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Direct Evidence of Coexisting Horseshoe and Extended Helix Conformations of Membrane-Bound Alpha-Synuclein



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Good luck! The physiologically relevant conformation of membrane-bound α-Synuclein (αS) can be either a horseshoe or an extended helix structure. Experimental data obtained by site-directed spin labeling in combination with pulsed electron paramagnetic resonance provide compelling evidence of the coexistence of the horseshoe structure and an extended helix of αS bound to a membrane surface, and potentially resolve the debate on the structure of membrane-bound αS.

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