Retention of bioactive ligand conformation in a gaseous protein-trisaccharide complex.
Arrhenius parameters, obtained with the blackbody infrared radiative dissociation technique, are reported for the dissociation of gaseous protonated complexes of a single-chain variable fragment (scFv) of the monoclonal antibody Se155-4 with structurally constrained trisaccharide ligands that resemble the bioactive conformer. The similarity in the dissociation activation energies measured for the +10 charge-state complexes of the constrained ligands and the native trisaccharide is evidence that the bioactive conformation of the native ligand is retained in the gas phase.
Kitova
Elena N
EN
Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2G2.
Wang
Weijie
W
Bundle
David R
DR
Klassen
John S
JS
D000911:Antibodies, Monoclonal / Q000737:chemistry; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D005740:Gases; D007128:Immunoglobulin Fragments / Q000737:chemistry*; D007700:Kinetics; D008969:Molecular Sequence Data; D011487:Protein Conformation; D021241:Spectrometry, Mass, Electrospray Ionization; D055672:Static Electricity; D014312:Trisaccharides / Q000737:chemistry*
D000911:Antibodies, Monoclonal; D005740:Gases; D007128:Immunoglobulin Fragments; D014312:Trisaccharides