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Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR
L Mayne1, Y Paterson, D Cerasoli
1Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104-6059.
Biochemistry
|November 10, 1992
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.