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Volumn 4, Issue 4, 1996, Pages 363-366

Knowledge-based potentials for protein folding: What can we learn from known protein structures?

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 0030584681     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00041-X     Document Type: Article
Times cited : (62)

References (14)
  • 1
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    • Anfinsen, C.B.1
  • 2
    • 0028818340 scopus 로고
    • Protein structure prediction by threading methods: Evaluation of current techniques
    • Lemer, C., Rooman, M. & Wodak, S. (1995). Protein structure prediction by threading methods: evaluation of current techniques. Proteins 23, 337-355.
    • (1995) Proteins , vol.23 , pp. 337-355
    • Lemer, C.1    Rooman, M.2    Wodak, S.3
  • 3
    • 0028326042 scopus 로고
    • Monte Carlo simulations of protein folding II. Application to Protein A, ROP and Crambin
    • Kolinski, A. & Skolnick, J. (1994). Monte Carlo simulations of protein folding II. Application to Protein A, ROP and Crambin. Proteins 18, 353-366
    • (1994) Proteins , vol.18 , pp. 353-366
    • Kolinski, A.1    Skolnick, J.2
  • 4
    • 0029055313 scopus 로고
    • LINUS: A hierarchical procedure to predict the fold of a protein
    • Srinivasan, R. & Rose, G.D. (1995). LINUS: a hierarchical procedure to predict the fold of a protein. Proteins 22, 81-99.
    • (1995) Proteins , vol.22 , pp. 81-99
    • Srinivasan, R.1    Rose, G.D.2
  • 5
    • 0017021957 scopus 로고
    • Medium and long range interaction parameters between amino acids for predicting three-dimensional structures of proteins
    • Tanaka, S. & Scheraga, H.A. (1976). Medium and long range interaction parameters between amino acids for predicting three-dimensional structures of proteins. Macromolecules 9, 945-950.
    • (1976) Macromolecules , vol.9 , pp. 945-950
    • Tanaka, S.1    Scheraga, H.A.2
  • 6
    • 0029563695 scopus 로고
    • Are database-derived potentials valid for scoring both forward and inverted protein folding?
    • Rooman, M.J. & Wodak, S.J. (1995). Are database-derived potentials valid for scoring both forward and inverted protein folding? Protein Eng. 8, 849-858.
    • (1995) Protein Eng. , vol.8 , pp. 849-858
    • Rooman, M.J.1    Wodak, S.J.2
  • 7
    • 0028892389 scopus 로고
    • Are proteins ideal mixtures of amino acids? Analysis of energy parameter sets
    • Godzik, A., Kolinski, A. & Skolnick, J. (1995). Are proteins ideal mixtures of amino acids? Analysis of energy parameter sets. Protein Sci. 4, 2107-2117.
    • (1995) Protein Sci. , vol.4 , pp. 2107-2117
    • Godzik, A.1    Kolinski, A.2    Skolnick, J.3
  • 10
    • 33845377127 scopus 로고
    • Estimation of effective interresidue contact energies from protein crystal structures: Quasi-chemical approximation
    • Miyazawa, S. & Jernigan, R.L. (1985). Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation. Macromolecules 18, 534-552
    • (1985) Macromolecules , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.L.2
  • 11
    • 0026726481 scopus 로고
    • A topology fingerprint approach to the inverse folding problem
    • Godzik, A., Skolnick, J. & Kolinski, A. (1992). A topology fingerprint approach to the inverse folding problem. J. Mol. Biol. 227, 227-238
    • (1992) J. Mol. Biol. , vol.227 , pp. 227-238
    • Godzik, A.1    Skolnick, J.2    Kolinski, A.3
  • 12
    • 0026785519 scopus 로고
    • Contact potential that recognizes the correct folding of globular proteins
    • Maiorov, V.N. & Crippen, G.M. (1992). Contact potential that recognizes the correct folding of globular proteins. J. Mol. Biol. 277, 876-888.
    • (1992) J. Mol. Biol. , vol.277 , pp. 876-888
    • Maiorov, V.N.1    Crippen, G.M.2
  • 13
    • 0030310479 scopus 로고    scopus 로고
    • Statistical geometry analysis of proteins: Implications for inverted structure predictions
    • (Hunter, L. & Klein, T.E., eds), World Scientific Press, Singapore
    • Tropsha, A., Singh, R.K., Vaisman, I.I. & Zheng. W. (1996). Statistical geometry analysis of proteins: implications for inverted structure predictions. In Pacific Symposium on Biocomputing. (Hunter, L. & Klein, T.E., eds), pp.614-623, World Scientific Press, Singapore.
    • (1996) In Pacific Symposium on Biocomputing. , pp. 614-623
    • Tropsha, A.1    Singh, R.K.2    Vaisman, I.I.3    Zheng, W.4
  • 14
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    • Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins
    • Cornette, J.L., Cease, K.B., Margalit, H., Spouge, J.L., Berzofsky, J.A. & DeLisi, C. (1987). Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins. J. Mol. Biol. 195, 659-685.
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    • Cornette, J.L.1    Cease, K.B.2    Margalit, H.3    Spouge, J.L.4    Berzofsky, J.A.5    DeLisi, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.