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.
Morgan
C S
CS
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA.
Holton
J M
JM
Olafson
B D
BD
Bjorkman
P J
PJ
Mayo
S L
SL
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
D006183:H-2 Antigens; D010455:Peptides; D011994:Recombinant Proteins