Table 2.
Structural features changing between wild-type and mutated PRPH2. Protean 3D and CLC Main Workbench results evidenced several structural changes in wild-type versus mutated PRPH2 protein, with details of involved aa.
| Structural Feature | Wild-Type Protein | Mutated Protein |
|---|---|---|
| Weight (da) | 39,186 | 39,271 |
| Absorption at 280nm 0.1% (= 1 g/L) | ||
| Non-reduced cysteines | 1891 | 1895 |
| Reduced cysteines | 1873 | 1877 |
| Count of hydrophobic (A, F, G, I, L, M, P, V, W) residues | 175 | 174 |
| Count of hydrophilic (C, N, Q, S, T, Y) residues | 95 | 96 |
| Pfam domain result | Tetraspanin (aa. 16–287) | |
| Uniprot domain result | Interaction domain with Melanoregulin (MREG) (aa. 341–346) | |
| Instability index | 92, 59 | 88, 72 |
| Amphiphilicity and hydropathy | Changes in aa. 26–28, 106, 181–184, 209, 258–261, 272, 307–315, 336 | |
| Flexibility | 287–305, 309–316 | 287–306, 310–316 |
| Disorder | 286–312, 328–346 | 286–310, 327–346 |
| Surface probability | Three residues (aa. 310–312) | Two residues (aa. 311–312) |
| / | One residue (aa. 335) | |
| Three residues (aa. 341–343) | Four residues (aa. 340–343) | |