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. 2023 Dec 11;14:8204. doi: 10.1038/s41467-023-43654-9

Fig. 4. Global conformational plasticity of empty vs NRASQ61K bound HLA-A*01:01/hβ2m visualized by hydrogen/deuterium exchange.

Fig. 4

a Mass spectrometric envelopes for peptide fragments comprising residues HLA-A*01:01 81–96 (magenta), HLA-A*01:01 139–154 (green), and hβ2m 41–56 (blue) for emptied HLA-A*01:01 with no HDX (i.e., all H sample) and 600 s HDX compared with NRASQ61K bound HLA-A*01:01 at 600 s HDX. The peptide fragment masses are noted. b Kinetic graphs of % deuterium uptake (back-exchange corrected) for different peptide fragments as a function of HDX time (0, 20, 60, 180, or 600 s) shown for emptied (blue) versus NRASQ61K bound (red) HLA-A*01:01/hβ2m. Data are mean % deuterium uptake ± SD from triplicate experiments. c Structure view of average % deuterium uptake at 600 s (back-exchange corrected) for empty and NRASQ61K bound HLA-A*01:01/hβ2m plotted onto PDB IDB 6MPP without or with atoms corresponding to NRASQ61K. Color ranges from deep blue (no deuterium uptake) to red (100% deuterium uptake). Black indicates regions where peptides were not obtained. Mean % deuterium uptakes at 600 s (back-exchange corrected) were resolved to individual peptide fragments and obtained from three independent samples.