메뉴 건너뛰기




Volumn 4, Issue 6, 2010, Pages 735-754

Accuracy of protein hydropathy predictions

Author keywords

Accuracy assessment; Amino acid solvent accessibility; Prediction accuracy

Indexed keywords


EID: 78650482076     PISSN: 17485673     EISSN: 17485681     Source Type: Journal    
DOI: 10.1504/IJDMB.2010.037550     Document Type: Article
Times cited : (4)

References (75)
  • 1
    • 0000104080 scopus 로고
    • An empirical hydrophobicity scale for alpha-amino-acids and some of its applications
    • Aboderin, A. (1971) 'An empirical hydrophobicity scale for alpha-amino-acids and some of its applications', Int. J. Biochem., Vol. 2, pp.537-544.
    • (1971) Int. J. Biochem. , vol.2 , pp. 537-544
    • Aboderin, A.1
  • 2
    • 0023465103 scopus 로고
    • Extension of the fragment method to calculate amino acid zwitterion and side chain partition coefficients
    • Abraham, D. and Leo, A. (1987) 'Extension of the fragment method to calculate amino acid zwitterion and side chain partition coefficients', Proteins, Vol. 2, pp.130-152.
    • (1987) Proteins , vol.2 , pp. 130-152
    • Abraham, D.1    Leo, A.2
  • 3
    • 13244259253 scopus 로고    scopus 로고
    • Evaluation of methods for predicting the topology of β-barrel outer membrane proteins and a consensus prediction method
    • Bagos, P., Liakopoulos, T. and Hamodrakas, S. (2005) 'Evaluation of methods for predicting the topology of β-barrel outer membrane proteins and a consensus prediction method', BMC Bioinformatics, Vol. 6, p.7.
    • (2005) BMC Bioinformatics , vol.6 , pp. 7
    • Bagos, P.1    Liakopoulos, T.2    Hamodrakas, S.3
  • 4
    • 0029029804 scopus 로고
    • The antisense homology box: A new motif within proteins that encodes biologically active peptides
    • Baranyi, L., Campbell, W., Ohshima, K., Fujimoto, S., Boros, M. and Okada, H. (1995) 'The antisense homology box: a new motif within proteins that encodes biologically active peptides', Nat. Med., Vol. 1, pp.894-901.
    • (1995) Nat. Med. , vol.1 , pp. 894-901
    • Baranyi, L.1    Campbell, W.2    Ohshima, K.3    Fujimoto, S.4    Boros, M.5    Okada, H.6
  • 5
    • 2642518000 scopus 로고    scopus 로고
    • Hydrophobic complementarity in protein-protein docking
    • Berchanski, A., Shapira, B. and Eisenstein, M. (2004) 'Hydrophobic complementarity in protein-protein docking', Proteins, Vol. 56, pp.130-142.
    • (2004) Proteins , vol.56 , pp. 130-142
    • Berchanski, A.1    Shapira, B.2    Eisenstein, M.3
  • 6
    • 0345059376 scopus 로고    scopus 로고
    • Announcing the worldwide Protein Data Bank
    • DOI 10.1038/nsb1203-980
    • Berman, H., Henrick, K. and Nakamura, H. (2003) 'Announcing the worldwide protein data bank', Nature Struct. Biol., Vol. 10, p.980. (Pubitemid 37500485)
    • (2003) Nature Structural Biology , vol.10 , Issue.12 , pp. 980
    • Berman, H.1    Henrick, K.2    Nakamura, H.3
  • 7
    • 11144246404 scopus 로고    scopus 로고
    • Benchmarking B cell epitope prediction: Underpeformance of existing methods
    • Blythe, M.J. and Flower, D.R. (2005) 'Benchmarking B cell epitope prediction: underpeformance of existing methods', Prot. Sci., Vol. 14, pp.246-248.
