Ideas of Order for Amyloid Fibril Structure Ronald Wetzel  Structure  Volume 10, Issue 8, Pages 1031-1036 (August 2002) DOI: 10.1016/S0969-2126(02)00809-2

Figure 1 β-Helical Portions of Globular Proteins (A) Residues 1–178 of the left-handed parallel β-helical protein UDP-N-acetylglucosamine acyltransferase (Protein Data Bank code 1lxa). (B) Residues 261–427 of the right-handed parallel β-helical protein P.69 pertactin (1dab). Models were constructed in Viewer Lite (Accelerys). Structure 2002 10, 1031-1036DOI: (10.1016/S0969-2126(02)00809-2)

Figure 2 β Sheet and Packing Structure in a Left-Handed (A–C) and Right-Handed (D–F) β Helix Two rungs of helix showing β strands and turn regions ([A], residues 17–57 of 1lxa; [D], residues 261–307 of 1dab). Ball and stick models of the same two rungs of helix ([B], 1lxa; [E], 1dab) with amino acids colored to indicate chemical similarities (hydrophobics, green; neutral hydrophilics, beige; acidics, red; basics, blue; Gly and Pro residues, purple) and water oxygens colored cyan. CPK representations of the same two rungs of helix ([C], 1lxa; [F], 1dab) are shown with the same color code. Models were constructed in Viewer Lite (Accelerys). Structure 2002 10, 1031-1036DOI: (10.1016/S0969-2126(02)00809-2)

Figure 3 Some Structural Features of Globular Proteins May Suppress Amyloid Formation A C-terminal cluster of α helices (red) may help cap the β helix of UDP N-acetylglucosamine acyltransferase (1lxa) and prevent its oligomerization into a polymeric, extended β sheet structure. Model was constructed in Viewer Lite (Accelerys). Structure 2002 10, 1031-1036DOI: (10.1016/S0969-2126(02)00809-2)