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. Author manuscript; available in PMC: 2010 Jan 1.
Published in final edited form as: Annu Rev Biochem. 2009;78:177–204. doi: 10.1146/annurev.biochem.78.082907.145410

Figure 3.

Figure 3

Ultrastructures and models of PrPRES fibrils. A. Negative-stained transmission electron micrographs of proteinase K-treated wild-type or GPI-anchorless PrPRES amyloid fibrils (34). B. Electron micrographs and crystallographically refined images of hexagonal 2D crystals and of proteinase K-treated PrPRES. On the left, the 2D crystals are shown together with fibrils. Adapted from (45). C. Top-down view of PrPRES trimers according to the spiral (47, 48) and β-helix (46) models. Glycans (aqua), α-helices (blue) and β-strands (green) are highlighted. Adapted from (48). D. Parallel, in-register β-sheet model of synthetic fibrils of human PrP residues 120-231. Adapted from (50).