Table 1.
Prediction of the secondary structure § and physicochemical properties of the peptides.
| Peptide | JPred4 (Jnetpred) | Predict Protein (RePROF) | DBAASP v3.0 (MF Scale) | |||
|---|---|---|---|---|---|---|
| µHn | Hn | Z | I0 | |||
| R23R vs. R23R* | ||||||
| RKKRRQRRRGGGGLHITDMAWKR | β-strand 14–18 a.a. (LHITD) | Helix 2–9 a.a. (KKRRQRRR), β-strand 14–18 a.a. (LHITD) | 0.36 | 0.91 | +9 | 12.51 |
| RKKRRQRRRGG-Sar §§(A)-GLHITD-Nle §§§(M)-AWKR | Helix 2–9 a.a. (KKRRQRRR), other 10–14 a.a. (GGAGL), helix 18–22 (DMAWK) | 0.32 | 0.84 | +9 | 12.51 | |
| RKKRRQRRRGG-Sar(A)-GLHITD-Nle(L)-AWKR | β-strand 14–18 a.a. (LHITD) | Helix 2–9 a.a. (KKRRQRRR), other 10–14 a.a. (GGAGL), helix 18–22 (DMAWK) | 0.29 | 0.79 | +9 | 12.51 |
| RKKRRQRRRGG-Sar(P)-GLHITD-Nle(M)-AWKR | Helix 2–9 a.a. (KKRRQRRR), other 10–14 a.a. (GGAGL) | 0.29 | 0.77 | +9 | 12.51 | |
| RKKRRQRRRGG-Sar(P)-GLHITD-Nle(L)-AWKR | Helix 2–9 a.a. (KKRRQRRR), other 10–14 a.a. (GGPGL) | 0.27 | 0.73 | +9 | 12.51 | |
| R23L vs. R23L* | ||||||
| RKKRRQRRRGGGGITDFGIFIGL | β-strand 17–21 a.a. (FGIFI) | Helix 3–9 a.a. (KRRQRRR), other 10–15 a.a. (GGGGIT), β-strand 16–21 a.a. (DFGIFI) | 0.24 | 0.18 | +7 | 12.41 |
| RKKRRQRRRGG-Sar(A)-GITDFGIFIGL | β-strand 17–21 a.a. (FGIFI) | Helix 3–9 a.a. (KKRRQRRR), other 10–15 a.a. (GGAGIT) | 0.18 | 0.11 | +7 | 12.41 |
| RKKRRQRRRGG-Sar(P)-GITDFGIFIGL | β-strand 17–21 a.a. (FGIFI) | Helix 3–9 a.a. (KKRRQRRR), other 10–15 a.a. (GGPGIT) | 0.14 | 0.04 | +7 | 12.41 |
§ The predicted secondary structure elements of length ≥5 a.a. §§ For calculations, sarcosine (Sar) was replaced by analogs similar in properties and structure: alanine (A) and proline (P). §§§ For calculations, norlecine (Nle) was replaced by analogs of similar properties and structure: methionine (M) and leucine (L). µHn is the normalized hydrophobic moment, Hn is the normalized hydrophobicity, Z is the value of charge at pH 7, I0 is the value of isoelectric point.