TABLE 3.
The protein structure statistics of the MERS CoV inhibitor peptides.
| ID | α-helix (residues range) | α-helix % | Counts of residues | Frequency of residues | |||||
|---|---|---|---|---|---|---|---|---|---|
| Negative charge | Positive charge | Non-charged | Hydrophobic | Hydrophilic | Other | Half-life in mammals (h) | |||
| # 1 | 2–34 | 91.7 | 5 | 2 | 29 | 15 | 14 | 7 | 1.9 |
| # 2 | 2–34 | 91.7 | 4 | 2 | 30 | 15 | 14 | 7 | 1.9 |
| # 3 | 2–34 | 91.7 | 5 | 3 | 28 | 14 | 14 | 8 | 1.9 |
| # 4 | 2–34 | 91.7 | 6 | 2 | 28 | 15 | 13 | 8 | 1.9 |
| # 5 | 2–34 | 91.7 | 6 | 2 | 28 | 15 | 13 | 8 | 1.9 |
| # 6 | 2–34 | 91.7 | 5 | 2 | 29 | 15 | 13 | 8 | 1.9 |
| # 7 | 2–34 | 91.7 | 5 | 2 | 29 | 15 | 13 | 8 | 1.9 |
| # 8 | 2–34 | 91.7 | 6 | 2 | 28 | 15 | 13 | 8 | 1.9 |
| # 9 | 2–34 | 91.7 | 6 | 3 | 27 | 14 | 13 | 9 | 1.9 |
| # 10 | 2–34 | 91.7 | 8 | 3 | 25 | 14 | 11 | 11 | 1.9 |
| # 11 | 2–34 | 91.7 | 8 | 4 | 24 | 13 | 11 | 12 | 1.9 |
| # 12 | 2–34 | 91.7 | 9 | 4 | 23 | 12 | 11 | 13 | 1.9 |