Intramolecular Cohesion of Coils Mediated by Phenylalanine–Glycine Motifs in the Natively Unfolded Domain of a Nucleoporin
Figure 2
Molecular dimensions of the simulated FG domain structures.
(A) Average radii of gyration of Nup116 FG domains simulated at different simulation temperatures. Box-plot of average radii of gyration (Rg) in units of Angstroms calculated from twenty replicate 1 ns simulations at 300, 325, and 350 K for the wild-type and F>A mutant FG domains. (B) Histogram of radii of gyration (calculated using only the atoms in the peptide backbone) for the 10,000 FG domains structures sampled from the 350 K simulations. (C) Histogram of end-to-end distances (calculated from the terminal C and N atoms) for 10,000 FG domain structures obtained by sampling every 1 ps of the final 500 ps of each of the twenty replicate MD simulations at 350 K.