CIRCULAR-DICHROISM DETERMINATION OF CLASS-I MHC-PEPTIDE EQUILIBRIUM DISSOCIATION-CONSTANTS

Citation
Cs. Morgan et al., CIRCULAR-DICHROISM DETERMINATION OF CLASS-I MHC-PEPTIDE EQUILIBRIUM DISSOCIATION-CONSTANTS, Protein science, 6(8), 1997, pp. 1771-1773
Citations number
12
Categorie Soggetti
Biology
Journal title
ISSN journal
09618368
Volume
6
Issue
8
Year of publication
1997
Pages
1771 - 1773
Database
ISI
SICI code
0961-8368(1997)6:8<1771:CDOCME>2.0.ZU;2-Z
Abstract
Class I major histocompatibility complex (MHC) molecules bind peptides derived from degraded proteins for display to T cells of the immune s ystem. Peptides bind to MHC proteins with varying affinities, dependin g upon their sequence and length. We demonstrate that the thermal stab ility of the MHC-peptide complex depends directly on peptide binding a ffinity. We use this correlation to develop a convenient method to det ermine peptide dissociation constants by measuring MHC-peptide complex stability using thermal denaturation profiles monitored by circular d ichroism.