| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1009951 |
| landingPage: |
http://www.iedb.org/assay/1512804 |
| type: |
Literature
|
| publicationVenue: |
J Mol Recognit
|
| dates: |
1993
|
| study type: | b cell assays |
| subject species: | Tobacco mosaic virus |
| fullName: |
G Zeder-Lutz
D Altschuh
S Denery-Papini
J P Briand
G Tribbick
M H Van Regenmortel
|
| method: |
surface plasmon resonance (SPR)
|
| name: |
Epitope analysis using kinetic measurements of antibody binding to synthetic peptides presenting single amino acid substitutions.
|
| description: |
The kinetic constants of peptides with single amino acid substitutions were also determined. The largest difference was unexpectedly noted for substitution Leu to Ser at position 4, which led to a 2-fold increase in the association constant (ka), a 30-fold increase in the dissociation constant (kd), and a 15-fold decrease in the equilibrium affinity constant (Ka). A large difference also was noted for substitution Ile to Leu at position 5, which led to 2-fold increase in the association constant (ka), a 6-fold increase in the dissociation constant (kd), and a 3-fold decrease in the equilibrium affinity constant (Ka). The mAb did not bind to peptides with substitutions of Glu to Gln at position 7 or Ile to Lys at position 9.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |