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Unfolded annealing molecular dynamics conformers for wild type and disease associated variants of alpha synuclein show no propensity for beta sheetformation

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Figure

Figure 1. At the end of the unfolding MD, wild-type alpha-synuclein still resembles somewhat the initial “candy-cane” structure, while the mutants have assumed
Table 1. Average values for molecular volumes (MV), solvent-accessible surface areas (SASA), and sec-ing and AMD
Figure 3. Secondary structure assignment per residue for the micelle-bound alpha-sybuclein (PDB code 1XQ8), last conformer from NPT MD, and energy-minimized time average AMD conformers of (a) wild-type; (b) A30P; and (c) A53T alpha-synuclein
Figure 4. Number of AMD conformers folded into a particular type of secondary structure at positions (a) 30 and (b) 53 in wild-type (A30 and A53) or disease-associated mutants (A30P and A53T) of alpha-synuclein
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