title: Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR.
abstract: We have used hydrogen-exchange labeling detected by 2D NMR to study antibody-protein interactions for two monoclonal antibodies raised against horse cytochrome c. The data show that these antibodies bind mainly to the large 37-59 omega-loop of the cytochrome c molecule. In addition, the results provide some suggestive evidence concerning units of local structural flexibility in cytochrome c.
authors.affiliation: Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104-6059.
authors.forename: L
authors.initials: L
authors.lastname: Mayne
authors.forename: Y
authors.initials: Y
authors.lastname: Paterson
authors.forename: D
authors.initials: D
authors.lastname: Cerasoli
authors.forename: S W
authors.initials: SW
authors.lastname: Englander
mesh_terms: D000911:Antibodies, Monoclonal / Q000378:metabolism*; D001666:Binding Sites, Antibody; D003574:Cytochrome c Group / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D000939:Epitopes / Q000378:metabolism; D006859:Hydrogen / Q000378:metabolism*; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D015394:Molecular Structure
chemical_list: D000911:Antibodies, Monoclonal; D003574:Cytochrome c Group; D000939:Epitopes; D006859:Hydrogen