doi: 10.1021/bi00159a006.
Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR
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- PMID: 1384698
- DOI: 10.1021/bi00159a006
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Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR
Biochemistry.
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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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