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. Author manuscript; available in PMC: 2012 Mar 16.

Published in final edited form as: J Am Chem Soc. 2011 Feb 22;133(10):3390–3400. doi: 10.1021/ja1072178

(a, b) Transmission electron microscopy images of Aβ(1–40) fibrils (a) without and (b) with Cu²⁺, which is 0.4 molar equivalence (eq.) to Aβ. Cu²⁺ ions were added after the fibril formation was complete throughout this work. (c) Comparison of 1D ¹³C CPMAS spectra of Aβ(1–40) fibrils without (black) and with () 0.4 molar eq. of Cu²⁺, together with signal assignments. The samples were labeled with uniformly ¹³C-, ¹⁵N-labeled amino acids at V12, F20, A21, I31, G33 and with ¹³C_εH₃ selectively labeled at M35. (d) Comparison of the 2D ¹³C/¹³C correlation spectra for the same fibrils samples without (black) and with () Cu²⁺. The spectra were obtained at magic angle spinning (MAS) at 20 kHz. In (d), a fpRFDR sequence of 1.6 ms⁸⁷ was used for ¹³C-¹³C exchange.

Inline graphic — (a, b) Transmission electron microscopy images of Aβ(1–40) fibrils (a) without and (b) with Cu²⁺, which is 0.4 molar equivalence (eq.) to Aβ. Cu²⁺ ions were added after the fibril formation was complete throughout this work. (c) Comparison of 1D ¹³C CPMAS spectra of Aβ(1–40) fibrils without (black) and with () 0.4 molar eq. of Cu²⁺, together with signal assignments. The samples were labeled with uniformly ¹³C-, ¹⁵N-labeled amino acids at V12, F20, A21, I31, G33 and with ¹³C_εH₃ selectively labeled at M35. (d) Comparison of the 2D ¹³C/¹³C correlation spectra for the same fibrils samples without (black) and with () Cu²⁺. The spectra were obtained at magic angle spinning (MAS) at 20 kHz. In (d), a fpRFDR sequence of 1.6 ms⁸⁷ was used for ¹³C-¹³C exchange.