Table 1 13C ssNMR chemical shifts and linewidths in frozen solutions of Aβ40 in monomeric (mono), oligomeric (oligo), and fibrillar (fib) states, determined from 2D 13C-13C ssNMR spectra in Figs. 3 and 4
From: Early events in amyloid-β self-assembly probed by time-resolved solid state NMR and light scattering
Residue | CO | Cα | Cβ | Cγ | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
mono | oligo | fib | coil | mono | oligo | fib | coil | mono | oligo | fib | coil | mono | oligo | fib | Coil | |
V18 | 175.6 ± 2.1 | 174.2 ± 2.0 | nd | 176.3 | 62.5 ± 2.5 | 61.0 ± 1.8 | nd | 62.2 | 34.5 ± 2.5 | 36.0 ± 2.0 | nd | 32.9 | 22.4 ± 2.7 | 22.0 ± 2.9 | nd | 21.1, 20.3 |
F19 | ur | ur | 173.4 ± 1.2 | 175.8 | 58.5* | 57.0 ± 2.0 | 56.3 ± 1.8 | 57.5 | 40.3 ± 2.8 | 42.6 ± 3.0 | 44.3 ± 1.3 | 39.6 | ||||
V24 | 176.1 ± 2.7 | ur | 174.8 ± 1.5 | 176.3 | 63.3 ± 3.0 | 61.7 ± 2.5 | 60.8 ± 1.3 | 62.2 | 32.0* | 33.0 ± 3.0 | 35.7* | 32.9 | ur | ur | 21.3* | 21.1, 20.3 |
G25 | 175.5 ± 2.7 | 174.7 ± 2.4 | 173.6 ± 1.6 | 174.9 | 45.7 ± 1.9 | 45.5 ± 2.5 | 47.0 ± 2.1 | 45.1 | ||||||||
S26 | 174.3 ± 1.6 | 174.3 ± 2.0 | 174.5 ± 2.7 | 174.6 | 58.6 ± 2.7 | 58.5 ± 2.0 | 58.0 ± 2.0 | 58.3 | 64.0 ± 2.4 | 64.0 ± 3.0 | 66.2 ± 2.4 | 63.8 | ||||
A30 | 177.7 ± 2.2 | 175.6 ± 2.0 | 175.3 ± 1.6 | 177.8 | 53.5 ± 1.5 | 52.1 ± 1.8 | 52.3 ± 1.0 | 52.5 | 20.5 ± 2.5 | 22.2 ± 3.4 | 20.2 ± 1.4 | 19.1 | ||||
I31 | 176.1 ± 2.7 | 175.6 ± 2.0 | 174.8 ± 1.5 | 176.4 | 62.3* | 60.6 ± 2.3 | 60.8 ± 1.2 | 61.1 | 39.0 ± 2.8 | 42.3 ± 2.5 | 41.2 ± 1.5 | 38.8 | ur | 28.6 ± 3.6, 17.4 ± 3.2 | 28.6 ± 1.6,18.8* | 27.2, 17.4 |
G33 | 173.9 ± 2.6 | 170.7 ± 1.6 | nd | 174.9 | 46.1 ± 1.8 | 44.9 ± 1.9 | nd | 45.1 | ||||||||
L34 | 176.2 ± 2.5 | ur | 173.4 ± 1.5 | 177.6 | 56.2 ± 2.8 | ur | 56.2 ± 1.9 | 55.1 | 42.0 ± 3.4 | 45.5 ± 3.5 | 41.4 ± 1.8 | 42.4 | 27.5 ± 2.9 | 28.8 ± 3.0 | 28.6 ± 1.2 | 26.9 |
M35 | 177.3 ± 2.3 | 174.7 ± 2.9 | 173.4 ± 1.5 | 176.3 | 55.2 ± 2.8 | 54.6 ± 1.5 | 55.0 ± 1.2 | 55.4 | ur | ur | 36.1* | 32.9 | ur | ur | 33.0* | 32.0 |