    • (2005) Prot. Sci. , vol.14 , pp. 246-248
    • Blythe, M.J.1    Flower, D.R.2
  • 8
    • 0016192651 scopus 로고
    • Surface tension of amino acid solutions: A hydrophobicity scale of the amino acid residues
    • Bull, H. and Breese, K. (1974) 'Surface tension of amino acid solutions: a hydrophobicity scale of the amino acid residues', Arch. Biochem. Biophys, Vol. 161, pp.665-670.
    • (1974) Arch. Biochem. Biophys , vol.161 , pp. 665-670
    • Bull, H.1    Breese, K.2
  • 9
    • 0026539511 scopus 로고
    • Structure-derived hydrophobic potential. Hydrophobic potential derived from X-ray structures of globular proteins is able to identify native folds
    • Casari, G. and Sippl, M. (1992) 'Structure-derived hydrophobic potential. Hydrophobic potential derived from X-ray structures of globular proteins is able to identify native folds', J. Mol. Biol., Vol. 224, pp.725-732.
    • (1992) J. Mol. Biol. , vol.224 , pp. 725-732
    • Casari, G.1    Sippl, M.2
  • 10
    • 0035937259 scopus 로고    scopus 로고
    • Predicting the functional consequences of non synonymous single nucleotide polymorphisms: Structure-based assessment of amino acid variation
    • Chasman, D. and Adams, R. (2001) 'Predicting the functional consequences of non synonymous single nucleotide polymorphisms: structure-based assessment of amino acid variation', J. Mol. Biol., Vol. 307, pp.683-706.
    • (2001) J. Mol. Biol. , vol.307 , pp. 683-706
    • Chasman, D.1    Adams, R.2
  • 11
    • 0017187836 scopus 로고
    • The nature of the accessible and buried surfaces in proteins
    • Chothia, C. (1976) 'The nature of the accessible and buried surfaces in proteins', J. Mol. Biol., Vol. 105, pp.1-12.
    • (1976) J. Mol. Biol. , vol.105 , pp. 1-12
    • Chothia, C.1
  • 12
    • 0036238844 scopus 로고    scopus 로고
    • Identification of novel membrane proteins by searching for patterns in hydropathy profiles
    • Clements, J.D. and Martin, R.E. (2002) 'Identification of novel membrane proteins by searching for patterns in hydropathy profiles', Eur. J. Biochem., Vol. 269, pp.2101-2107.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2101-2107
    • Clements, J.D.1    Martin, R.E.2
  • 13
    • 0023645034 scopus 로고
    • Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins
    • Cornette, J., Cease, K., Margalit, H., Spouge, J., Berzofsky, J. and DeLisi, C. (1987) 'Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins', J. Mol. Biol., Vol. 195, pp.659-685.
    • (1987) J. Mol. Biol. , vol.195 , pp. 659-685
    • Cornette, J.1    Cease, K.2    Margalit, H.3    Spouge, J.4    Berzofsky, J.5    DeLisi, C.6
  • 14
    • 0032857714 scopus 로고    scopus 로고
    • The correlation of protein hydropathy with the base composition of coding sequences
    • D'Onofrio, G., Jabbari, K., Musto, H. and Bernardi, G. (1999) 'The correlation of protein hydropathy with the base composition of coding sequences', Gene, Vol. 238, pp.3-14.
    • (1999) Gene , vol.238 , pp. 3-14
    • D'Onofrio, G.1    Jabbari, K.2    Musto, H.3    Bernardi, G.4
  • 15
    • 0026345864 scopus 로고
    • Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme
    • Dao-pin, S., Anderson, D., Baase, W., Dahlquist, F. and Matthews, B. (1991) 'Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme', Biochemistry, Vol. 30, pp.11521-11529.
    • (1991) Biochemistry , vol.30 , pp. 11521-11529
    • Dao-pin, S.1    Anderson, D.2    Baase, W.3    Dahlquist, F.4    Matthews, B.5
  • 16
    • 0025371555 scopus 로고
    • A critical evaluation of the hydropathy profile of membrane proteins
    • Degli Esposti, M., Crimi, M. and Venturoli, G. (1990) 'A critical evaluation of the hydropathy profile of membrane proteins', Eur. J. Biochem., Vol. 190, pp.207-219.
