Table 5.
Relative peptide preorganization free energies.
| Peptide | % Foldedb | ΔΔ GI |
|---|---|---|
| aSdc1 | 5.8/3.8 | 0.0 (0.2) |
| A0F | 3.4/0.3 | 0.9 (0.8) |
| A0N | 3.6/0.6 | 0.7 (0.7) |
| A0M | 4.0/0.8 | 0.6 (0.6) |
| E4K | 5.0/3.2 | 0.1 (0.3) |
| F2I | 1.1/1.1 | 0.9 (0.1) |
| E3D,T1T | 4.6/0.6 | 0.6 (0.7) |
| Sdc2 | 2.0/0.8 | 0.8 (0.4) |
| Sdc3 | 0.7/0.6 | 1.2 (0.1) |
| aCaspr4 | 2.6/8.6 | 0.0 (0.5) |
| aCaspr4-F0A | 5.7/1.6 | 0.3 (0.5) |
| aYAAEKYWA | 8.4/0.1 | 1.0 (1.6) |
ΔGI (kcal/mol) corresponds to step I in Figure 1. Here, we tabulate the relative values ΔΔGI, compared to Sdc1.
a
These peptides were simulated for 2 × 200 ns, the others for 2 × 100 ns.
b
The “folded” peptide has the extended conformation seen in the bound state.