title: High-throughput screening of holoprotein conformational stability by dynamic ligand exchange-affinity capillary electrophoresis.
abstract: Dynamic ligand exchange-affinity capillary electrophoresis (DLE-ACE) is introduced as a convenient platform for assessing the conformational stability and relative affinity of a holoprotein to different ligands without off-line sample pretreatment, since ligand exchange and protein unfolding processes are integrated in-capillary during electromigration.
authors.affiliation: Department of Chemistry, McMaster University, 1280 Main Street West, Hamilton, ON, Canada L8S 4M1.
authors.forename: G
authors.initials: G
authors.lastname: Seguí-Lines
authors.forename: J M A
authors.initials: JM
authors.lastname: Gavina
authors.forename: J C
authors.initials: JC
authors.lastname: D'Amaral
authors.forename: P
authors.initials: P
authors.lastname: Britz-McKibbin
mesh_terms: D019075:Electrophoresis, Capillary / Q000379:methods*; D008024:Ligands; D008832:Microchemistry / Q000379:methods; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000032:analysis*; D013816:Thermodynamics
chemical_list: D008024:Ligands; D011506:Proteins