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Volumn 6, Issue 7, 1997, Pages 1467-1481

Statistical significance of hierarchical multi-body potentials based on Delaunay tessellation and their application in sequence-structure alignment

Author keywords

Delaunay tessellation; Fold recognition; High order interactions; Multi body potential; Protein folding; Threading potential

Indexed keywords

CARBON; FERREDOXIN; PROTEIN;

EID: 0030806961     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060711     Document Type: Article
Times cited : (82)

References (23)
  • 3
    • 0027318317 scopus 로고
    • An empirical energy function for threading protein sequence through the folding motif
    • Bryant SH, Lawrence CE. 1993. An empirical energy function for threading protein sequence through the folding motif. Proteins 16:92-112.
    • (1993) Proteins , vol.16 , pp. 92-112
    • Bryant, S.H.1    Lawrence, C.E.2
  • 5
    • 85053520810 scopus 로고
    • Local regression models
    • Chambers J, Hastie T, eds. New York: Chapman and Hall.
    • Cleveland W, Grosse E, Shyu W. 1992. Local regression models. In: Chambers J, Hastie T, eds. Statistical models in S. New York: Chapman and Hall. pp 309-376.
    • (1992) Statistical Models in S , pp. 309-376
    • Cleveland, W.1    Grosse, E.2    Shyu, W.3
  • 7
    • 0026726481 scopus 로고
    • Topology fingerprint approach to the inverse protein folding problem
    • Godzik A, Kolinski A, Skolnick J. 1992. Topology fingerprint approach to the inverse protein folding problem. J Mol Biol 227:227-283.
    • (1992) J Mol Biol , vol.227 , pp. 227-283
    • Godzik, A.1    Kolinski, A.2    Skolnick, J.3
  • 8
    • 0027645835 scopus 로고
    • De novo and inverse folding predictions of protein structure and dynamics
    • Godzik A, Kolinski A, Skolnick J. 1993. De novo and inverse folding predictions of protein structure and dynamics. J Comput Aided Mol Des 7:397-438.
    • (1993) J Comput Aided Mol des , vol.7 , pp. 397-438
    • Godzik, A.1    Kolinski, A.2    Skolnick, J.3
  • 9
    • 0027050011 scopus 로고
    • Sequence-structure matching in globular proteins: Application to supersecondary and tertiary structure determination
    • Godzik A, Skolnick J. 1992. Sequence-structure matching in globular proteins: Application to supersecondary and tertiary structure determination. Proc Natl Acad Sci USA 89:12098-12102.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 12098-12102
    • Godzik, A.1    Skolnick, J.2
  • 10
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm U, Sander C. 1994. Enlarged representative set of protein structures. Protein Sci 3:522-524.
    • (1994) Protein Sci , vol.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 11
    • 0026505184 scopus 로고
    • Evaluation of protein models by atomic solvation preference
    • Holm L, Sander C. 1992. Evaluation of protein models by atomic solvation preference. J Mol Biol 225:93-105.
    • (1992) J Mol Biol , vol.225 , pp. 93-105
    • Holm, L.1    Sander, C.2
  • 13
    • 0027522362 scopus 로고
    • Estimation of the maximum change in stability of globular proteins upon mutation of a hydrophobic residue to another of smaller size
    • Lee B. 1993. Estimation of the maximum change in stability of globular proteins upon mutation of a hydrophobic residue to another of smaller size. Protein Sci 2:733-738.
    • (1993) Protein Sci , vol.2 , pp. 733-738
    • Lee, B.1
  • 15
    • 0025908265 scopus 로고
    • The role of internal packing interactions in determining the structure and stability of a protein
    • Lim W, Sauer R. 1991. The role of internal packing interactions in determining the structure and stability of a protein. J Mol Biol 219:359-376.
    • (1991) J Mol Biol , vol.219 , pp. 359-376
    • Lim, W.1    Sauer, R.2
  • 16
    • 33845377127 scopus 로고
    • Estimation of effective interresidue contact energies from protein crystal structures: Quasi-chemical approximation
    • Miyazawa S, Jernigan RL. 1983. Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation. Macromolecules 18:534-552.
    • (1983) Macromolecules , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.L.2
  • 17
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O. 1995. Molten globule and protein folding. Adv Protein Chem 47:83-229.
    • (1995) Adv Protein Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.1
  • 18
    • 0030054951 scopus 로고    scopus 로고
    • Delaunay tessellation of proteins: Four-body nearest-neighbor propensities of amino-acid residues
    • Singh RK, Tropsha A, Vaisman I. 1996. Delaunay tessellation of proteins: Four-body nearest-neighbor propensities of amino-acid residues. J Comp Bio 3:213-221.
    • (1996) J Comp Bio , vol.3 , pp. 213-221
    • Singh, R.K.1    Tropsha, A.2    Vaisman, I.3
  • 19
    • 0029000696 scopus 로고
    • Knowledge-based potentials for proteins
    • Sippl MJ. 1995. Knowledge-based potentials for proteins. Curr Opin Struct Biol 5:229-235.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 229-235
    • Sippl, M.J.1
  • 20
    • 0029055313 scopus 로고
    • LINUS: A hierarchic procedure to predict the fold of a protein
    • Srinivasan R, Rose G. 1995. LINUS: A hierarchic procedure to predict the fold of a protein. Proteins 22:81-99.
    • (1995) Proteins , vol.22 , pp. 81-99
    • Srinivasan, R.1    Rose, G.2
  • 23
    • 0031310710 scopus 로고    scopus 로고
    • A new approach to protein fold recognition based on Delaunay tessellation of protein structure
    • Altman R, Dunker K, Hunter L, Klein T, eds. Maui, Hawaii: World Scientific Publishing Co. Pte. Ltd.
    • Zheng W, Cho S, Vaisman I, Tropsha A. 1997. A new approach to protein fold recognition based on Delaunay tessellation of protein structure. In: Altman R, Dunker K, Hunter L, Klein T, eds. Pacific Symposium on Biocomputing '97. Maui, Hawaii: World Scientific Publishing Co. Pte. Ltd. pp 486-497.
    • (1997) Pacific Symposium on Biocomputing '97 , pp. 486-497
    • Zheng, W.1    Cho, S.2    Vaisman, I.3    Tropsha, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.