Abstract
Using a combination of all-atom and coarse-grained molecular dynamics simulations to interpret a range of x-ray scattering experiments, we aim to understand the role of membrane deformation in the action of the Parkinson's Disease protein, α-Synuclein. Our simulation results have led to the hypothesis that αS flattens curved membranes by screening the repulsive interactions between negatively charged, acidic headgroups, thereby reducing the effective area per headgroup and relieving the inherent positive curvature of the lipids on the outer leaflet of synaptic vesicles. We hope to address the question of whether αS influences a membrane's mechanical properties as a route to evaluating this hypothesis. Additionally, we aim to understand the role of αS in recruiting sub-domains of positively charged lipids. A second, smaller peptide (the CRAC motif from gp41) is also studied in an effort to build the computational tools necessary for matching the x-ray data that is used for calculating a membrane's material properties.
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