Figure 8.

(A) Experimental (symbols) and simulated (solid and dashed lines) ¹⁵N fpRFDR-CT data for amylin fibrils with AMY07, AMY08, AMY09, and AMY11 isotopic labeling patterns, detected through ¹³C NMR signals of C_α sites in the indicated residues. The experimental data serve as constraints on the backbone ψ torsion angles of residues in parentheses. Simulations are for ψ values ranging from ±30° (most rapidly decreasing solid line) to ±170° (least rapidly decreasing dashed line), in ±20° steps. Data for AMY07, AMY08, and AMY09 were obtained at 100.8 MHz ¹³C NMR frequency and 20.00 kHz MAS frequency. Data for AMY11 were obtained at 150.7 MHz ¹³C NMR frequency and 15.00 kHz MAS frequency. (B) ¹³C NMR spectra from which AMY08 (left) and AMY11 (right) data were obtained, with ¹⁵N dipolar evolution periods and assignments of ¹³C_α lines indicated.