Figure 6.

Secondary structure variation along MD simulations of WT- and L55P-TTR. (A): WT-TTR, control run (at 310 K); (B–F): WT-TTR, runs 1 to 5; (G): L55P-TTR, control run (at 310 K); (H–L): L55P-TTR, runs 1 to 5. All runs, except the control runs, were performed at 500 K. Secondary structure was assigned with the program STRIDE.⁶⁵ Residues in β-sheet are shown in gray, helical motifs are represented in dark gray, and residues in nonregular or other secondary structure are shown in white.