Table 1.
FTIR-based evaluation of secondary structure content in different species of human tau incubated in the absence or presence of heparin and doxycycline for 24 h.
| Samples | Wavenumber (cm−1) | Relative Amide I' contribution | Assignments |
|---|---|---|---|
| Tau | 1,610 | 1.2 | Side chains |
| 1,619 | 4.0 | PPII helix | |
| 1,631 | 15.9 | Low frequency β-sheet | |
| 1,645 | 42.2 | Random coil | |
| 1,658 | 22.1 | α-helix + open loop | |
| 1,671 | 12.9 | β-turn | |
| 1,683 | 1.6 | High frequency β-sheet | |
| Tau:hep | 1,615 | 10.3 | Cross-β |
| 1,632 | 30.6 | Low frequency β-sheet | |
| 1,640 | 15.9 | Random coil | |
| 1,652 | 17.2 | α-helix | |
| 1,662 | 13.6 | Open loop | |
| 1,672 | 8.9 | β-turn | |
| 1,681 | 3.3 | High frequency β-sheet | |
| Tau:hep:DOX | 1,614 | 4.2 | Cross-β |
| 1,626 | 12.9 | Low frequency β-sheet | |
| 1,637 | 27.0 | Random coil | |
| 1,649 | 20.3 | α-helix | |
| 1,659 | 18.4 | Open loop | |
| 1,670 | 14.2 | β-turn | |
| 1,682 | 2.8 | High frequency β-sheet |