Table 5 Hydrophobicity parameters
From: 50 years of amino acid hydrophobicity scales: revisiting the capacity for peptide classification
Index | Name | Description |
|---|---|---|
0 | Max. exact β-strand score (EBSS) | Parameter to score the probability of a sequence with ≥10 AA to be a TM β-sheet [16] |
1 | Min. exact β-strand score (EBSS) | |
2 | Max. alternating hydrophobicity | High alternating hydrophobicity probing for polar and unpolar AA alternation typical for transmembrane β-sheets [14, 15] |
3 | Min. alternating hydrophobicity | |
4 | Max. hydrophobicity-moment α | Analyzing the distribution of hydrophobicity considering the amino acid distribution in α-helices with an angle between amino acids of 100° to probe for potential to form a TM α-helix [13] |
5 | Min. hydrophobicity-moment α | |
6 | Max. hydrophobicity-moment β | Analyzing the distribution of hydrophobicity considering the amino acid distribution of β-sheets with an angle between amino acids of 180° to probe for potential to form a TM β-sheet [13] |
7 | Min. hydrophobicity-Moment β | |
8 | Max. average hydrophobicity | Average hydrophobicity of the peptide [33] |
9 | Min. average hydrophobicity |