| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1009310 |
| landingPage: |
http://www.iedb.org/assay/1513049 |
| type: |
Literature
|
| publicationVenue: |
Biochemistry
|
| dates: |
1999
|
| study type: | b cell assays |
| subject species: | Tobacco mosaic virus |
| fullName: |
L Choulier
N Rauffer-Bruyè
re
M Ben Khalifa
F Martin
D Altschuh
|
| method: |
surface plasmon resonance (SPR)
|
| name: |
Kinetic analysis of the effect on Fab binding of identical substitutions in a peptide and its parent protein.
|
| description: |
The epitope sequence is cited in The epitope sequence is cited in Moudallal et al. (1985) EMBO J. 4:1231-1235 [PMID:16453613].
CPmutHis contains two mutations, T28I and E95D, to reduce aggregation properties of the protein. Binding parameters for the binding of the epitope-specific mAb to the antigen were determined using a BIAcore 2000 instrument. Mutations in the epitope (S142E, S142N, or E145A) did not lead to significant changes in binding. The epitope was synthesized with Lys-Gly added to the N-terminus.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |