Figure 8
From: Identification of key regions and residues controlling Aβ folding and assembly
Secondary structure dynamics of WT and singly substituted variants of Aβ42. Twenty μM Aβ42 was prepared in 10 mM sodium phosphate, pH 7.4, and incubated with shaking at 37 °C. Secondary structure dynamics were assessed using CD during 994 h of incubation. Panels are (A) WT, (B) D-H14, (C) D-F20, (D) D-A21, and (E) D-M35. (F) Spectra of WT and substituted variants at the end of the assembly process. (G) Molar ellipticity for each peptide was determined at that wavelength at which the molar ellipticity was at a minimum in the final secondary structure formed. Lines obtained from linear regression analysis of the data were used to determine assembly rates dθ/dt. Numbers adjacent to each line are the calculated rates in kdeg cm2 dmol−1/hour.
