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. 2005 Apr 8;89(1):433–443. doi: 10.1529/biophysj.105.059642

FIGURE 2.

FIGURE 2

(a) Unfolding pathway of WT-TTR trajectory II at 350 K. (a) Initial structure. The DAGH sheet is in the front whereas the CBEF sheet is in the back. (b) The 800-ps snapshot. Major conformational changes are in the loop regions with some minor changes in the H strand. The original D strand becomes a surface loop. (c) The 1200-ps snapshot. The D strand that adopts a loop conformation separates from the core of the protein. (d) The 1800-ps snapshot. Most of the A, G, and H strands are disrupted. The inner sheet and outer sheet lose significant amount of native contacts. (b) The final snapshot of the continued 5-ns run of L55P-TTR trajectory II at 350 K. No α-sheet is formed. The outer (CBEF) sheet is intact whereas the inner (DAGH) sheet is severely disrupted. A shift in the β-strand D is illustrated. This three-residue shift along the upstream protein main chain, Leu-58–Thr-60, resembles “the β-slip” observed in the highly amyloidogenic TTR triple mutant G53S/E54D/L55S-TTR (45).