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PROPERTY.PPT
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1993-05-05
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Properties of amino acids ACDEFGHIKLMNPQRSTVWY-
Structure of file:
Comments (begins from blank)
{ Property names (from 1-st position of string)
Literature source (from 1-st position of string)
Values of amino acid properties }
Hydrophilicity Hopp-Woods
T.P.Hopp, K.R.Woods, PNAS 78 (1981) 3824
-.5 -1.0 3.0 3.0 -2.5 0.0 -.5 -1.8 3.0 -1.8
-1.3 .2 0.0 .2 3.0 .3 -.4 -1.5 -3.4 -2.3
Hydropathy Kyte-Doolittle
J.Kyte, R.F.Doolittle J.Mol.Biol 157 (1982) 105
1.8 2.5 -3.5 -3.5 2.8 -.4 -3.2 4.5 -3.9 3.8
1.9 -3.5 -1.6 -3.5 -4.5 -.8 -.7 4.2 -.9 -1.3
Polarity Grantham
R.Grantham P.M.Cullis C.C.F.Southgate Science 206 (1979) 575
8.1 5.5 13. 12.3 5.2 9. 10.4 5.2 11.3 4.9
5.7 11.6 8. 10.5 10.5 9.2 8.6 5.9 5.4 6.2
Side-chain volume Grantham
R.Grantham Science 185 (1975) 862
31 55 54 83 132 3 96 111 119 111
105 56 32.5 85 124 32 61 84 170 136
Hydrophobicity Eisenberg
Eisenberg J.Mol.Biol. 1984, v.179, p.125-142
.62 0.29 -0.90 -0.74 1.19 0.48 -0.40 1.38 -1.50 1.06
0.64 -0.78 0.12 -0.85 -2.53 -0.18 -0.05 1.08 0.81 0.26
Alpha-helix Chou-Fasman
1.42 0.7 1.01 1.51 1.13 0.57 1.0 1.08 1.16 1.21
1.45 0.67 0.57 1.11 0.98 0.77 0.83 1.06 1.08 0.69
Beta-strand Chou-Fasman
0.83 1.19 0.54 0.37 1.38 0.75 0.87 1.60 0.74 1.30
1.05 0.89 0.55 1.10 0.93 0.75 1.19 1.70 1.37 1.47
Beta-turn Chou-Fasman
Chou P.Y., Fasman G.D. Biophys.J. 1979, 26,367-384
0.66 1.19 1.46 0.74 0.60 1.56 0.95 0.47 1.01 0.59
0.60 1.56 1.52 0.98 0.95 1.43 0.96 0.50 0.96 1.14
Hydrophobicity Bogardt et al.
Bogardt R.A. et al., J. Mol. Evol. 1980. V.15. P.197-218
23.1 40.3 17.5 17.8 76.1 2.7 23.1 83.6 43.5 57.6
44.3 2.4 73.5 0.0 22.6 1.9 1.9 49.6 100. 70.8
Volume Bogardt et al.
Bogardt R.A. et al., J. Mol. Evol. 1980. V.15. P.197-218
15.9 28.0 31.3 47.2 77.2 0.0 49.2 63.6 68.0 63.6
62.8 35.4 41.0 51.3 70.8 18.1 34.0 47.7 100. 78.5
Polarity Bogardt et al.
Bogardt R.A. et al., J. Mol. Evol. 1980. V.15. P.197-218
25.9 7.4 100. 93.8 1.2 37.0 43.2 0.0 64.2 0.0
4.9 63.0 21.0 45.7 51.9 32.1 21.0 8.6 4.9 9.9
Isoelectric point Bogardt et al.
Bogardt R.A. et al., J. Mol. Evol. 1980. V.15. P.197-218
39.2 26.3 0.0 3.2 38.6 38.5 59.2 39.2 86.9 38.6
35.7 31.3 40.2 34.4 100.0 34.8 45.7 38.5 37.7 34.4
HPLC Parker
Parker J.M.R. et al., Biochemistry, 1986,25,5425
2.1 1.4 10 7.8 -9.2 5.7 2.1 -0.8 5.7 -9.2
-4.2 7 2.1 6. 4.2 6.5 5.2 -3.7 -10. -1.9
Length of Peptide
Eroshkin
1. 1. 1. 1. 1. 1. 1. 1. 1. 1.
1. 1. 1. 1. 1. 1. 1. 1. 1. 1.
Hydrophobicity Fauchere-Pliska
Fauchere J., Pliska V., Eur.J.Med.Chem., 1893,18,369-375
.31 1.54 -0.77 -0.64 1.79 0 .13 1.8 -0.99 1.7
1.23 -0.6 .72 -0.22 -1.01 -0.04 .26 1.22 2.25 0.96
Recognizability Eroshkin
Eroshkin, Molec. Biol.,
-1.44 -0.1 1.5 1.43 -0.65 -1.73 0.16 -1.1 1.31 -1.14
-0.9 1.12 0.23 0.77 1.13 .65 .04 -1.24 .02 -0.08
Charge
Eroshkin
0. 0. -1. -1. 0. 0. 0 0. 1. 0.
0. 0. 0. 0. 1. 0. 0. 0. 0. 0.
Chargeness
Eroshkin
0. 0. 1. 1. 0. 0. 0. 0. 1. 0.
0. 0. 0. 0. 1. 0. 0. 0. 0. 0.
Charge +
Eroshkin
0. 0. 0. 0. 0. 0. 0. 0. 1. 0.
0. 0. 0. 0. 1. 0. 0. 0. 0. 0.