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. Author manuscript; available in PMC: 2017 Sep 6.
Published in final edited form as: Structure. 2016 Aug 18;24(9):1537–1549. doi: 10.1016/j.str.2016.07.007

Figure 2.

Figure 2

Details of the TDP-43 helical subdomain monomeric structure by molecular simulation. See also Figure S2. (A) Correspondence between chemical shift deviations from random coil reference values (top) and 3JHNHα scalar coupling constants predicted from the simulation ensemble of TDP-43310–350 (red) and measured by experiment (black, open circles) demonstrate that the simulation faithfully captures structural character of the helical subdomain. (B) Based on regions of continuous backbone dihedral angles (ϕ,ψ), α-helical structure of TDP-43 peptide shows extended helical structure primarily in the 321 to 334 region. (i–v) Ensemble members and their total population (labeled %) representing populated regions of the α-helix map based on structural clustering. (C) Secondary structure sampled by each position in the TDP-43 simulated ensemble based on DSSP in three classes. Data are plotted as mean ± SEM for simulation data.