TABLE 3.
Primary sequences and physicochemical properties of Library 3 peptides, which correspond to W-position III shown in Figures 1G–I.
| Name | Trp (W) | Sequence | Length (r) | Chargea | H | μH | 
| E20 | 3 | VV RR WR RR WR RW | 12 | 7 | 0.177 | 0.904 | 
| E18 | 3 | WV RR WR RV VR RW RR | 14 | 8 | 0.166 | 0.914 | 
| E15 | 3 | VV RR WR RV VR RW RR RW | 16 | 9 | 0.159 | 0.86 | 
| E12 | 3 | WV RR WR RV VR RW RR VV RR | 18 | 10 | 0.153 | 0.865 | 
| E9 | 3 | RW VR RW RR VV RR WR RV VR RV | 20 | 11 | 0.148 | 0.864 | 
| E6 | 3 | RR WV RR WR RV VR RW RR VV RR VV | 22 | 12 | 0.144 | 0.834 | 
| E3 | 3 | RR VV RR WR RV VR RW VR VW RR VV RR | 24 | 13 | 0.141 | 0.824 | 
| E22 | 4 | RR WV RV WR RW WR | 12 | 6 | 0.448 | 1.002 | 
| E34 | 4 | RR WV RV WR RW VR RW | 14 | 7 | 0.399 | 0.995 | 
| E33 | 4 | RR WV RV WR RW WR RV | 14 | 7 | 0.399 | 0.962 | 
| E37 | 4 | RR WV RV WR RW VR VW RR | 16 | 8 | 0.363 | 0.931 | 
| E40 | 4 | RR WV RV WR RW VR RW RR VV | 18 | 9 | 0.334 | 0.923 | 
| E43 | 4 | RR WV RV WR RW VR VW RR VV RR | 20 | 10 | 0.311 | 0.884 | 
| E46 | 4 | RR WR RV VR RW VR VW RR WV RR VR | 22 | 12 | 0.191 | 0.87 | 
| E47 | 4 | RR WR RV VR RW VR VW RR VV RR WR | 22 | 12 | 9.191 | 0.88 | 
| E50 | 4 | RR WR RV VR RW VR VW RR VV RR WR RV | 24 | 13 | 0.184 | 0.873 | 
| E87 | 5 | RR WV RV WR RW WR RW | 14 | 7 | 0.473 | 1.035 | 
| E92 | 5 | RR WV RW WR RW VR VW RR | 16 | 8 | 0.427 | 0.955 | 
| E96 | 5 | RR WV RV WR RW VR RW RR VW | 18 | 9 | 0.391 | 0.966 | 
H (hydrophobicity) and μH (hydrophobic moment) were determined using the online peptide modeling software heliquest.ipmc.cnrs.fr/; peptides of the same length are minor positional variants of W; r, residues.
The sequences were modeled as idealized amphipathic helices based on helical wheel diagrams using the online modeling software Heliquest, which also provides the physicochemical properties listed in the table.
aAll charges are positive.