Abstract
Membrane lipid composition plays a central role in establishing the physical characteristics of cellular membranes and changes in this composition initiate important cell signaling events such as platelet aggregation and apoptosis. One of these changes is the collapse of lipid asymmetry across the membrane carried out by members of the Ca2+-activated transmembrane protein 16 (TMEM16) family of lipid scramblases. Previously, we performed brute-force, all-atom molecular dynamics (MD) simulations on the fungal nhTMEM16 and showed that the protein transported zwitterionic 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC) lipids from one leaflet to the other in an irregular cycle of building and collapsing lipid “stacks” within the protein’s membrane-exposed hydrophilic groove.
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