Protein Folding：蛋白质折叠.ppt

* Figure 6 Models for protofilament packing. (a) A twisted pair of rectangular protofilaments in which an interactive surface is colored purple. The protofilament twist accompanies the filament twist. (b) A supercoiled pair of protofilaments in which the regions involved in packing interactions rotate around each protofilament. In the correlated twist model a, interacting regions would be fixed relative to the cross-β structure, and other regions could accommodate large loops and/or folded domains that would not interfere with protofilament packing. Similar models can be constructed with more than two protofilaments, in which the cross section rotates as a rigid unit in the helical structure. Keeping the cross section fixed means that all packing contacts can be preserved in the helical fibril. This is the case for the four-protofilament model in Fig. 5 e. PNAS. 2002;99(14):9196-201 * Figure 1? Recent three-dimensional structural models of fibrillar aggregates from different sources. (a) The protofilament of Aβ viewed down the long axis of the fibril. The segments 12–24 (red) and 30–40 (blue) are shown. (b) The fibril from the C-terminal domain 218–289 of the fungal prion protein HET-s The ribbon diagram shows the four β-strands (orange) (residues 226–234, 237–245, 262–270, and 273–282) and the long loop between β2 and β3 from one molecule. Flanking molecules along the fibril axis (gray) are shown. (c) Atomic structure of the microcrystals assembled from the GNNQQNY peptide. Each β-strand is a peptide molecule. (d) The protofilament from amylin. Green, yellow, and pink β-strands indicate residues 12–17, 22–27, and 31–37, respectively. The unstructured N-terminal tail is shown on the right of the panel along with the disulfide bridge between Cys2 and Cys7. (e) The fibril from the NM region of Sup35p. The colored ribbons indicate residues 25–38 (red), 39–90 (blue), and 91–106 (green). The unstructured regions 1–20 (red dashed lines) and 158–250 (black dashed lines)