    • (1990) Eur. J. Biochem. , vol.190 , pp. 207-219
    • Degli Esposti, M.1    Crimi, M.2    Venturoli, G.3
  • 17
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. (1990) 'Dominant forces in protein folding', Biochemistry, Vol. 29, pp.7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.1
  • 18
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg, D. and MacLachan, A. (1986) 'Solvation energy in protein folding and binding', Nature, Vol. 319, pp.199-203.
    • (1986) Nature , vol.319 , pp. 199-203
    • Eisenberg, D.1    MacLachan, A.2
  • 20
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • Engelman, D., Steitz, T. and Goldman, A. (1986) 'Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins', Annu. Rev. Biophys. Biophys. Chem., Vol. 15, pp.321-353.
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 321-353
    • Engelman, D.1    Steitz, T.2    Goldman, A.3
  • 21
    • 0026567907 scopus 로고
    • Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect
    • Eriksson, A., Baase, W., Zhang, X., Heinz, D., Blaber, M., Baldwin, E. and Matthews, B. (1992) 'Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect', Science, Vol. 255, pp.178-183.
    • (1992) Science , vol.255 , pp. 178-183
    • Eriksson, A.1    Baase, W.2    Zhang, X.3    Heinz, D.4    Blaber, M.5    Baldwin, E.6    Matthews, B.7
  • 22
    • 0000484499 scopus 로고
    • Hydrophobic parameters π of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides
    • Fauchére, J. and Pliška, V. (1983) 'Hydrophobic parameters π of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides', Eur. J. Med. Chem., Vol. 18, pp.369-375.
    • (1983) Eur. J. Med. Chem. , vol.18 , pp. 369-375
    • Fauchére, J.1    Pliška, V.2
  • 23
    • 0029619259 scopus 로고
    • Knowledge-based secondary structure assignment
    • Frishman, D. and Argos, P. (1995) 'Knowledge-based secondary structure assignment', Proteins, Vol. 23, pp.566-579.
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 24
    • 0021670437 scopus 로고
    • The apolar surface area of amino acids and its empirical correlation with hydrophobic free energy
    • Frömmel, C. (1984) 'The apolar surface area of amino acids and its empirical correlation with hydrophobic free energy', J. Theor. Biol., Vol. 111, pp.247-260.
    • (1984) J. Theor. Biol. , vol.111 , pp. 247-260
    • Frömmel, C.1
  • 25
    • 0021977590 scopus 로고
    • Amino acid side-chain partition energies and distribution of residues in soluble proteins
    • Guy, H. (1985) 'Amino acid side-chain partition energies and distribution of residues in soluble proteins', Biophys. J., Vol. 47, pp.61-70.
    • (1985) Biophys. J. , vol.47 , pp. 61-70
    • Guy, H.1
  • 26
    • 0027092678 scopus 로고
    • Selection of representative protein data sets
    • Hobohm, U., Scharf, M. and Schneider, S.C. (1992) 'Selection of representative protein data sets', Protein Sci., Vol. 1, pp.409-417.
    • (1992) Protein Sci. , vol.1 , pp. 409-417
    • Hobohm, U.1    Scharf, M.2    Schneider, S.C.3
  • 27
    • 0025039476 scopus 로고
    • Predicting surface exposure of amino acids from protein sequence
    • Holbrook, S., Muskal, S. and Kim, S.H. (1990) 'Predicting surface exposure of amino acids from protein sequence', Protein Eng., Vol. 3, pp.659-665.
    • (1990) Protein Eng. , vol.3 , pp. 659-665
    • Holbrook, S.1    Muskal, S.2    Kim, S.H.3
  • 28
    • 0000448982 scopus 로고
    • Prediction of protein antigenic determinants from amino acid sequences
    • Hopp, T. and Woods, K. (1981) 'Prediction of protein antigenic determinants from amino acid sequences', Proc. Natl. Acad. Sci., Vol. 78, pp.3824-3828.
