Figure 2 | Scientific Reports

Figure 2

From: High-resolution NMR characterization of low abundance oligomers of amyloid-β without purification

Figure 2

RFDR-based 2D 1H/1H chemical shift correlation spectra of freshly dissolved (red) and aggregated (blue) forms of Aβ1-40.

(a) Side-chain to Hα, (b) side-chain and (c) Hβ-Hα and Hα -Hα regions of the overlaid 2D spectra were recorded under 2.7 kHz MAS. The dotted circle highlights the Ser and Gly fingerprints of the aggregated Aβ1-40 sample. Peak assignments are given for the mixed Aβ1-40 sample. The spectra were acquired with a 50 ms mixing time at 600 MHz in 100% D2O, 10 mM sodium phosphate buffer, pH 7.4 and 37 °C. Total Aβ1-40 concentrations for both samples were 462 μM; the estimated oligomer concentration in the aggregated sample is 35 ± 12 μM. The acquisition time was 4 days.

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