Table 2.
Band Decomposition of FTIR Amide I′ Band at Different Temperatures
| Secondary structure | scFv‐h3D6a | DF‐VH | ||||||
|---|---|---|---|---|---|---|---|---|
| 25°C | 60°C | 25°C | 55°C | |||||
| Center (cm−1) | % Area | Center(cm−1) | % Area | Center (cm−1) | % Area | Center (cm−1) | % Area | |
| ↑ Fr. antip. β‐sheet | 1681 | 9 | 1683 | 4 | 1684 | 5 | 1683 | 6 |
| ↑ Fr. loops/turns | – | – | 1671 | 11 | – | – | 1669 | 15 |
| ↓ Fr. loops/turns | 1660 | 30 | 1662 | 6 | 1663 | 33 | – | – |
| α‐helix | – | – | 1653 | 15 | – | – | – | – |
| Random coil | – | – | 1644 | 14 | – | – | 1648 | 39 |
| ↓ Fr. antip. β‐sheet | 1636 | 60 | 1636 | 16 | 1637 | 60 | 1633 | 12 |
| WL fibril | – | – | 1626 | 23 | – | – | 1627 | 5 |
| Amyloid fibril | 1612b | 1 | 1615 | 9 | 1611b | 2 | 1617 | 24 |
a
Data for the scFv‐h3D6 are already published and are shown only for comparative purposes 13. ↑ Fr, high frequency; ↓ Fr, low frequency; antip, antiparallel.
b
These correspond to side‐chains rather than to amyloid fibrils.