrates, lipids, DNA, or small molecules, are critical events in many biological processes. The discovery and characterization of these interactions is essential to a complete...
-
Reliable determinations of protein-ligand interactions by direct ESI-MS measurements: Are we there yet?
Download2012
Klassen, John S., Kitova, Elena N., Schnier, Paul D., El-Hawiet, Amr
The association-dissociation of noncovalent interactions between protein and ligands, such as other proteins, carbohydrates, lipids, DNA, or small molecules, are critical events in many biological processes. The discovery and characterization of these interactions is essential to a complete...
-
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...
-
2013
Klassen, John S., Xia, Ming, Tan, Ming, Wang, Leyi, Han, Ling, Kitova, Elena N., Jiang, Xi, Kitov, Pavel I.
Noroviruses (NoVs), the major cause of viral acute gastroenteritis, recognize histo-blood group antigens (HBGAs) as receptors or attachment factors. To gain a deeper understanding of the interplay between NoVs and their hosts, the affinities of recombinant P dimers (P2's) of a GII.4 NoV (VA387)...
-
2013
Jiang, Xi, Klassen, John S., Kitova, Elena N., Wang, Leyi, Han, Ling, Kitov, Pavel I., Xia, Ming, Tan, Ming
Noroviruses (NoVs), the major cause of viral acute gastroenteritis, recognize histo-blood group antigens (HBGAs) as receptors or attachment factors. To gain a deeper understanding of the interplay between NoVs and their hosts, the affinities of recombinant P dimers (P2's) of a GII.4 NoV (VA387)...
-
Dissociation kinetics of the streptavidin-biotin interaction measured using direct electrospray ionization mass spectrometry analysis
Download2013
Kitova, Elena N., Klassen, John S., Deng, Lu
Dissociation rate constants (koff) for the model high affinity interaction between biotin (B) and the homotetramer of natural core streptavidin (S4) were measured at pH 7 and temperatures ranging from 15 to 45 °C using electrospray ionization mass spectrometry (ESI-MS). Two different approaches...
-
Dissociation kinetics of the streptavidin-biotin interaction measured using direct electrospray ionization mass spectrometry analysis
Download2013
Deng, Lu, Klassen, John S., Kitova, Elena N.
Dissociation rate constants (koff) for the model high affinity interaction between biotin (B) and the homotetramer of natural core streptavidin (S4) were measured at pH 7 and temperatures ranging from 15 to 45 °C using electrospray ionization mass spectrometry (ESI-MS). Two different approaches...