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IMB Jena Image Library: 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)
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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