Fig. 6
From: A post-translational modification of human Norovirus capsid protein attenuates glycan binding
Hydrogen/deuterium exchange (HDX) MS experiments reveal changes in protein dynamics upon deamidation. a Deuterium uptake differences of the wild-type and deamidated GII.4 Saga P-dimer mapped to the crystal structure (pdb: 4 × 06). b Deuterium uptake differences of the wild-type and deamidated P-dimer in presence and absence of 10 mM B trisaccharide. Significant (*p < 0.01, Student’s T-test) protection is detected in peptides covering the canonical binding site (G443, Y444), whereas this effect is absent in the deamidated P-dimer. The reduction in HDX observed in peptide 283–303 can be narrowed down to residues Y299-L303, as a peptide covering residues I283-N298 shows no differences in exchange at the 8 h time point (see Supplementary Data 1–4 for details). All measurements were performed in triplicate, and error bars indicate the standard deviation. A complete collection of deuterium uptake plots is found in in Supplementary Data 1–4
