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. 1997 Aug;6(8):1771-3.
doi: 10.1002/pro.5560060819.

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

C S Morgan  1 , J M Holton, B D Olafson, P J Bjorkman, S L Mayo
Affiliations

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

C S Morgan et al. Protein Sci. 1997 Aug.

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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