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Table 2 Mean amino acid propensities for α-helix and β-strand conformations

From: Dependence of α-helical and β-sheet amino acid propensities on the overall protein fold type

Amino acid

α-helix

β-strand

 

Exposed residues

Buried residues

Total residues

Exposed residues

Buried residues

Total residues

V

0.83

0.89

0.91

2.31

1.57

2.00

I

0.96

1.01

1.04

2.02

1.39

1.79

L

1.16

1.27

1.28

1.18

0.93

1.15

M

1.03

1.29

1.26

1.01

0.84

1.01

P

0.48

0.41

0.44

0.49

0.42

0.40

A

1.43

1.37

1.41

0.48

0.72

0.75

C

0.63

0.85

0.85

1.24

1.07

1.36

F

0.88

0.99

1.00

1.50

1.10

1.4

Y

0.91

0.98

0.98

1.71

1.12

1.37

W

0.87

1.09

1.07

1.90

0.91

1.23

Q

1.34

1.21

1.26

0.96

0.82

0.72

S

0.74

0.80

0.76

0.86

0.85

0.81

T

0.72

0.84

0.78

1.58

1.08

1.21

N

0.74

0.77

0.73

0.71

0.76

0.63

H

0.90

0.85

0.87

1.15

0.98

0.99

D

0.91

0.73

0.82

0.61

0.76

0.55

K

1.25

1.13

1.17

1.14

0.98

0.76

E

1.51

1.25

1.39

0.89

0.86

0.65

R

1.31

1.13

1.21

1.27

0.82

0.85

G

0.28

0.59

0.44

0.41

0.81

0.67