    • (1981) Proc. Natl. Acad. Sci. , vol.78 , pp. 3824-3828
    • Hopp, T.1    Woods, K.2
  • 29
    • 0024558250 scopus 로고
    • The nature of the hydrophobic binding of small peptides at the bilayer interface: Implications for the insertion of transbilayer helices
    • Jacobs, R. and White, S. (1989) 'The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices', Biochemistry, Vol. 28, pp.3421-3437.
    • (1989) Biochemistry , vol.28 , pp. 3421-3437
    • Jacobs, R.1    White, S.2
  • 30
    • 0018784438 scopus 로고
    • Surface and inside volumes in globular proteins
    • Janin, J. (1979) 'Surface and inside volumes in globular proteins', Nature, Vol. 277, pp.491-492. Janin, J., Miller, S. and Chothia, C. (1988) 'Surface, subunit interfaces and interior of oligomeric proteins', J. Mol. Biol., Vol. 204, pp.155-164.
    • (1979) Nature , vol.277 , pp. 491-492
    • Janin, J.1
  • 31
    • 0016708277 scopus 로고
    • Amino acid properties and side-chain orientation in proteins: A cross correlation approach
    • Jones, D. (1975) 'Amino acid properties and side-chain orientation in proteins: a cross correlation approach', J. Theor. Biol., Vol. 50, pp.2577-2637.
    • (1975) J. Theor. Biol. , vol.50 , pp. 2577-2637
    • Jones, D.1
  • 32
    • 0037132511 scopus 로고    scopus 로고
    • Reliability of transmembrane predictions in whole genome data
    • Käll, L. and Sonnhammer, E. (2002) 'Reliability of transmembrane predictions in whole genome data', FEBS Lett., Vol. 532, pp.415-418.
    • (2002) FEBS Lett. , vol.532 , pp. 415-418
    • Käll, L.1    Sonnhammer, E.2
  • 33
    • 0018800255 scopus 로고
    • Local interactions as a structure determinant for protein molecules. II
    • Krigbaum, W. and Komoriya, A. (1979) 'Local interactions as a structure determinant for protein molecules. II', Biochim. Biophys. Acta, Vol. 576, pp.204-248.
    • (1979) Biochim. Biophys. Acta , vol.576 , pp. 204-248
    • Krigbaum, W.1    Komoriya, A.2
  • 34
    • 0015241654 scopus 로고
    • Hydration of macromolecules. IV. Polypeptide conformation in frozen solutions
    • Kuntz, I. (1971) 'Hydration of macromolecules. IV. Polypeptide conformation in frozen solutions', J. Amer. Chem. Soc., Vol. 93, pp.516-518.
    • (1971) J. Amer. Chem. Soc. , vol.93 , pp. 516-518
    • Kuntz, I.1
  • 35
    • 9344234406 scopus 로고    scopus 로고
    • Comparative computational analysis of prion proteins reveals two fragments with unusual structural properties and a pattern of increase in hydrophobicity associated with disease-promoting mutations
    • Kuznetsov, I. and Rackovsky, S. (2004) 'Comparative computational analysis of prion proteins reveals two fragments with unusual structural properties and a pattern of increase in hydrophobicity associated with disease-promoting mutations', Protein Sci., Vol. 13, pp.3230-3244.
    • (2004) Protein Sci. , vol.13 , pp. 3230-3244
    • Kuznetsov, I.1    Rackovsky, S.2
  • 36
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R. (1982) 'A simple method for displaying the hydropathic character of a protein', J. Mol. Biol, Vol. 157, pp.105-132.
    • (1982) J. Mol. Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.2
  • 37
    • 33751104704 scopus 로고    scopus 로고
    • Improved method for predicting linear B-cell epitopes
    • Larsen, J.E.P., Lund, O. and Nielsen, M. (2006) 'Improved method for predicting linear B-cell epitopes', Immunome Res., Vol. 2, p.2.
