Table 2.
Global structural properties of LV-peptides in 80% TFE/water (v/v) (for sequences see Table 1)
| Peptide | fαCD [%]∗ | fαMD [%]† | Cα-RMSD (all) [Å]‡ | Cα-RMSD (core) [Å]‡ |
|---|---|---|---|---|
| A: Increased content of helix-breaking residues | ||||
| L16 | 83.0 ± 3.2 | 80.3 ± 7.5 | 1.7 ± 0.6 | 0.7 ± 0.1 |
| LLV16 | 84.0 ± 3.7 | 79.1 ± 8.8 | 1.9 ± 0.5 | 0.9 ± 0.2 |
| LV16 | 78.0 ± 4.4 | 76.2 ± 9.3 | 1.9 ± 0.5 | 1.0 ± 0.3 |
| VVL16 | 67.0 ± 5.5 | 66.1 ± 12.7 | 2.7 ± 0.7 | 1.4 ± 0.4 |
| LV16-G8P9 | 71.0 ± 6.2 | 71.4 ± 11.9 | 3.7 ± 1.2 | 2.6 ± 0.9 |
| B: 11 Leu / 5 Val unevenly distributed | ||||
| LVL | 62.0 ± 8.8 | 79.2 ± 7.9 | 1.9 ± 0.5 | 1.1 ± 0.3 |
| VLV | 62.0 ± 5.9 | 77.2 ± 6.2 | 2.3 ± 0.4 | 0.9 ± 0.2 |
| L-LV-L | 75.0 ± 5.2 | 78.1 ± 8.7 | 2.3 ± 0.3 | 0.9 ± 0.2 |
| LV-L-LV | 67.0 ± 6.1 | 80.1 ± 7.2 | 1.6 ± 0.4 | 0.8 ± 0.2 |
Given are averages and standard errors taken over nonoverlapping 10 ns time windows.
∗
α-Helix content from CD experiment (10).
†
Average α-helix content from DSSP analysis (72) of the MD trajectories.
‡
RMSD of the Cα atoms relative to an ideal α-helix (all: average over the complete sequence, core: average over Cα atoms from residues 5–20). Rigid-body translations and rotations have been removed via a least-square fitting of the backbone to the reference helix (42,43).