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. Author manuscript; available in PMC: 2019 Sep 1.
Published in final edited form as: Biochim Biophys Acta Biomembr. 2018 Mar 14;1860(9):1687–1697. doi: 10.1016/j.bbamem.2018.03.011

Figure 1.

Figure 1

Oligomerization and β-sheet formation in DMD simulations with different number of peptides. (A) Probabilities of observing oligomers of various sizes, (B) the total β-sheet content, and probabilities of observing (C) β-sheet rich oligomers formed by various number of β-strands and (D) β-sheets comprised of different numbers of β-strands were calculated for simulations with a given number of peptides. All analyses were averaged over all 50 independent simulations and only the last half of each trajectory was used. In panels A, C & D, the probability of each aggregate shown in the heat map was weighted according to its size (i.e., the number of composite peptides). Error bars in panel B denote the standard error of means (S.E.M).