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Circular dichroism determination of class I MHC-peptide equilibrium dissociation constants

✍ Scribed by Chantal S. Morgan; James M. Holton; Barry D. Olafson; Pamela J. Bjorkman; Stephen L. Mayo

Book ID: 105356475
Publisher: Cold Spring Harbor Laboratory Press
Year: 1997
Tongue: English
Weight: 272 KB
Volume: 6
Category: Article
ISSN: 0961-8368
DOI: 10.1002/pro.5560060819

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✦ Synopsis

Abstract

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.

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