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Circular dichroism determination of class I MHC‐peptide equilibrium dissociation constants
Author(s) -
Morgan Chantal S.,
Holton James M.,
Olafson Barry D.,
Bjorkman Pamela J.,
Mayo Stephen L.
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560060819
Subject(s) - circular dichroism , chemistry , peptide , dissociation constant , equilibrium constant , crystallography , physics , stereochemistry , biochemistry , receptor
Class I major histocompatibility complex (MHC) molecules bind peptides derived from degraded proteins for display to T cells of the immune system. Peptides bind to MHC proteins with varying affinities, depending upon their sequence and length. We demonstrate that the thermal stability of the MHC‐peptide complex depends directly on peptide binding affinity. We use this correlation to develop a convenient method to determine peptide dissociation constants by measuring MHC‐peptide complex stability using thermal denaturation profiles monitored by circular dichroism.