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- W2977337140 abstract "Abstract Parkinson’s disease is associated with the aggregation of the protein α-synuclein. While α-synuclein can exist in multiple oligomeric states, the dimer has been a subject of extensive debates. Here, using an array of biophysical approaches, we demonstrate that α-synuclein in vitro exhibits primarily a monomer-dimer equilibrium in nanomolar concentrations and up to a few micromolars. We then use spatial information from hetero-isotopic cross-linking mass spectrometry experiments as restrains in discrete molecular dynamics simulations to obtain the ensemble structure of dimeric species. Out of eight structural sub-populations of dimers, we identify one that is compact, stable, abundant, and exhibits partially exposed β-sheet structures. This compact dimer is the only one where the hydroxyls of tyrosine 39 are in proximity that may promote dityrosine covalent linkage upon hydroxyl radicalization, which is implicated in α-synuclein amyloid fibrils. We propose that this α-synuclein dimer features etiological relevance to Parkinson’s disease." @default.
- W2977337140 created "2019-10-10" @default.
- W2977337140 creator A5032488236 @default.
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- W2977337140 date "2019-10-07" @default.
- W2977337140 modified "2023-10-18" @default.
- W2977337140 title "Structural and Dynamic Insights Into α-Synuclein Dimer Conformations" @default.
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- W2977337140 doi "https://doi.org/10.1101/795997" @default.
- W2977337140 hasPublicationYear "2019" @default.
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