    • (2006) Immunome Res. , vol.2 , pp. 2
    • Larsen, J.E.P.1    Lund, O.2    Nielsen, M.3
  • 38
    • 0023463401 scopus 로고
    • Distribution of accessible surfaces of amino acids in globular proteins
    • Lawrence, C., Auger, I. and Mannella, C. (1987) 'Distribution of accessible surfaces of amino acids in globular proteins', Proteins, Vol. 2, pp.153-161.
    • (1987) Proteins , vol.2 , pp. 153-161
    • Lawrence, C.1    Auger, I.2    Mannella, C.3
  • 39
    • 0017157584 scopus 로고
    • A simplified representation of protein conformations for rapid simulation of protein folding
    • Levitt, M. (1976) 'A simplified representation of protein conformations for rapid simulation of protein folding', J. Mol. Biol., Vol. 104, pp.59-107.
    • (1976) J. Mol. Biol. , vol.104 , pp. 59-107
    • Levitt, M.1
  • 40
    • 0038309560 scopus 로고    scopus 로고
    • Analysis of accessible surface of residues in proteins
    • Lins, L., Thomas, A. and Brasseur, R. (2003) 'Analysis of accessible surface of residues in proteins', Protein Sci., Vol. 12, pp.1406-1417.
    • (2003) Protein Sci. , vol.12 , pp. 1406-1417
    • Lins, L.1    Thomas, A.2    Brasseur, R.3
  • 41
    • 0031765884 scopus 로고    scopus 로고
    • Hydropathy profile alignment: A tool to search for structural homologues of membrane proteins
    • DOI 10.1016/S0168-6445(98)00018-7, PII S0168644598000187
    • Lolkema, J. and Slotboom, D. (1998) 'Hydropathy profile alignment: a tool to search for structural homologues of membrane proteins', FEMS Microbiol. Rev., Vol. 22, pp.305-322. (Pubitemid 28557047)
    • (1998) FEMS Microbiology Reviews , vol.22 , Issue.4 , pp. 305-322
    • Lolkema, J.S.1    Slotboom, D.-J.2
  • 42
    • 0018077908 scopus 로고
    • Hydrophobic character of amino acid residues in globular proteins
    • Manavalan, P. and Ponnuswamy, P. (1978) 'Hydrophobic character of amino acid residues in globular proteins', Nature, Vol. 275, pp.673-674.
    • (1978) Nature , vol.275 , pp. 673-674
    • Manavalan, P.1    Ponnuswamy, P.2
  • 43
    • 0018990802 scopus 로고
    • Prediction of peptide retention times in high-pressure liquid chromatography on the basis of amino acid composition
    • Meek, J. (1980) 'Prediction of peptide retention times in high-pressure liquid chromatography on the basis of amino acid composition', Proc. Natl. Acad. Sci., Vol. 77, pp.1632-1636.
    • (1980) Proc. Natl. Acad. Sci. , vol.77 , pp. 1632-1636
    • Meek, J.1
  • 44
    • 0001469314 scopus 로고
    • Empirical studies of hydrophobicity. 1. Effect of protein size on the hydrophobic behavior of amino acids
    • Meirovitch, H., Rackovsky, S. and Scheraga, H. (1980) 'Empirical studies of hydrophobicity. 1. Effect of protein size on the hydrophobic behavior of amino acids', Macromolecules, Vol. 13, pp.1398-1405.
    • (1980) Macromolecules , vol.13 , pp. 1398-1405
    • Meirovitch, H.1    Rackovsky, S.2    Scheraga, H.3
  • 45
    • 0344406716 scopus 로고    scopus 로고
    • Reliability measures for membrane protein topology prediction algorithms
    • Melen, K., Krogh, A. and von Heijne, G. (2003) 'Reliability measures for membrane protein topology prediction algorithms', J. Mol. Biol., Vol. 327, pp.735-744.
