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Skip to Search Results- 4Protein–ligand complexes
- 2Collision-induced dissociation
- 2Dissociation kinetics
- 2Electrospray ionization mass spectrometry
- 2Hydrogen bonds
- 2Hydrogen/deuterium exchange mass spectrometry
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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...
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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...
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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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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...
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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...