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

Abstract

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. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.