    • (2003) J. Mol. Biol. , vol.327 , pp. 735-744
    • Melen, K.1    Krogh, A.2    Von Heijne, G.3
  • 46
    • 0023645203 scopus 로고
    • Interior and surface of monomeric proteins
    • Miller, S., Janin, J., Lesk, A. and Chothia, C. (1987) 'Interior and surface of monomeric proteins', J. Mol. Biol., Vol. 196, pp.641-656.
    • (1987) J. Mol. Biol. , vol.196 , pp. 641-656
    • Miller, S.1    Janin, J.2    Lesk, A.3    Chothia, C.4
  • 47
    • 33845377127 scopus 로고
    • Estimation of effective interresidue contact energies from protein crystal structures: Quasi-chemical approximation
    • Miyazawa, S. and Jernigan, R. (1985) 'Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation', Macromolecules, Vol. 18, pp.534-552.
    • (1985) Macromolecules , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.2
  • 48
    • 0029919190 scopus 로고    scopus 로고
    • Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading
    • Miyazawa, S. and Jernigan, R. (1996) 'Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading', J. Mol. Biol., Vol. 256, pp.623-644.
    • (1996) J. Mol. Biol. , vol.256 , pp. 623-644
    • Miyazawa, S.1    Jernigan, R.2
  • 49
    • 0032960853 scopus 로고    scopus 로고
    • Self-consistent estimation of inter-residue protein contact energies based on an equilibrium mixture approximation of residues
    • Miyazawa, S. and Jernigan, R. (1999) 'Self-consistent estimation of inter-residue protein contact energies based on an equilibrium mixture approximation of residues', Proteins, Vol. 34, pp.49-68.
    • (1999) Proteins , vol.34 , pp. 49-68
    • Miyazawa, S.1    Jernigan, R.2
  • 50
    • 1342310510 scopus 로고    scopus 로고
    • Correlation between sequence hydrophobicity and surface-exposure pattern of database proteins
    • Moelbert, S., Emberly, E. and Tang, C. (2004) 'Correlation between sequence hydrophobicity and surface-exposure pattern of database proteins', Protein Sci., Vol. 13, pp.752-762.
    • (2004) Protein Sci. , vol.13 , pp. 752-762
    • Moelbert, S.1    Emberly, E.2    Tang, C.3
  • 51
    • 78650504896 scopus 로고    scopus 로고
    • Evaluation of methods for the prediction of membrane spanning regions
    • Möller, S., Croning, M. and Apweiler, R. (2004) 'Evaluation of methods for the prediction of membrane spanning regions', Bioinformatics, Vol. 17, p.53.
    • (2004) Bioinformatics , vol.17 , pp. 53
    • Möller, S.1    Croning, M.2    Apweiler, R.3
  • 52
    • 0032531058 scopus 로고    scopus 로고
    • Tertiary structure of the major house dust mite allergen Der p 2: Sequential and structural homologies
    • Mueller, G., Benjamin, D. and Rule, G. (1998) 'Tertiary structure of the major house dust mite allergen Der p 2: sequential and structural homologies', Biochemistry, Vol. 37, pp.12707-12714.
    • (1998) Biochemistry , vol.37 , pp. 12707-12714
    • Mueller, G.1    Benjamin, D.2    Rule, G.3
  • 53
    • 2442499729 scopus 로고    scopus 로고
    • Improved prediction of MHC class I and class II epitopes using a novel Gibbs sampling approach
    • Nielsen, M., Lundegaard, C., Worning, P., Hvid, C.S., Lamberth, K., Buus, S., Brunak, S. and Lund, O. (2004) 'Improved prediction of MHC class I and class II epitopes using a novel Gibbs sampling approach', Bioinformatics, Vol. 20, pp.1388-1397.
    • (2004) Bioinformatics , vol.20 , pp. 1388-1397
    • Nielsen, M.1    Lundegaard, C.2    Worning, P.3    Hvid, C.S.4    Lamberth, K.5    Buus, S.6    Brunak, S.7    Lund, O.8
  • 54
    • 0019042107 scopus 로고
    • Prediction of the surface-interior diagram of globular proteins by an empirical method
    • Nishikawa, K. and Ooi, T. (1980) 'Prediction of the surface-interior diagram of globular proteins by an empirical method', Int. J. Pept. Protein Res., Vol. 16, pp.19-32.
