Powered by

© August 2007 Lorentz JÄNTSCHI && Sorana Daniela BOLBOACĂ

Up

0	Name	L3	L	[1]	[2]	[3]	[4]	[5]	[6]	[7]	[8]	[9]	[10]	[11]	[12]	[13]	[14]	[15]	[16]	[17]	[18]	[19]	[20]	[21]	[22]	[23]	[24]	[25]	[26]	[27]
1	Alanine	Ala	A	0.616	1.8	-0.17	0.11	47	-0.50	0.20	0.62	0.74	0.30	1.60	-0.40	0.61	0.39	1.15	2.10	0.35	12.97	0.31	1.36	-0.30	0.42	0.44	0.10	5.33	-0.75	41
2	Arginine	Arg	R	0.000	-4.5	-0.81	2.58	-26	3.00	1.40	-2.53	0.64	-1.40	-12.30	-0.59	0.69	-3.95	0.58	4.20	-1.50	11.72	-1.01	0.15	-1.10	-1.56	-2.42	1.91	4.18	0.80	-14
3	Asparagine	Asn	N	0.236	-3.5	-0.42	2.05	-41	0.20	-0.50	-0.78	0.63	-0.50	-4.80	-0.92	0.89	-1.91	-0.77	7.00	-0.99	11.42	-0.60	0.33	-0.20	-1.03	-1.32	0.48	3.71	-0.05	-28
4	Aspartate	Asp	D	0.028	-3.5	-1.23	3.49	-18	3.00	-3.10	-0.90	0.62	-0.60	-9.20	-1.31	0.61	-3.81	0.65	10.00	-2.15	10.85	-0.77	0.11	-1.40	-0.51	-0.31	0.78	3.59	-0.40	-55
5	Cysteine	Cys	C	0.68	2.5	0.24	-0.13	52	-1.00	4.10	0.29	0.91	0.90	2.00	0.17	0.36	0.25	-1.20	1.40	0.76	14.63	1.54	1.27	6.30	0.84	0.58	-1.42	7.93	-1.90	49
6	Glutamine	Gln	Q	0.251	-3.5	-0.58	2.36	-18	0.20	-2.80	-0.85	0.62	-0.70	-4.10	-0.91	0.97	-1.30	-0.11	6.00	-0.93	11.76	-0.22	0.33	-0.20	-0.96	-0.71	0.95	3.87	0.75	-10
7	Glutamate	Glu	E	0.043	-3.5	-2.02	2.68	8	3.00	-1.80	-0.74	0.62	-0.70	-8.20	-1.22	0.51	-2.91	-0.71	7.80	-1.95	11.89	-0.64	0.25	0.00	-0.37	-0.34	0.83	3.65	-1.30	-31
8	Glycine	Gly	G	0.501	-0.4	-0.01	0.74	0	0.00	0.00	0.48	0.72	0.30	1.00	-0.67	0.81	0.00	-1.84	5.70	0.00	12.43	0.00	1.09	1.20	0.00	0.00	0.33	4.48	0.00	0
9	Histidine	His	H	0.165	-3.2	-0.96	2.06	-42	-0.50	0.50	-0.40	0.78	-0.10	-3.00	-0.64	0.69	-0.64	3.12	2.10	-0.65	12.16	0.13	0.68	-1.30	-2.28	-0.01	-0.50	5.10	-4.80	8
10	Isoleucine	Ile	I	0.943	4.5	0.31	-0.6	100	-1.80	4.80	1.38	0.88	0.70	3.10	1.25	-1.45	1.82	-2.92	-8.00	1.83	15.67	1.80	1.44	4.30	1.81	2.46	-1.13	8.83	-3.65	99
11	Leucine	Leu	L	0.943	3.8	0.56	-0.55	100	-1.80	5.70	1.06	0.85	0.50	2.80	1.22	-1.65	1.82	0.75	-9.20	1.80	14.90	1.70	1.47	6.60	1.80	2.46	-1.18	8.47	-4.05	97
12	Lysine	Lys	K	0.283	-3.9	-0.99	2.71	-37	3.00	-3.10	-1.50	0.52	-1.80	-8.80	-0.67	0.46	-2.77	2.06	5.70	-1.54	11.36	-0.99	0.09	-3.60	-2.03	-2.45	1.40	2.95	-0.05	-23
13	Methionine	Met	M	0.738	1.9	0.23	-0.1	74	-1.30	4.20	0.64	0.85	0.40	3.40	1.02	-0.66	0.96	-3.85	-4.20	1.10	14.39	1.23	1.42	2.50	1.18	1.10	-1.59	8.95	-1.50	74
