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Table 3 Improvement of protein secondary structure prediction with the addition of a "residue-specific" RSA threshold for Chou-Fasman and HMM method.

From: Impact of residue accessible surface area on the prediction of protein secondary structures

 

Applied Threshold

 

Chou-Fasman

HMM

 

Mean

Median

Mean

Median

A

11.89

10.43

-5.29

-5.41

C

3.33

1.27

4.26

4.93

D

11.73

10.77

5.81

6.66

E

9.16

8.56

-3.55

-3.76

F

-0.32

-0.39

1.12

1.55

G

9.11

6.72

12.79

14.25

H

10.92

12.61

2.83

3.28

I

-0.01

-1.45

0.08

0.41

K

8.31

5.76

0.25

0.35

L

1.08

1.21

-3.53

-3.49

M

0.17

-0.40

-3.60

-3.62

N

8.38

8.71

7.20

8.12

P

12.32

10.08

11.97

13.56

Q

10.35

9.07

-2.55

-2.53

R

9.67

8.32

-1.21

-1.10

S

11.61

7.89

5.07

5.79

T

1.68

0.16

5.22

6.10

V

-0.23

-0.61

2.20

2.50

W

-0.57

-0.71

-0.78

-0.84

Y

0.74

0.68

0.87

1.04

Total Improvement

9.99

8.69

3.37

3.92

 

Applied Threshold

 

Chou-Fasman

HMM

 

Tertile

Mean ± standard deviation

Tertile

Mean ± standard deviation

A

12.15

12.50

-4.31

-2.69

C

2.64

1.76

3.85

2.93

D

13.61

13.17

8.94

6.01

E

10.35

9.48

-1.97

-1.04

F

-0.23

-1.88

-0.17

1.37

G

9.29

8.80

18.48

13.14

H

12.23

11.60

4.48

3.76

I

-0.51

0.09

-0.41

0.21

K

8.20

8.57

1.17

1.34

L

0.72

0.49

-3.35

-1.79

M

1.76

-0.81

-1.42

-1.64

N

8.40

8.46

10.72

7.05

P

12.72

14.91

17.33

11.05

Q

10.40

10.65

-0.73

-0.66

R

9.57

9.99

0.28

0.37

S

10.10

13.09

7.41

5.28

T

0.52

0.60

6.44

5.30

V

-0.28

-0.20

0.97

2.02

W

-0.87

-0.63

-0.50

0.44

Y

0.75

0.92

1.15

1.25

Total Improvement

10.23

10.34

4.32

3.62

  1. The bold-underlined values are those values that show improvements using leave-one-out cross-validation when they are compared with the original method. See the text for more details.