Table 2.
Amino acid sequence, net charge, hydrophobicity of wild-type and mutants of sprG1312-encoded peptides.
| Amino acid sequencea | Net chargeb | Hydrophobicityb | |
|---|---|---|---|
| SprG144 | MVALLKSLERRRLMITISTMLQFGLFLIALIGLVIKLIELSNKK | 4.98 | 1.01 |
| SprG131 | MITISTMLQFGLFLIALIGLVIKLIELSNKK | 1.98 | 1.39 |
| SprG131∆9 | MITISTMLQFGLFLIALIGLVI | −0.02 | 2.29 |
| SprG131∆2 | MITISTMLQFGLFLIALIGLVIKLIELSN | −0.02 | 1.75 |
| SprG131-K2K3 | MKKITISTMLQFGLFLIALIGLVIKLIELSN | 1.98 | 1.39 |
| SprG131-F10A-F13A | MITISTMLQAGLALIALIGLVIKLIELSNKK | 1.98 | 1.32 |
| SprG131_F10E-F13E | MITISTMLQEGLELIALIGLVIKLIELSNKK | −0.02 | 0.98 |
| SprG131-1xFLAG-Nt | MDYKDDDDKTISTMLQFGLFLIALIGLVIKLIELSNKK | −1.02 | 0.42 |
| SprG131-1xFLAG-Ct | MITISTMLQFGLFLIALIGLVIKLIELSNKKDYKDDDDK | −1.02 | 0.42 |
| SprG131-3xFLAG-Ct | MITISTMLQFGLFLIALIGLVIKLIELSNKKDYKDDDDKDYKDDDDKDYKDDDDK | −7.01 | −0.67 |
a
Hydrophobic amino acids are shown in red, negatively charged amino acids in green and positively charged amino acids in blue. Mutations are underlined.
b
The charge and the hydrophobicity index (based on Kyte-Doolittle scale) have been calculated thanks to the R package «Peptides» (Osorio et al., 2015).