14	Phenylalanine	Phe	F	1.00	2.8	1.13	-0.32	92	-2.50	4.40	1.19	0.88	0.50	3.70	1.92	-1.52	2.27	-1.41	-9.20	1.69	14.00	1.79	1.57	7.50	1.74	2.54	-2.12	9.03	-6.15	100
15	Proline	Pro	P	0.711	-1.6	-0.45	2.23	-46	0.00	-2.20	0.12	0.64	-0.30	-0.20	0.49	-0.17	0.99	-0.53	2.10	0.84	11.37	0.72	0.54	2.20	0.86	1.29	0.73	3.87	-1.10	N/A
16	Serine	Ser	S	0.359	-0.8	-0.13	0.84	-7	0.30	-0.50	-0.18	0.66	-0.10	0.60	0.55	0.42	-1.24	-0.26	6.50	-0.63	11.23	-0.04	0.97	-0.60	-0.64	-0.84	0.52	4.09	0.55	-5
17	Threonine	Thr	T	0.45	-0.7	-0.14	0.52	13	-0.40	-1.90	-0.05	0.70	-0.20	1.20	-0.28	0.29	-1.00	-0.45	5.20	-0.27	11.69	0.26	1.08	-2.20	-0.26	-0.41	0.07	4.49	-0.60	13
18	Tryptophan	Trp	W	0.878	-0.9	1.85	0.3	84	-3.40	1.00	0.81	0.85	0.30	1.90	0.50	-1.20	2.13	-1.14	-10.00	1.35	13.93	2.25	1.00	7.90	1.46	2.56	-0.51	7.66	-7.00	97
19	Tyrosine	Tyr	Y	0.88	-1.3	0.94	0.68	49	-2.30	3.20	0.26	0.76	-0.40	-0.70	1.67	-1.43	1.47	0.13	-1.90	0.39	13.42	0.96	0.83	7.10	0.51	1.63	-0.21	5.89	-5.85	63
20	Valine	Val	V	0.825	4.2	-0.07	-0.31	79	-1.50	4.70	1.08	0.86	0.60	2.60	0.91	-0.75	1.30	-0.13	-3.70	1.32	15.71	1.22	1.37	5.90	1.34	1.73	-1.27	7.63	-2.50	76

[Ref]	Property	Source
[1]	Hydrophobicity	Black S.D., Mould D.R., Black SD, Mould DR, Development of Hydrophobicity Parameters to Analyze Proteins Which Bear Post- or Cotranslational Modifications, Anal Biochem, 1991, 193, 72-82. http://psyche.uthct.edu/shaun/SBlack/aagrease.html
[2]	Hydrophobicity	Kyte J, Doolittle RF, A Simple Method for Displaying the Hydropathic Character of a Protein, J Mol Biol 1982, 157, 105-132.
[3]	Hydrophobicity	Wimley WC, White SH, Experimentally determined hydrophobicity scale for proteins at membrane interfaces, Nature Struct Biol, 1996, 3, 842-848.
[4]	Hydrophobicity	Hessa T, Kim H, Bihlmaier K, Lundin C, Boekel J, Andersson H, Nilsson I, White SH, von Heijne G, Recognition of transmembrane helices by the endoplasmic reticulum translocon, Nature, 2005, 433, 377-381.
[5]	Hydrophobicity Index at pH = 2	Sereda TJ, Mant CT, Sonnichsen FD, Hodges RS, Reversed-phase chromatography of synthetic amphipathic a-helical peptides as a model for ligand/receptor interactions effect of changing hydrophobic environment on the relative hydrophilicity/hydrophobicity of amino acid side- chains, J Chromatogr A, 1994, 676(1), 139-153.
[6]	Hydrophilic index	Hoop TP, Woods KR, Prediction of protein antigenic determinants from amino acid sequences, Proc Natl Acad Sci USA, 1981,78, 3824-3828.
