Figure 5.

Impact of W196 hAIF_Δ1-101 mutations on the dynamics of the β-hairpin and its environment. Representative conformations of the (a) β-hairpin and the central β-strand and the (b) His-rich helix and the loop connecting it to the central β-strand in final MD structures of selected replicates for each W196_ox variant. MD final replicates are shown in grey in each panel. All panels compare to the crystallographic WT_ox structure (4BV6) that shows the β-hairpin in red, the C-loop in orange, and the rest of the protein in purple. Open green arrows indicate relevant displacements of structural elements relative to the crystallographic WT_ox structure. The lower panel in (a) shows the time evolution of the distances between Cαs of the residue at position 196 in the β-hairpin and P488 in the β-sheet. For each variant, data show averaged values for the 5 MD replicates run for each model in the hAIF_∆1-101ox (bold lines) and CTC (line) states. Ramachandran plots of the distribution of key main chain Φ/ψ conformational along the MD of selected replicates for each (c) oxidized and (d) reduced W196 variant.