Fig. 5
Hydrogen-deuterium exchange mass spectrometry of the NiV G ectodomain in the presence and absence of monomeric ephrinB2. a Relative fractional exchange rates of NiV G residues. Residue ranges were defined by the heatmap generated with DynamX. b Hydrogen-deuterium exchange rates for selected NiV G peptides from apo- and ephrinB2-167-bound NiV G. Mean and s.d. values for deuterium uptake are shown for each time point, n = 3. c Relative fractional exchange rates of key NiV G regions mapped onto the crystal structure of the NiV G globular domain bound to monomeric ephrinB2. Residue ranges were defined as in a. d Estimated location of the predicted α-helical stalk region of NiV G (black line) superposed on a representative 2D class average of NiV G obtained by electron microscopy. The estimated location of peptide 127–140, which undergoes the greatest increase in exchange upon ephrinB2-167 binding is shown with a red line