[7]	An optimal hydrophobicity scale	Cornette JL, Cease KB, Margalit H, Spouge JL, Berzofsky JA, DeLisi C, Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins, J Mol Biol, 1987, 195, 659-685.
[8]	A normalized consensus hydrophobicity scale	Eisenberg D, Schwarz E, Komaromy M, Wall R, Analysis of membrane and surface protein sequences with the hydrophobic moment plot, J Mol Biol, 1984, 179, 125-142.
[9]	Hydrophobicity	Rose GD, Geselowitz AR, Lesser GJ, Lee RH, Zehfus MH, Hydrophobicity of amino acid residues in globular proteins, Science, 1985, 229, 834-838.
[10]	Hydrophobicity	Janin J, Surface and inside volumes in globular proteins, Nature, 1979, 277, 491-492.
[11]	Hydrophobicity	Engelman DM, Steitz TA, Goldman A, Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins, Annu Rev Biophys Biophys Chem, 1986, 15, 321-353.
[12]	Hydrophobicity	Sweet RM, Eisenberg D, Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure, J Mol Biol, 1983, 171, 479-488.
[13]	Hydrophobicity	Bull HB, Breese K, Surface tension of amino acid solutions: A hydrophobicity scale of the amino acid residues, Arch Biochem Biophys, 1974, 161, 665-670.
[14]	Hydrophilicity	Roseman MA, Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds, J Mol Biol, 1988, 200, 513-522.
[15]	Hydrophobicity	Welling GW, Weijer WJ, Van der Zee R, Welling-Wester S, Prediction of sequential antigenic regions in proteins, FEBS Lett, 1985, 188, 215-218.
[16]	Hydrophilicity	Parker JMR, Guo D, Hodges RS, New Hydrophilicity Scale Derived from High-Performance Liquid Chromatography Peptide Retention Data: Correlation of Predicted Surface Residues with Antigenicity and X-ray-Derived Accessible Sites?, Biochemistry, 1986, 25, 5425-5431.
[17]	Hydrophobicity at pH = 7.5	Cowan R, Whittaker RG, Hydrophobicity indices for amino acid residues as determined by HPLC, Peptide Research, 1990, 3, 75-80.
[18]	Hydrophobic character	Manavalan P, Ponnuswamy PK. Hydrophobic character of amino acid residues in globular proteins, Nature, 1978, 275, 673-674.
[19]	Hydrophobic parameters	Fauchere J-L, Pliska VE, Hydrophobic parameters of amino-acid side-chains from the partitioning of N-acetyl-amino-acid amide, Eur J Med Chem, 1983, 18, 369-375.
[20]	Hydrophobicity	Rao MJK, Argos P, A conformational preference parameter to predict helices in integral membrane proteins, Biochim Biophys Acta, 1986, 869, 197-214.
[21]	Hydrophobicity	Wilson KJ, Honegger A, Stotzel RP, Hughes GJ, The behaviour of peptides on reverse-phase supports during high-pressure liquid chromatography, Biochem J, 1981, 199, 31-41.
[22]	Hydrophobicity at ph = 3.4	Cowan R, Whittaker RG, Hydrophobicity indices for amino acid residues asdetermined by HPLC, Peptide Research, 1990, 3, 75-80.
[23]	Patition coefficients	Abraham DJ, Leo AJ, Extension of the fragment method to calculate amino acid zwitterions and side chain partition coefficients, Proteins, 1987, 2, 130-152.
[24]	Partition energies	Amino acid side-chain partition energies and distribution of residues in soluble proteins, Biophys J, 1985, 47, 61-70.
[25]	Effective Interresidue Contact Energies	Miyazawa S, Jernigen RL, Estimation of Effective Interresidue Contact Energies from Protein Crystal Structures: Quasi-Chemical Approximation, Macromolecules, 1985, 18, 534-552.
[26]	Hydrophobicity - Gibbs free energy	Urry D. W., The change in Gibbs free energy for hydrophobic association - Derivation and evaluation by means of inverse temperature transitions, Chem Phys Lett, 2004, 399(1-3), 177-183.
[27]	Hydrophobicity Index at pH = 7	Monera OD, Sereda TJ, Zhou NE, Kay CM, Hodges RS, Relationship of sidechain hydrophobicity and alpha-helical propensity on the stability of the single-stranded amphipathic alpha-helix, J Pept Sci, 1995, 1(5), 319-329.