Kinetic analysis of the effect on Fab binding of identical substitutions in a peptide and its parent protein.

Title:

Kinetic analysis of the effect on Fab binding of identical substitutions in a peptide and its parent protein.

identifier:	1513039
description:	epitope description:RGTGSYNRSSFES antigen name:Capsid protein host organism:Mus musculus BALB/c antibody name:57P, 145P
aggregation:	instance of dataset
availability:	available
primaryPublications:	10090739

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 Altschuh, D. et al. (1992) Biochemistry. Jul. 14 31(27):6298-304 [PMID: 1627568]. Binding parameters for the binding of the epitope-specific mAb to the antigen were determined using a BIAcore 2000 instrument. Mutations in the epitope (S142A, E145A, or S146A) did not lead to significant changes in binding. However, mutation S142E or S142N increased the dissociation rate about 10- or 5-fold respectively. The dissociation rate for the S14E mutant protein bound to Fab 57P was calculated to be 2.63E-3s^-1.

name:	iedb
homePage:	http://www.iedb.org

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