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. 2001 Jan;10(1):212–219. doi: 10.1110/ps.30301

Table 1.

Hydrophobicitya and helicityb scales, determined experimentally from the properties of KKAAAXAAAAAXAAWAAXAAAKKKK-amide peptides, and used in development of TM finder

AA Hydrophobicitya Helicityb KDc GESd Eisenberge
F 5.00 (1) 1.26 (4) 2.8 (4) 3.7 (1) 1.19 (2)
W 4.88 (2) 1.07 (10) −0.9 (11) 1.9 (7) 0.81 (5)
L 4.76 (3) 1.28 (2) 3.8 (3) 2.8 (4) 1.06 (4)
I 4.41 (4) 1.29 (1) 4.5 (1) 3.1 (3) 1.38 (1)
M 3.23 (5) 1.22 (6) 1.9 (6) 3.4 (2) 0.64 (6)
V 3.02 (6) 1.27 (3) 4.2 (2) 2.6 (5) 1.08 (3)
C 2.50 (7) 0.79 (19) 2.5 (5) 2 (6) 0.29 (9)
Y 2.00 (8) 1.11 (8) −1.3 (12) −0.7 (13) 0.26 (10)
A 0.16 (9) 1.24 (5) 1.8 (7) 1.6 (8) 0.62 (7)
T −1.08 (10) 1.09 (9) −0.7 (9) 1.2 (9) −0.05 (12)
E −1.50 (11) 0.85 (18) −3.5 (18) −8.2 (17) −0.74 (15)
D −2.49 (12) 0.89 (16) −3.5 (17) −9.2 (19) −0.9 (18)
Q −2.76 (13) 0.96 (13) −3.5 (15) −4.1 (15) −0.85 (17)
R −2.77 (14) 0.95 (14) −4.5 (20) −12.3 (20) −2.53 (20)
S −2.85 (15) 1.00 (11) −0.8 (10) 0.6 (11) −0.18 (13)
G −3.31 (16) 1.15 (7) −0.4 (8) 1.0 (10) 0.48 (8)
N −3.79 (17) 0.94 (15) −3.5 (16) −4.8 (16) −0.78 (16)
H −4.63 (18) 0.97 (12) −3.2 (14) −3 (14) −0.4 (14)
P −4.92 (19) 0.57 (20) −1.6 (13) −0.2 (12) 0.12 (11)
K −5.00 (20) 0.88 (17) −3.9 (19) −8.8 (18) −1.5 (19)

a Hydrophobicity of each guest ``X'' residue, scaled from HPLC retention times (Liu and Deber 1998a).

b Nonpolar phase helical propensity of each guest ``X'' residue, scaled from circular dichroism measurements of peptides in n-butanol (Liu and Deber 1998b; Wang et al. 1999).

c Kyte and Doolittle (1982).

d Engelman et al. (1986).

e Eisenberg et al. (1984).