Supplementary Figure 2: Derivation of an all atom model of full-length, lipid-free monomeric apoA-I
From: A consensus model of human apolipoprotein A-I in its monomeric and lipid-free state
Panel (a) shows a single molecule from the reported crystal structure of the apoA-I1–184 dimer. Panel (b) shows the folding of helix 6 previously proposed by Mei et. al.34, and the fold of helix 6 used for the time-averaged structure (right). Panel (c) shows the final time-averaged model. Molecules are colored as previously defined by Mei et. al.34. Purple and cyan represent consensus sequence peptide A and B homology sequences, green represents exon-3-encoded region (residues 1–43) and yellow are prolines.
