File S1 - Cross Dimerization of Amyloid-β and αSynuclein Proteins in Aqueous Environment: A Molecular Dynamics Simulations Study

Supporting files. Figure S1, Evolution of the a) total inter-peptide interaction strength, and b) inter peptide distance over 150 ns for the dimerising trajectories. Figure S2, The backbone mean square fluctuation (MSF) for the a) N-terminal residues, b) middle regions, and c) C-terminal residues of Aβ1–42, and the d) N-terminal residues, e) middle regions, and f) C-terminal residues of αSyn1–95. The data for the last 50 ns of the dimerising trajectories are shown in gray, with the averages in green (solid line). Corresponding average data for the same systems for the initial 50 ns is provided in green (broken line). Average data for the non-dimerising systems is shown in maroon (broken line) for comparison. Figure S3, Residue wise maximum electrostatic (left column) and van der Waal (right column) interaction energies (in kcal mol−1) of αSyn1–95 with Aβ1–42 for clusters C1, C2, C3, C4 and C5. Table S1, Mean value of the inter-residue sidechain distances (dSB, in Å) between the residues that form salt bridges in the clusters a) C1, b) C2, c) C3, d) C5. Standard deviations are provided in braces. The first residue belongs to αSyn1–95; the second residue belongs to Aβ1–42. Table S2, Mean values of the total number of internal contacts formed in the Aβ1–42 (NintAβ) and αSyn1–95 (NintαS) proteins in the five clusters. The corresponding radii of gyration (in Å) have been denoted as RgAβ and RgαS. (PDF)