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. 2011 Oct 13;7(10):e1002144. doi: 10.1371/journal.pcbi.1002144

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Dalchau et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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The peptide optimization model of Fig. 2 was used to simulate a labeled cohort of peptide-MHC complexes by switching from generation of an unlabeled MHC population to a labeled population for 5 min (yellow blocks). The plots represent the concentration of total labeled MHC (blue), labeled MHC with medium or high affinity peptide (green) and labeled MHC with high affinity peptide only (red), at each time point. Simulations were performed in the absence (A) and presence (B) of tapasin. Corresponding experimental results [6] are also reported (circles). Simulations were conducted for representative low, medium and high affinity peptides with a separate dissociation rate and generation rate for each peptide , and a separate peptide binding rate for each HLA–B allele (Table S1 in Text S1; Protocol S1).

Inline graphic — The peptide optimization model of Fig. 2 was used to simulate a labeled cohort of peptide-MHC complexes by switching from generation of an unlabeled MHC population to a labeled population for 5 min (yellow blocks). The plots represent the concentration of total labeled MHC (blue), labeled MHC with medium or high affinity peptide (green) and labeled MHC with high affinity peptide only (red), at each time point. Simulations were performed in the absence (A) and presence (B) of tapasin. Corresponding experimental results [6] are also reported (circles). Simulations were conducted for representative low, medium and high affinity peptides with a separate dissociation rate and generation rate for each peptide , and a separate peptide binding rate for each HLA–B allele (Table S1 in Text S1; Protocol S1).