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. Author manuscript; available in PMC: 2016 Sep 23.
Published in final edited form as: Biochemistry. 2016 Sep 7;55(37):5272–5278. doi: 10.1021/acs.biochem.6b00649

Figure 2.

Figure 2

(a) Ribbon diagram representation of TTR monomer and labeling schemes for the solid-state NMR experiments. The 13CO (green) and 13Cα (red) carbons of the amino acids are labeled if the internuclear distance in the native TTR tetramer are between 4 and 6 Å. (b) 13C CPMAS spectra of the native and amyloid states of TTR prepared from 13CO-Phe and 13Cα-Tyr labeled TTR. (c) 2D PDSD spectra of the native and amyloid states of TTR with a contour level of 1.5 % with respect to the diagonal peak obtained using a mixing time of 500 ms at a 1H frequency of 830 MHz. * denotes spinning sidebands. For the solid-state NMR experiments, the native tetrameric TTR at pH 7.3 was precipitated using 90 % ammonium sulfate and dried under Ar gas. Both dried native and amyloid samples were rehydrated with 5 μL water.