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. Author manuscript; available in PMC: 2017 Mar 17.
Published in final edited form as: Biochemistry. 2016 Aug 23;55(35):4971–4981. doi: 10.1021/acs.biochem.6b00347

Figure 1.

Figure 1

“Question”: What are the important factors for a compact, folded lipid-free apoA-I molecule to open up and accept lipid? Panel A shows apoA-I in the compact, in-solution conformation (left) and the conformation that it assumes with lipid (right) in rHDL. Panel B illustrates the unique features of lipidated apoA-I generated by cholate dialysis (top) and ABCA1-catalyzed lipidation (bottom). The top panel shows two antiparallel strands of apoA-I on a POPC lipid disc with coincidence of the 5,5′ helices. The bottom panel shows three antiparallel strands that belt a sphere of lipids composed of glycerophospholipid, sphingomyelin, and cholesterol with the 5,5′,5″ helical regions coincident.