Esteras-Chopo et al. 10.1073/pnas.0505905102.

Supporting Information

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Supporting Text
Supporting Figure 4
Supporting Figure 5
Supporting Figure 6
Supporting Figure 7
Supporting Figure 8
Supporting Figure 9
Supporting Figure 10
Supporting Figure 11




Supporting Figure 4

Fig. 4. Electron micrographs of AmyBergerac (AMYBG) (pH 2.6, c » 70 mM, and t = 3 months). (a) Incubation at room temperature. (b) Incubation at 37°C. The black arrows point to some of the numerous nuclei that can be found in this sample. Figure corresponds to Stability of a–SH3 Proteins with Amyloidogenic Insertions.





Supporting Figure 5

Fig. 5. Binding of thioflavin (ThT) to mature fibrils of 1-SH. Figure corresponds "Conformational Transition and Amyloid Fibril Formation of a–SH3 Variants with Amyloidogenic Insertions.





Supporting Figure 6

Fig. 6. Far-UV (Left) and near-UV (Right) evolution of all a-SH3 variants studied in this work (t = 0 and 3 months). Electron micrographs of the C-terminus variants are also shown (magnification: 89,000). Figure corresponds to Conformational Transition and Amyloid Fibril Formation of a–SH3 Variants with Amyloidogenic Insertion.





Supporting Figure 7

Fig. 7. CD (a) and EM (b) analysis of the insoluble (b1) and soluble (b2) fractions of Ab-SH samples (pH 2.6, c » 300 mM, t = 8 months, and room temperature). Figure corresponds Conformational Transition and Amyloid Fibril Formation of a–SH3 Variants with Amyloidogenic Insertions.





Supporting Figure 8

Fig. 8. Far-UV CD of a 300-mM solution of 1-SH incubated for 18 months at pH 2.6 and room temperature. Figure corresponds to Conformational Transition and Amyloid Fibril Formation of a–SH3 Variants with Amyloidogenic Insertions.





Supporting Figure 9

Fig. 9. Effect of phosphate salts (between 1 and10 mM) in 1-SH amyloid fibril formation. Far-UV CD and electron micrograph of a 300-mM sample incubated for 6 days at pH 2.6 and room temperature.Figure corresponds to Conformational Transition and Amyloid Fibril Formation of a–SH3 Variants with Amyloidogenic Insertions.





Supporting Figure 10

Fig. 10. Isolation of the protease-resistant core of mature fibrils. (a) Extensive pepsin proteolysis of 1-SH mature fibrils isolated by ultracentrifugation. (b) MS characterization of the insoluble fraction of the proteolysis reaction of 1-SH and result of the sequencing. Figure corresponds to Isolation of the Protease-Resistant Core of 1-SH Fibrils.





Supporting Figure 11

Fig. 11. Aminopeptidase resistance of 1-SH mature fibrils. The peaks corresponding to the reaction products are labeled with the name of the species. Figure corresponds to Isolation of the Protease-Resistant Core of 1-SH Fibrils.