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. Author manuscript; available in PMC: 2015 Jun 1.
Published in final edited form as: FEBS J. 2014 Apr 28;281(11):2525–2542. doi: 10.1111/febs.12809

Figure 6.

Figure 6

Residue segments predicted to promote or prevent amyloid formation mapped on the structure of lipid-free apoA-I monomer. Three N-terminal amyloid hot spots predicted in residues 14-22, 53-58, and 69-72 are mapped on the crystal structure of free Δ(185-243)apoA-I [10]. The fourth predicted “hot spot”, 227-232, is in the flexible C-terminal region (irregular line) that forms the primary lipid binding site in apoA-I driving its adsorption to phospholipid surface [18]. Residues 76-81 that are expected to form a β-breaking motif at pH 7 are in purple. Extended segment 44-55 is in red.