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Volumn 12, Issue 3, 2003, Pages 627-634

Prediction of β-turns in proteins from multiple alignment using neural network

Author keywords

Turns; Multiple alignment; Neural networks; Prediction; Secondary structure; Web server

Indexed keywords

ACCURACY; AMINO ACID SEQUENCE; ARTICLE; CORRELATION COEFFICIENT; NERVE CELL NETWORK; PREDICTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SCORING SYSTEM;

EID: 0037372098     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0228903     Document Type: Article
Times cited : (125)

References (26)
  • 2
    • 0030963006 scopus 로고    scopus 로고
    • Prediction of β-turns
    • Chou, K.C. 1997. Prediction of β-turns. J. Pept. Res. 49: 120-144.
    • (1997) J. Pept. Res. , vol.49 , pp. 120-144
    • Chou, K.C.1
  • 3
    • 0034327349 scopus 로고    scopus 로고
    • Prediction of tight turns and their types in proteins
    • -. 2000. Prediction of tight turns and their types in proteins. Anal. Biochem. 286: 1-16.
    • (2000) Anal. Biochem. , vol.286 , pp. 1-16
  • 4
    • 0030808140 scopus 로고    scopus 로고
    • Classification and prediction of β-turn types
    • Chou, K.C. and Blinn, J.R. 1997. Classification and prediction of β-turn types. J. Protein Chem. 16: 575-595.
    • (1997) J. Protein Chem. , vol.16 , pp. 575-595
    • Chou, K.C.1    Blinn, J.R.2
  • 6
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, β-sheet and random coil regions calculated from proteins
    • Chou, P.Y. and Fasman, G.D. 1974. Conformational parameters for amino acids in helical, β-sheet and random coil regions calculated from proteins. Biochemistry 13: 211-222.
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 7
    • 0018476871 scopus 로고
    • Prediction of β-turns
    • -. 1979. Prediction of β-turns. Biophys. J. 26: 367-384.
    • (1979) Biophys. J. , vol.26 , pp. 367-384
  • 9
    • 0017873321 scopus 로고
    • Analysis and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J., Osguthorpe, D.J., and Robson, B. 1987. Analysis and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120: 97-120.
    • (1987) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 10
    • 0033752859 scopus 로고    scopus 로고
    • β- and γ-turns in proteins revisited: A new set of amino acid-dependent positional preferences and potential
    • Guruprasad, K. and Rajkumar, S. 2000. β- and γ-turns in proteins revisited: A new set of amino acid-dependent positional preferences and potential. J. Biosci. 25: 143-156.
    • (2000) J. Biosci. , vol.25 , pp. 143-156
    • Guruprasad, K.1    Rajkumar, S.2
  • 11
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF: A program to identify and analyze structural motifs in proteins
    • Hutchinson, E.G. and Thornton, J.M. 1996. PROMOTIF: A program to identify and analyze structural motifs in proteins. Protein Sci. 5: 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 12
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D.T. 1999. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292: 195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 13
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. 1983. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 14
    • 0036855904 scopus 로고    scopus 로고
    • An evaluation of β-turn prediction methods
    • Kaur, H. and Raghava, G.P.S. 2002. An evaluation of β-turn prediction methods. Bioinformatics 18: 1508-1514.
    • (2002) Bioinformatics , vol.18 , pp. 1508-1514
    • Kaur, H.1    Raghava, G.P.S.2
  • 15
    • 0036467068 scopus 로고    scopus 로고
    • Alignments grow, secondary structure prediction improves
    • Przybylski, D. and Rost, B. 2002. Alignments grow, secondary structure prediction improves. Proteins 46: 197-205.
    • (2002) Proteins , vol.46 , pp. 197-205
    • Przybylski, D.1    Rost, B.2
  • 16
    • 0023803244 scopus 로고
    • Predicting the secondary structure of globular proteins using neural network models
    • Qian, N. and Sejnowski, T.J. 1988. Predicting the secondary structure of globular proteins using neural network models. J. Mol. Biol. 202: 865-884.
    • (1988) J. Mol. Biol. , vol.202 , pp. 865-884
    • Qian, N.1    Sejnowski, T.J.2
  • 17
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J.S. 1981. The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34: 167-339.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 19
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile based neural networks
    • Rost, B. 1996. PHD: Predicting one-dimensional protein structure by profile based neural networks. Meth. Enzymol. 266: 525-539.
    • (1996) Meth. Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 20
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B. and Sander, C. 1993. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232: 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 21
    • 0022471098 scopus 로고
    • Learning representations by back-propagation errors
    • Rumelhart, D.E., Hinton, G.E., and Williams, R.J. 1986. Learning representations by back-propagation errors. Nature 323: 533-536.
    • (1986) Nature , vol.323 , pp. 533-536
    • Rumelhart, D.E.1    Hinton, G.E.2    Williams, R.J.3
  • 22
    • 0032900496 scopus 로고    scopus 로고
    • Prediction of the location and type of β-turns in proteins using neural networks
    • Shepherd, A.J., Gorse, D., and Thornton, J.M. 1999. Prediction of the location and type of β-turns in proteins using neural networks. Protein Sci. 8: 1045-1055.
    • (1999) Protein Sci. , vol.8 , pp. 1045-1055
    • Shepherd, A.J.1    Gorse, D.2    Thornton, J.M.3
  • 23
    • 0034713833 scopus 로고    scopus 로고
    • Role of amino acid residues at turns in the conformational stability and folding of human lysozyme
    • Takano, K., Yamagata, Y., and Yutani, K. 2000. Role of amino acid residues at turns in the conformational stability and folding of human lysozyme. Biochemistry 39: 8655-8665.
    • (2000) Biochemistry , vol.39 , pp. 8655-8665
    • Takano, K.1    Yamagata, Y.2    Yutani, K.3
  • 24
    • 0024279235 scopus 로고
    • Analysis and prediction of the different types of β-turns in proteins
    • Wilmot, C.M. and Thomton, J.M. 1988. Analysis and prediction of the different types of β-turns in proteins. J. Mol. Biol. 203: 221-232.
    • (1988) J. Mol. Biol. , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thomton, J.M.2
  • 26
    • 0031149431 scopus 로고    scopus 로고
    • Prediction of β-turns in proteins by 1-4 & 2-3 correlation model
    • Zhang, C.T. and Chou, K.C. 1997. Prediction of β-turns in proteins by 1-4 & 2-3 correlation model. Biopolymers 41: 673-702.
    • (1997) Biopolymers , vol.41 , pp. 673-702
    • Zhang, C.T.1    Chou, K.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.