| 摘要 |
The binding sites of binding proteins and their binding partners are characterized, at the individual amino acid level, by a combination of heavy hydrogen (tritium or deuterium) exchange labeling and sequential degradation (preferably, by carboxypeptidase) and analysis of labeled fragments under slowed exchange conditions. By first labeling the binding partner and labeling the binding site of the protein indirectly (by exchange at the binding surface), the binding site may be differentiated from allosterically protected segments of the binding protein.
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