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Table 1.
Relative quantification of exchange efficiency by MS
MHC I alleleMHC I monomer folded withTemplate peptide exchanged forEfficiency of exchange
   % 
H-2Kb FAPGNAPAL SIINFEKL 105.5 ± 4.7 
FAPGNWPAL 94.2 ± 10.8 
FAPGNYPAA 84.4 ± 6.2 
FAPGNAPAL 4.2 ± 0.1 
0.1 ± 0.1 
SIINFEKL 107.4 ± 12.6 
HLA-A*02:01 IAKEPVHGV NLVPMVATV 101.3 ± 13.2 
LLDQLIEEV 86.0 ± 14.6 
GLCTLVAML 70.7 ± 16.3 
IAKEPVHGV 27.4 ± 2.7 
7.2 ± 2.2 
NLVPMVATV 80.5 ± 15.3 
MHC I alleleMHC I monomer folded withTemplate peptide exchanged forEfficiency of exchange
   % 
H-2Kb FAPGNAPAL SIINFEKL 105.5 ± 4.7 
FAPGNWPAL 94.2 ± 10.8 
FAPGNYPAA 84.4 ± 6.2 
FAPGNAPAL 4.2 ± 0.1 
0.1 ± 0.1 
SIINFEKL 107.4 ± 12.6 
HLA-A*02:01 IAKEPVHGV NLVPMVATV 101.3 ± 13.2 
LLDQLIEEV 86.0 ± 14.6 
GLCTLVAML 70.7 ± 16.3 
IAKEPVHGV 27.4 ± 2.7 
7.2 ± 2.2 
NLVPMVATV 80.5 ± 15.3 

Peptide exchange on MHC I was performed with 0.5 µM monomers (H-2Kb or HLA-A*02:01), incubated with 50 µM peptide as described in Materials and methods. Monomers were also incubated in the absence of peptide to determine the stability of the complexes under these conditions. To quantify the amount of eluted peptide, standard curves were created with the respective synthetic peptides. H-2Kb–SIINFEKL and HLA-A*02:01–NLVPMVATV were measured as positive controls.

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