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Dynamic properties of human $$alpha$$-synuclein related to propensity to amyloid fibril formation

Fujiwara, Satoru*; Kono, Fumiaki*; Matsuo, Tatsuhito*; Sugimoto, Yasunobu*; Matsumoto, Tomoharu*; Narita, Tetsuhiro*; Shibata, Kaoru 

$$alpha$$-synuclein ($$alpha$$Syn) is an intrinsically disordered protein (IDP) with unknown function. $$alpha$$Syn is known to form amyloid fibrils, which are implicated with the pathogenesis of Parkinson's disease and other synucleinopathies. Elucidating the mechanism of fibril formation of $$alpha$$Syn is therefore important for understanding the mechanism of the pathogenesis of these diseases. Here, using the quasielastic neutron scattering (QENS) and small-angle X-ray scattering (SAXS) techniques, we investigated the dynamic and structural properties of $$alpha$$Syn. These results imply that fibril formation of $$alpha$$Syn requires not only the enhanced local motions but also the segmental motions such that the proper inter-molecular interactions are possible.

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Category:Biochemistry & Molecular Biology

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