title: Circular dichroism determination of class I MHC-peptide equilibrium dissociation constants.
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.
authors.affiliation: Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA.
authors.forename: C S
authors.initials: CS
authors.lastname: Morgan
authors.forename: J M
authors.initials: JM
authors.lastname: Holton
authors.forename: B D
authors.initials: BD
authors.lastname: Olafson
authors.forename: P J
authors.initials: PJ
authors.lastname: Bjorkman
authors.forename: S L
authors.initials: SL
authors.lastname: Mayo
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D016466:CHO Cells; D002942:Circular Dichroism; D006224:Cricetinae; D006183:H-2 Antigens / Q000737:chemistry* / Q000378:metabolism; D006358:Hot Temperature; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011489:Protein Denaturation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D006183:H-2 Antigens; D010455:Peptides; D011994:Recombinant Proteins