Figure 4 | Scientific Reports

Figure 4

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

Figure 4

Intermolecular binding analysis. (a) Interpeptide binding free energy estimation, as estimated using the MM-PBSA method. Van der Waals, electrostatic, and total binding energy values (±standard errors of mean) are reported in kcal/mol. (b) Average number of Aβ42 heavy-atom contacts per residue across the hexapeptide sequence. Standard error values were estimated by dividing the production data into four 35 ns long blocks (see Methods). (c–e) Quaternary heavy-atom contact probability maps: (c) WT-bound, (d) A2V-bound, and (e) A2T-bound systems.

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