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Mahsa Mofidi, Chris Edelmaier, Abhilash Sahoo, Sonya M. Hanson, Ehssan Nazockdast (Department of Applied Physical Sciences, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599)
Septins are a class of cytoskeletal proteins that preferentially bind to areas of positive micron-scale curvature on cellular membranes. Studies have shown that the amphipathic helix (AH) domain on the septin oligomer is indispensable for its micron-scale curvature sensing [1]. Yet, the underlying mechanism of this AH-mediated curvature sensing remains ambiguous. Here we take the first step towards understanding this mechanism, by studying the interactions of AH domain with planar membranes, using all atom simulations. Our results show that (a) the extended AH tends to remain helical when it is unbound in the solution; (b) the AH approaches lipid head groups through charged interactions of its flanking C-terminal amino acids; and (c) the ending parts of the bound AH appear to dissociate from the membrane, while the rest of the AH remains bound to the membrane.