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. Author manuscript; available in PMC: 2009 Apr 10.
Published in final edited form as: Biochemistry. 2008 Oct 2;47(43):11340–11347. doi: 10.1021/bi801503r

Fig. 9. Model of two possible conformations of apoA-I at the surface of a spherical lipid particle.

Fig. 9

At high apoA-I surface concentration, the N-terminal helix bundle remains closed and out of contact with the lipid surface (left). At low surface coverage where a greater surface area is available, the helix bundle is open so that the α-helices can make contact with the lipid surface (right). Cholesterol content in the lipid surface also modulates the equilibrium between the two conformations.