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

Authors

  • Chantal S. Morgan,

    1. Division of Chemistry and Chemical Engineering, California Institute of Technology, MC 147-75, Pasadena, California 91125
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  • James M. Holton,

    1. Division of Biology, California Institute of Technology, MC 147-75, Pasadena, California 91125
    Current affiliation:
    1. Division of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720-3206
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  • Barry D. Olafson,

    1. Division of Biology, California Institute of Technology, MC 147-75, Pasadena, California 91125
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  • Pamela J. Bjorkman,

    1. Division of Biology, California Institute of Technology, MC 147-75, Pasadena, California 91125
    2. Howard Hughes Medical Institute, California Institute of Technology, MC 147-75, Pasadena, California 91125
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  • Stephen L. Mayo

    Corresponding author
    1. Division of Biology, California Institute of Technology, MC 147-75, Pasadena, California 91125
    2. Howard Hughes Medical Institute, California Institute of Technology, MC 147-75, Pasadena, California 91125
    • Howard Hughes Medical Institute, Division of Biology, California Institute of Technology, MC 147-75, Pasadena, California 91125
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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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