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. 1992 Nov 10;31(44):10678-85.
doi: 10.1021/bi00159a006.

Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR

L Mayne  1 , Y Paterson, D Cerasoli, S W Englander
Affiliations

Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR

L Mayne et al. Biochemistry. .

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.

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