The Amino Acid Repository

Individual properties and images of amino acidsa

Properties and images (name: NIST WebBook, three letter code: GIF, one letter code: VRML)

amino acid     

mass 

surface b

volume c

pKa d

pI e

solubility e

density e
Alanine ALA

A

71.09

115

88.6

-

6.107

16.65

1.401
Arginine ARG

R

156.19

225

173.4

~12

10.76

15

1.1
Aspartic Acid ASP

D

114.11

150

111.1

4.5

2.98

0.778

1.66
Asparagine ASN

N

115.09

160

114.1

-

-

3.53

1.54
Cysteine CYS

C

103.15

135

108.5

9.1-9.5

5.02

very

-
Glutamic Acid GLU

E

129.12

190

138.4

4.6

3.08

0.864

1.460
Glutamine GLN

Q

128.14

180

143.8

-

-

2.5

-
Glycine GLY

G

57.05

75

60.1

-

6.064

24.99

1.607
Histidine HIS

H

137.14

195

153.2

6.2

7.64

4.19

-
Isoleucine ILE

I

113.16

175

166.7

-

6.038

4.117

-
Leucine LEU

L

113.16

170

166.7

-

6.036

2.426

1.191
Lysine LYS

K

128.17

200

168.6

10.4

9.47

very

-
Methionine MET

M

131.19

185

162.9

-

5.74

3.381

1.340
Phenylalanine PHE

F

147.18

210

189.9

-

5.91

2.965

-
Proline PRO

P

97.12

145

112.7

-

6.3

162.3

-
Serine SER

S

87.08

115

89.0

-

5.68

5.023

1.537
Threonine THR

T

101.11

140

116.1

-

-

very

-
Tryptophan TRP

W

186.12

255

227.8

-

5.88

1.136

-
Tyrosine TYR

Y

163.18

230

193.6

9.7

5.63

0.0453

1.456
Valine VAL

V

99.14

155

140.0

-

6.002

8.85

1.230

a mass [dalton], surface [Å2], volume [Å3], pKa [side chain], pI [at 25°C], solubility [g/100g, 25°C], density [crystal density, g/ml],
    name: information from NIST Chemistry WebBook, three letter code: GIF, one letter code: VRML

b C.Chothia, J. Mol. Biol., 105(1975)1-14

c A.A. Zamyatin, Prog. Biophys. Mol. Biol., 24(1972)107-123

d C. Tanford, Adv. Prot. Chem., 17(1962)69-165

e The Merck Index, Merck & Co. Inc., Nahway, N.J., 11(1989); CRC Handbook of Chem.& Phys., Cleveland, Ohio, 58(1977)

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Hydrophobicity scales a

Residue non-polar 
surface area b
[A2]		 Estimated hydrophobic effect 
for residue burial
[kcal/mol]		 Estimated hydrophobic effect 
for side chain burial c
[kcal/mol]
Gly  47 1.18 0.0
Ala 86 2.15 1.0
Val 135 3.38 2.2
Ile 155 3.88 2.7
Leu 164 4.10 2.9
Pro 124 3.10 1.9
Cys 48 1.20 0.0
Met 137 3.43 2.3
Phe 39+155 3.46 2.3
Trp 37+199 4.11 2.9
Tyr 38+116 2.81 1.6
His 43+86 2.45 1.3
Thr 90 2.25 1.1
Ser 56 1.40 0.2
Gln 66 1.65 0.5
Asn 42 1.05 -0.1
Glu 69 1.73 0.5
Asp 45 1.13 -0.1
Lys 122 3.05 1.9
Arg 89 2.23 1.1

a P.A.Karplus, Protein Science 6(1997)1302-1307
b All surfaces associated with main- and side-chain carbon atoms were included except for amide, carb-
oxylate and guanidino carbons. For aromatic side chains, the aliphatic and aromatic surface areas are
reported seperately.
c The values are obtained from the previous column by substracting the value for Gly (1.18 kcal/mol) from
each residue.

