| Title : Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR - Mayne_1992_Biochemistry_31_10678 |
| Author(s) : Mayne L , Paterson Y , Cerasoli DM , Englander SW |
| Ref : Biochemistry , 31 :10678 , 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. |
| PubMedSearch : Mayne_1992_Biochemistry_31_10678 |
| PubMedID: 1384698 |
Mayne L, Paterson Y, Cerasoli DM, Englander SW (1992)
Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR
Biochemistry
31 :10678
Mayne L, Paterson Y, Cerasoli DM, Englander SW (1992)
Biochemistry
31 :10678