    • (1980) Int. J. Pept. Protein Res. , vol.16 , pp. 19-32
    • Nishikawa, K.1    Ooi, T.2
  • 55
    • 0015217634 scopus 로고
    • The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale
    • Nozaki, Y. and Tanford, J. (1971) 'The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale', J. Biol. Chem., Vol. 246, pp.2211-2217.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2211-2217
    • Nozaki, Y.1    Tanford, J.2
  • 56
    • 0019332406 scopus 로고
    • Internal residue criteria for predicting three-dimensional protein structures
    • Olsen, K. (1980) 'Internal residue criteria for predicting three-dimensional protein structures', Biochem. Biophys. Acta, Vol. 622, pp.259-267.
    • (1980) Biochem. Biophys. Acta , vol.622 , pp. 259-267
    • Olsen, K.1
  • 57
    • 0035255017 scopus 로고    scopus 로고
    • Quantitative comparison of the ability of hydropathy scales to recognize surface β-strands in proteins
    • Palliser, C. and Parry, D. (2001) 'Quantitative comparison of the ability of hydropathy scales to recognize surface β-strands in proteins', Proteins, Vol. 42, pp.243-255.
    • (2001) Proteins , vol.42 , pp. 243-255
    • Palliser, C.1    Parry, D.2
  • 58
    • 0023055775 scopus 로고
    • 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
    • Parker, J., Guo, D. and Hodges, R. (1986) '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, Vol. 25, pp.5425-5432.
    • (1986) Biochemistry , vol.25 , pp. 5425-5432
    • Parker, J.1    Guo, D.2    Hodges, R.3
  • 61
    • 0027354210 scopus 로고
    • Hydrophobic characteristics of folded proteins
    • Ponnuswamy, P. (1993) 'Hydrophobic characteristics of folded proteins', Prog. Biophys. Mol. Biol., Vol. 59, pp.57-103.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 57-103
    • Ponnuswamy, P.1
  • 62
    • 0019333534 scopus 로고
    • Hydrophobic packing and spatial arrangement of amino acid residues in globular proteins
    • Ponnuswamy, P., Prabhakaran, M. and Manavalan, P. (1980) 'Hydrophobic packing and spatial arrangement of amino acid residues in globular proteins', Biochim. Biophys. Acta., Vol. 623, pp.301-316.
    • (1980) Biochim. Biophys. Acta. , vol.623 , pp. 301-316
    • Ponnuswamy, P.1    Prabhakaran, M.2    Manavalan, P.3
  • 63
    • 0022412192 scopus 로고
    • Hydrophobicity of amino acid residues in globular proteins
    • Rose, G., Geselowitz, A., Lesser, G., Lee, R. and Zehfus, M. (1985) 'Hydrophobicity of amino acid residues in globular proteins', Science, Vol. 229, pp.834-838.
    • (1985) Science , vol.229 , pp. 834-838
    • Rose, G.1    Geselowitz, A.2    Lesser, G.3    Lee, R.4    Zehfus, M.5
  • 64
    • 0024278357 scopus 로고    scopus 로고
    • Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds
    • Roseman, M.A. (1998) 'Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds', J. Mol. Biol., Vol. 200, pp.513-522.
    • (1998) J. Mol. Biol. , vol.200 , pp. 513-522
    • Roseman, M.A.1
  • 65
    • 33748254730 scopus 로고    scopus 로고
    • Prediction of continuous B-cell epitopes in an antigen using recurrent neural network
    • Saha, S. and Raghava, G.P. (2006) 'Prediction of continuous B-cell epitopes in an antigen using recurrent neural network', Proteins, Vol. 65, pp.40-48.
