Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR.
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.
Mayne
L
L
Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104-6059.
Paterson
Y
Y
Cerasoli
D
D
Englander
S W
SW
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
D000911:Antibodies, Monoclonal; D003574:Cytochrome c Group; D000939:Epitopes; D006859:Hydrogen