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Amino acids in proteins

Postranslational modifications of amino acids in proteins

Sulphydryls Disulfidebond
-2.0159
 Oxidation
+15.9994
(C,M) Cysteinylation
+119.1442
 Glutathionylation
+305.3117
Methylation
+14.0269
 Formylation
+28.0104
Acetylation
+42.0373
 Lipoic acid
+188.3147
Amines Farnesylation
+204.3556
 Myristoylation
+210.3598
(K/N) Biotinylation
+226.2994
 Palmitoylation
+238.4136
Stearoylation
+266.4674
 Geranylation
+272.4741
Acids & Pyroglutamic acid (Q)
-17.0306
 Deamidation (Q,N)
+0.9847
Amides(E/D/Q/N) Carboxylation (E,D)
+44.0098
Hydroxyl- Phosphorylation
+79.9799
 Sulphation
+80.0642
groups (S/T/Y)
Carbohydrates Pentoses
+132.1161
 Deoxyhexoses
+146.1430
(S/T/N) Hexosamines
+161.1577
 Hexoses
+162.1424
N-acetylhexosamines
+203.1950
 Sialic acid
+291.2579
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Solvent accessibility of amino acids in known protein structuresa

SEA (Solvent Exposed Area)

The solvent accessibility information was derived from (a). The data for this table was calculated from 55 proteins in the Brookhaven data base. The only clear trend in this table is that some residues, such as R and K, locate themselves so that they have access to the solvent. The hydrophobic residues, such as L and F, show no clear trend: they are found near the solvent as often as they are found buried.

Amino Acid

SEA >30 Å2

SEA <10 Å2

30 Å2 > SEA >10 Å2

S

0.70

0.20

0.10

T

0.71

0.16

0.13

A

0.48

0.35

0.17

G

0.51

0.36

0.13

P

0.78

0.13

0.09

C

0.32

0.54

0.14

D

0.81

0.09

0.10

E

0.93

0.04

0.03

Q

0.81

0.10

0.09

N

0.82

0.10

0.08

L

0.41

0.49

0.10

I

0.39

0.47

0.14

V

0.40

0.50

0.10

M

0.44

0.20

0.36

F

0.42

0.42

0.16

Y

0.67

0.20

0.13

W

0.49

0.44

0.07

K

0.93

0.02

0.05

R

0.84

0.05

0.11

H

0.66

0.19

0.15

a D. Bordo and P. Argos, J. Mol. Biol. 217(1991)721-729

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Mutation mass shifts

Residues DOWN the left indicate the EXPECTED residues

Residues ACROSS the top indicate the MUTANT residues

Gly

Ala

Ser

Pro

Val

Thr

Cys

Ile/ Leu

Asn

Asp

Gln/Lys

Glu

Met

His

Phe

Arg

Tyr

Trp
Gly

14

30

40

42

44

46

56

57

58

71

72

74

80

90

99

106

129
Ala

-14

16

26

28

30

32

42

43

44

57

58

60

66

76

85

92

115
Ser

-30

-16

10

12

14

15

26

27

28

41

42

44

50

60

69

76

99
Pro

-40

-126

-10

2

4

6

16

17

18

31

32

34

40

50

59

66

89
Val

-42

-28

-12

-2

2

4

14

15

16

29

30

32

38

48

57

64

87
Thr

-44

-30

-14

-4

-2

2

12

13

14

27

28

30

36

48

55

62

85
Cys

-46

-32

-16

-6

-4

-2

10

11

12

25

26

28

34

44

53

60

83
Leu/Ile

-56

-42

-26

-16

-14

-12

-10

1

2

15

16

18

24

34

43

50

73
Asn

-57

-43

-27

-17

-15

-13

-11

-1

1

14

15

17

23

33

42

49

72
Asp

-58

-44

-28

-18

-16

-14

-12

-2

-1

13

14

16

22

32

41

48

71
Gln/Lys

-71

-57

-41

-31

-29

-27

-25

-15

-14

-13

1

3

9

19

28

35

58
Glu

-72

-58

-42

-32

-30

-28

-26

-16

-15

-14

-1

2

8

18

27

34

57
Met

-74

-60

-44

-34

-32

-30

-28

-18

-17

-16

-3

-2

6

16

25

32

55
His

-80

-66

-50

-40

-38

-36

-34

-24

-23

-22

-9

-8

-6

10

19

26

49
Phe

-90

-76

-60

-50

-48

-46

-44

-34

-33

-32

-19

-18

-16

-10

9

16

39
Arg

-99

-85

-69

-59

-57

-55

-53

-43

-42

-41

-28

-27

-25

-19

-9

7

30
Tyr

-106

-92

-76

-66

-64

-62

-60

-450

-49

-48

-35

-34

-32

-26

-16

-7

23
Trp

-129

-115

-99

-89

-87

-85

-83

-73

-72

-71

-58

-57

-55

-49

-39

-30

-23

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