TABLE 2.

Optimized hydrophobicity calculation using the Wertz-Scheraga scalea

RankSignal sequenceWS score
1TorT0.758
2SfmC0.75
4TraU0.737
7FocC0.731
8TreA0.722
10CcmH0.72
11FecB0.718
12YraI0.718
13TolB0.712
16AsmA0.708
19NikA0.703
24FlgI0.698
26DsbA0.691
27AppA0.69
33PcoE0.683
34BtuF0.682
44PapJ0.673
46YbcL0.672
53DsbC0.667
58ArtJ0.664
62ArtI0.662
65YraP0.659
71YcfS0.658
72FlgA0.656
76LivK0.654
83Agp0.652
92ModA0.649
93MalE0.648
94PhoA0.648
104LivJ0.643
119FepB0.635
122EcoT0.633
142MepA0.621
155AnsB0.61
158Ivy0.608
  • a The hydrophobicities of the signal sequences of the proteins listed fused to thioredoxin-1 were calculated using the Wertz-Scheraga (WS) scale (44) with a window length of 12 amino acids. The relative hydrophobicities compared to the 171 other signal sequences in our data set are listed, with a rank of 1 being the most hydrophobic. Signal sequences that promote SRP-dependent export of thioredoxin are shown in boldface type.