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Table 1 Amino acid physical properties.

From: A four-column theory for the origin of the genetic code: tracing the evolutionary pathways that gave rise to an optimized code

Properties:

1

2

3

4

5

6

7

8

9

Frequency (%)

F – Phe

135

19.80

0.35

5.48

2.8

3.7

218

0.88

5.0

4.39

L – Leu

124

21.40

0.13

5.98

3.8

2.8

180

0.85

4.9

10.15

I – Ile

124

21.40

0.13

6.02

4.5

3.1

182

0.88

4.9

6.95

M – Met

124

16.25

1.43

5.74

1.9

3.4

204

0.85

5.3

2.28

V – Val

105

21.57

0.13

5.96

4.2

2.6

160

0.86

5.6

7.01

S – Ser

73

9.47

1.67

5.68

-0.8

0.6

122

0.66

7.5

6.46

P – Pro

90

17.43

1.58

6.30

-1.6

-0.2

143

0.64

6.6

4.26

T – Thr

93

15.77

1.66

6.16

-0.7

1.2

146

0.70

6.6

5.12

A – Ala

67

11.50

0.00

6.00

1.8

1.6

113

0.74

7.0

7.80

Y – Tyr

141

18.03

1.61

5.66

-1.3

-0.7

229

0.76

5.4

3.30

H – His

118

13.69

51.60

7.59

-3.2

-3.0

194

0.78

8.4

2.03

Q – Gln

114

14.45

3.53

5.65

-3.5

-4.1

189

0.62

8.6

3.45

N – Asn

96

12.28

3.38

5.41

-3.5

-4.8

158

0.63

10.0

4.37

K – Lys

135

15.71

49.50

9.74

-3.9

-8.8

211

0.52

10.1

6.32

D – Asp

91

11.68

49.70

2.77

-3.5

-9.2

151

0.62

13.0

5.19

E – Glu

109

13.57

49.90

3.22

-3.5

-8.2

183

0.62

12.5

6.72

C – Cys

86

13.46

1.48

5.07

2.5

2.0

140

0.91

4.8

1.10

W – Trp

163

21.67

2.10

5.89

-0.9

1.9

259

0.85

5.2

1.09

R – Arg

148

14.28

52.00

10.76

-4.5

-12.3

241

0.64

9.1

5.23

G – Gly

48

3.40

0.00

5.97

-0.4

1.0

85

0.72

7.9

6.77

Weights:

0.000

0.155

0.000

0.028

0.218

0.000

0.277

0.179

0.142

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  1. Definitions of the 9 properties used to construct the distance matrix:
  2. 1. Volume from van der Waals radii [32].
  3. 2. Bulkiness – a measure of the shape of the side chain [33].
  4. 3. Polarity – a measure of the electric field strength around the molecule [33].
  5. 4. Isoelectric point [33].
  6. 5. Hydrophobicity scale [34].
  7. 6. Hydrophobicity scale [35].
  8. 7. Surface area accessible to water in an unfolded peptide [36].
  9. 8. Fraction of accessible area lost when a protein folds [37].
  10. 9. Polar requirement [30].
  11. The frequencies column shows the mean percentage of each amino acid in the protein sequences of modern organisms [6].