    • (2006) Proteins , vol.65 , pp. 40-48
    • Saha, S.1    Raghava, G.P.2
  • 66
    • 29344454454 scopus 로고    scopus 로고
    • Frequencies of hydrophobic and hydrophilic runs and alternations in proteins of known structure
    • Schwarz, R. and King, J. (2006) 'Frequencies of hydrophobic and hydrophilic runs and alternations in proteins of known structure', Protein Sci., Vol. 15, pp.102-112.
    • (2006) Protein Sci. , vol.15 , pp. 102-112
    • Schwarz, R.1    King, J.2
  • 67
    • 0021112868 scopus 로고
    • Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure
    • Sweet, R. and Eisenberg, D. (1983) 'Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure', J. Mol. Biol., Vol. 171, pp.479-488.
    • (1983) J. Mol. Biol. , vol.171 , pp. 479-488
    • Sweet, R.1    Eisenberg, D.2
  • 69
    • 0027730735 scopus 로고
    • HYDRO: A program for protein hydropathy predictions
    • Vihinen, M. and Torkkila, E. (1993) 'HYDRO: a program for protein hydropathy predictions', Comput. Methods Programs Biomed., Vol. 41, pp.121-129.
    • (1993) Comput. Methods Programs Biomed. , vol.41 , pp. 121-129
    • Vihinen, M.1    Torkkila, E.2
  • 70
    • 0028361031 scopus 로고
    • Accuracy of protein flexibility predictions
    • Vihinen, M., Torkkila, E. and Riikonen, P. (1994) 'Accuracy of protein flexibility predictions', Proteins, Vol. 19, pp.141-149.
    • (1994) Proteins , vol.19 , pp. 141-149
    • Vihinen, M.1    Torkkila, E.2    Riikonen, P.3
  • 71
    • 3042579686 scopus 로고    scopus 로고
    • Best α-helical transmembrane protein topology predictions are achieved using hidden Markov models and evolutionary information
    • Viklund, H. and Elofsson, A. (2004) 'Best α-helical transmembrane protein topology predictions are achieved using hidden Markov models and evolutionary information', Protein Sci., Vol. 13, pp.1908-1917.
    • (2004) Protein Sci. , vol.13 , pp. 1908-1917
    • Viklund, H.1    Elofsson, A.2
  • 72
    • 1542577828 scopus 로고    scopus 로고
    • The amino-acid mutational spectrum of human genetic disease
    • Vitkup, D., Sander, C. and Church, G. (2003) 'The amino-acid mutational spectrum of human genetic disease', Genome Biol, Vol. 4, p.R72.
    • (2003) Genome Biol , vol.4
    • Vitkup, D.1    Sander, C.2    Church, G.3
  • 73
    • 0018485028 scopus 로고
    • Trans-membrane translocation of proteins: The direct transfer model
    • von Heijne, G. and Blomberg, C. (1979) 'Trans-membrane translocation of proteins: the direct transfer model', Eur. J. Biochem., Vol. 97, pp.175-181.
    • (1979) Eur. J. Biochem. , vol.97 , pp. 175-181
    • Von Heijne, G.1    Blomberg, C.2
  • 74
    • 0017926896 scopus 로고
    • Influence of water on protein structure. An analysis of the preferences of amino acid residues for the inside or outside and for specific conformations in a protein molecule
    • Wertz, D. and Scheraga, H. (1978) 'Influence of water on protein structure. An analysis of the preferences of amino acid residues for the inside or outside and for specific conformations in a protein molecule', Macromolecules, Vol. 11, pp.9-15.
    • (1978) Macromolecules , vol.11 , pp. 9-15
    • Wertz, D.1    Scheraga, H.2
  • 75
    • 0014349825 scopus 로고
    • The characterization of amino acid sequences in proteins by statistical methods
    • Zimmerman, J., Eliezer, N. and Simha, R. (1968) 'The characterization of amino acid sequences in proteins by statistical methods', J. Theor. Biol, Vol. 21, pp.170-201.
    • (1968) J. Theor. Biol , vol.21 , pp. 170-201
    • Zimmerman, J.1    Eliezer, N.2    Simha, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.