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Volumn 19, Issue 1, 1994, Pages 55-72

Combining evolutionary information and neural networks to predict protein secondary structure

Author keywords

evolutionary information; multiple alignment profiles; prediction of secondary structure class; prediction of secondary structure content; secondary structure prediction

Indexed keywords

AMINO ACID COMPOSITION; AMINO ACID SEQUENCE; ARTICLE; CLONE; COMPUTER MODEL; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; STATISTICAL ANALYSIS; STRUCTURE ANALYSIS;

EID: 0028300741     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.340190108     Document Type: Article
Times cited : (1353)

References (135)
  • 7
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 8
  • 13
    • 0026030641 scopus 로고
    • Database of homology‐derived structures and the structural meaning of sequence alignment
    • (1991) Proteins , vol.9 , pp. 56-68
    • Schneider, R.1    Sander, C.2
  • 14
    • 0026754015 scopus 로고
    • Accurate modeling of protein conformation by automatic segment matching
    • (1992) J. Mol. Biol. , vol.226 , pp. 507-533
    • Levitt, M.1
  • 15
    • 0026675799 scopus 로고
    • Fast and simple Monte Carlo algorithm for side chain optimization in proteins: Application to model building by homology
    • (1992) Proteins , vol.14 , pp. 213-223
    • Holm, L.1    Sander, C.2
  • 22
    • 0025851973 scopus 로고
    • Prediction of protein folding from amino acid sequence over discrete conformation spaces
    • (1991) Biochemistry , vol.30 , pp. 4232-4237
    • Crippen, G.M.1
  • 28
    • 0025341310 scopus 로고
    • Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge‐based prediction of local structures of globular proteins
    • (1990) J. Mol. Biol. , vol.213 , pp. 859-883
    • Sippl, M.J.1
  • 29
    • 0026704815 scopus 로고
    • Detection of native‐like models for amino acid sequences of unknown three‐dimensional structure in a data base of known protein conformations
    • (1992) Proteins , vol.13 , pp. 258-271
    • Sippl, M.J.1    Weitckus, S.2
  • 30
    • 84995012219 scopus 로고    scopus 로고
    • Predictive power of mean force pair potentials in protein folding. Proteins
    • Sippl, M.J.1    Jaritz, M.2
  • 37
    • 0015243226 scopus 로고
    • Analysis of the code relating sequence to conformation in proteins: Possible implications for the mechanism of formation of helical regions
    • (1971) J. Mol. Biol. , vol.58 , pp. 237-259
    • Robson, B.1    Pain, R.H.2
  • 38
    • 0017105767 scopus 로고
    • Conformational properties of amino acid residues in globular proteins
    • (1976) J. Mol. Biol. , vol.107 , pp. 327-356
    • Robson, B.1
  • 40
    • 0016209912 scopus 로고
    • Structural principles of the globular organization of protein chains. A stereochemical theory of globular protein secondary structure
    • (1974) J. Mol. Biol. , vol.88 , pp. 857-872
    • Lim, V.I.1
  • 41
    • 0015243875 scopus 로고
    • Statistical analysis of the correlation among amino acid residues in helical, β‐structural and non‐regular regions of globular proteins
    • (1971) J. Mol. Biol. , vol.62 , pp. 613-624
    • Finkelstein, A.V.1    Ptitsyn, O.B.2
  • 49
    • 0024283401 scopus 로고
    • Improvements in a secondary structure prediction method based on a search for local sequence homologies and its use as a model building tool
    • (1988) Biochim. Biophys. Acta , vol.955 , pp. 283-295
    • Levin, J.M.1    Garnier, J.2
  • 50
    • 0024059423 scopus 로고
    • A simple method for predicting the secondary structure of globular proteins: Implications and accuracy
    • (1988) CABIOS , vol.4 , pp. 357-365
    • Gascuel, O.1    Golmard, J.L.2
  • 58
    • 0025026058 scopus 로고
    • Comparison of the structures of globing and phycocyanins: Evidence for evolutionary relationship
    • (1990) Proteins , vol.8 , pp. 133-155
    • Pastore, A.1    Lesk, A.M.2
  • 61
    • 0021028736 scopus 로고
    • Assessment of secondary structure prediction of proteins: Comparison of computerized Chou‐Fasman method with others
    • (1983) Biochim. Biophys. Acta , vol.748 , pp. 285-299
    • Nishikawa, K.1
  • 64
    • 0025935158 scopus 로고
    • Patterns of divergence in homologous proteins as indicators of secondary and tertiary structure of the catalytic domain of protein kinases
    • (1990) Adv. Enz. Reg. , vol.31 , pp. 121-181
    • Benner, S.A.1    Gerloff, D.2
  • 74
    • 84995034730 scopus 로고
    • Exercising multi‐layered networks on protein secondary structure. Elba, Italy: Int. J. Neural Syst.
    • (1992) , pp. 209-220
    • Rost, B.1    Sander, C.2
  • 79
    • 0020997912 scopus 로고
    • Dictionary of Protein secondary structure: Pattern recognition of hydrogen bonded and geometrical features
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 89
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • (1990) Proteins , vol.7 , pp. 205-214
    • Johnson, C.W.J.1
  • 92
    • 0020132173 scopus 로고
    • Correlation of the amino acid composition of a protein to its structural and biological characteristics
    • (1982) J. Biochem. , vol.91 , pp. 1821-1824
    • Nishikawa, K.1    Ooi, T.2
  • 101
    • 0024387058 scopus 로고
    • PRONET: A microcomputer program for predicting the secondary structure of proteins with a neural network
    • (1990) CABIOS , vol.5 , pp. 319-320
    • Bossa, F.1    Pascarella, S.2
  • 105
    • 84995083483 scopus 로고
    • How to make explicit a neural network trained to predict proteins secondary structure. ACASA, LAFORIA‐CNRS, Université Paris VI, 4 Place Jussieu, 75 252 Paris, CEDEX 05, France
    • (1993)
    • Tchoumatchenko, I.1    Vissotsky, F.2    Ganascia, J.‐G.3
  • 109
    • 0016259694 scopus 로고
    • Analysis of the code relating sequence to conformation in globular proteins‐Theory and application of expected information
    • (1974) Biochem. J. , vol.141 , pp. 853-867
    • Robson, B.1
  • 118
    • 0026447086 scopus 로고
    • Extracting information on folding from the amino acid sequence: Accurate predictions for protein regions with preferred conformation in the absence of tertiary interactions
    • (1992) Biochemistry , vol.31 , pp. 10226-10238
    • Rooman, M.J.1    Kocher, J.‐P.2    Wodak, S.J.3
  • 119
    • 0026458189 scopus 로고
    • Extracting information on folding from the amino acid sequence: Consensus regions with preferred conformation in homologous proteins
    • (1992) Biochemistry , vol.31 , pp. 10239-10249
    • Rooman, M.J.1    Wodak, S.J.2
  • 131
    • 0026734002 scopus 로고
    • Crystallographic structure and functional implications of the nitrogenase molybdenum‐iron protein from Azotobacter vinelandii
    • (1992) Nature (London) , vol.360 , pp. 553-560
    • Kim, J.1    Rees, D.C.2
  • 133
    • 0026628269 scopus 로고
    • Deconvolution of the circular dichroism spectra of proteins: The circular dichroism spectra of the antiparallel β‐sheet in proteins
    • (1992) Proteins , vol.13 , pp. 57-69
    • Perczel, A.1    Park, K.2    Fasman, G.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.