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Published August 1997 | public
Journal Article

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


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.

Additional Information

© 1997 The Protein Society. Received December 26, 1996; Accepted April 23, 1997. We thank B. Dahiyat, G. Hathaway, J. Johnson, and D. Penny for technical help, C. White for insightful discussions, and M. Ary for comments on the manuscript. C.S.M. is supported by the James Irvine Foundation and ARCS Foundation. P.J.B. acknowledges support from the Arthritis Foundation. S.L.M. acknowledges support from the Rita Allen Foundation, the David and Lucile Packard Foundation, and the Searle Scholars Program/The Chicago Community Trust.

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August 22, 2023
October 23, 2023