Figure 2 | Scientific Reports

Figure 2

From: Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors

Figure 2

Secondary structural content of bound and free Aβ42. (a) Residue-wise population distribution (in %) of the secondary structural elements in free Αβ42 monomer. The values were estimated from our earlier published REMD study42. Standard errors of mean were estimated by dividing the production portion of replicas into four 35 ns long, non-overlapping blocks (see Methods). (b–d) Differences (in percentage) in residue-wise β-strand, 310-helix, and α-helix propensities between bound and free Aβ42. Positive values indicate higher occurrence in the hexapeptide-bound system, and vice versa. (b) WT-bound, (c) A2V-bound, and (d) A2T-bound.

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