Thread: NMR paper Effect of antibody binding on protein motions studied by hydrogen-exchange labeling a
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Default Effect of antibody binding on protein motions studied by hydrogen-exchange labeling a
Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR.

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

Biochemistry. 1992 Nov 10;31(44):10678-85

Authors: Mayne L, Paterson Y, Cerasoli D, Englander SW

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.

PMID: 1384698 [PubMed - indexed for MEDLINE]



Source: PubMed
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