TABLE 2.

Optimized hydrophobicity calculation using the Wertz-Scheraga scale^a

Rank	Signal sequence	WS score
1	TorT	0.758
2	SfmC	0.75
4	TraU	0.737
7	FocC	0.731
8	TreA	0.722
10	CcmH	0.72
11	FecB	0.718
12	YraI	0.718
13	TolB	0.712
16	AsmA	0.708
19	NikA	0.703
24	FlgI	0.698
26	DsbA	0.691
27	AppA	0.69
33	PcoE	0.683
34	BtuF	0.682
44	PapJ	0.673
46	YbcL	0.672
53	DsbC	0.667
58	ArtJ	0.664
62	ArtI	0.662
65	YraP	0.659
71	YcfS	0.658
72	FlgA	0.656
76	LivK	0.654
83	Agp	0.652
92	ModA	0.649
93	MalE	0.648
94	PhoA	0.648
104	LivJ	0.643
119	FepB	0.635
122	EcoT	0.633
142	MepA	0.621
155	AnsB	0.61
158	Ivy	0.608

^aThe 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.