Table 2.
Summary of deuterium number incorporated into Aβ subpeptides or residues from different aggregated states
| Residue(s) | Total exchangeable protons | Deuterium incorporation |
|||
|---|---|---|---|---|---|
| Monomer∗ | LMW∗ | HMW† | Fibril‡ | ||
| 1–16§ | 15 | 15.2 ± 0.4 | 15.2 ± 0.4 | 14.7 ± 0.3 | 8.2 ± 0.3 |
| 17–19¶ | 3 | 2.8 ± 0.6 | 2.8 ± 0.6 | 0.9 ± 0.5 | 0.6 ± 0.4 |
| 21–23¶ | 3 | 3.1 ± 0.4 | 0.8 ± 0.5 | 0.2 ± 0.4 | 0.1 ± 0.3 |
| 24–33‖ | 10 | 9.7 ± 0.5 | 6.9 ± 0.6 | 5.5 ± 0.4 | 5.1 ± 0.3 |
| 34¶ | 1 | 1.1 ± 0.4 | 0.9 ± 0.4 | 0.2 ± 0.4 | 0.3 ± 0.1 |
| 35¶ | 1 | 0.9 ± 0.1 | 0.3 ± 0.1 | 0.3 ± 0.1 | 0.2 ± 0.1 |
| 36–40§ | 5 | 4.8 ± 0.1 | 3.7 ± 0.1 | 3.6 ± 0.1 | 3.7 ± 0.1 |
Uncertainties are calculated by error propagation.
∗
Aβ(1-40) monomer and LMW oligomers from fresh sample, labeled for 10 s.
†
Spherical HMW oligomers from 4-h aged samples, labeled for 1 h.
‡
Washed fibrils from 6-day aged sample, labeled for 24 h.
§
Values are determined from direct measurement of reporter peptides 1-16 and 35-40, respectively.
¶
Values are determined from labeling difference between partially overlapping peptide pairs.
‖
Value is determined by subtracting the deuterium number of residues 21–23 from reporter peptide 20-33.