Figure 4 | Scientific Reports

Figure 4

From: Presence of intrinsically disordered proteins can inhibit the nucleation phase of amyloid fibril formation of Aβ(1–42) in amino acid sequence independent manner

Figure 4

Absence of relevant interaction of IDPs with Aβ(1–42), assessed by solution nuclear magnetic resonance (NMR). (A, C, E) Overlay of the 2D 1H–15N HSQC spectra of Aβ(1–42) with various concentration of IDP-C1 at 15 ℃, pH 7.4. Aβ(1–42) (20 µM) with of 0 µM (cyan), 10 µM (red), 20 µM (yellow), 40 µM (green), and 80 µM (blue) of C1 (A), D10 (C), or FK20 (E). (B, D, F) Normalized chemical shift perturbation Δδ derived from 1H–15N HSQC spectra of Aβ(1–42) with 80 µM C1 (B), D10 (D), or FK20 (F) were plotted against residue numbers of Aβ(1–42).

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