Figure 3: 1D 13C ssNMR spectra of uniformly 13C- and 15N-labelled htt exon1 fibrils. | Nature Communications

Figure 3: 1D 13C ssNMR spectra of uniformly 13C- and 15N-labelled htt exon1 fibrils.

From: Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core

Figure 3

(a,d,g) Fibrils were formed at 37 °C, or (b,e,h) 22 °C, and studied using (a–c) cross-polarization (rigid residues), (d–f) direct polarization and (g–i) INEPT-based (mobile residues) MAS ssNMR. (c,f,i) Overlaid aliphatic regions, with assignments indicating the random coil (Prc) and PPII-helical Pro (PII). The NMR measurements were performed at 275 K on a 600 MHz (1H frequency) spectrometer.

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