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Volumn 37, Issue SUPPL. 3, 1999, Pages 81-87

Comparative modeling of CASP3 targets using PSI-BLAST and SCWRL

Author keywords

Backbone dependent rotamer library; Comparative modeling; Homology modeling; PSI BLAST; Side chains, SCWRL

Indexed keywords

ALGORITHM; AMINO ACID SEQUENCE; ANALYTIC METHOD; ARTICLE; GENETIC PROCEDURES; MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; FACTUAL DATABASE; SEQUENCE ALIGNMENT;

EID: 0032613301     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(1999)37:3+<81::AID-PROT12>3.0.CO;2-R     Document Type: Article
Times cited : (67)

References (16)
  • 3
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B, Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 1994;19:55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 4
    • 0030595366 scopus 로고    scopus 로고
    • Multiple sequence information for threading algorithms
    • Defay TR, Cohen FE. Multiple sequence information for threading algorithms. J Mol Biol 1996;262:314-323.
    • (1996) J Mol Biol , vol.262 , pp. 314-323
    • Defay, T.R.1    Cohen, F.E.2
  • 5
    • 0031588926 scopus 로고    scopus 로고
    • Predicting the conformational class of short and medium size loops connecting regular secondary structures: Application to comparative modeling
    • Rufino SD, Donate LE, Canard LHJ, Blundell TL. Predicting the conformational class of short and medium size loops connecting regular secondary structures: application to comparative modeling. J Mol Biol 1997;267:352-367.
    • (1997) J Mol Biol , vol.267 , pp. 352-367
    • Rufino, S.D.1    Donate, L.E.2    Canard, L.H.J.3    Blundell, T.L.4
  • 7
    • 0029811308 scopus 로고    scopus 로고
    • Prediction and evaluation of side-chain conformations for protein backbone structures
    • Shenkin PS, Farid H, Fetrow JS. Prediction and evaluation of side-chain conformations for protein backbone structures. Proteins 1996;26:323-352.
    • (1996) Proteins , vol.26 , pp. 323-352
    • Shenkin, P.S.1    Farid, H.2    Fetrow, J.S.3
  • 8
    • 0031576989 scopus 로고    scopus 로고
    • Homology modeling with a backbone-dependent rotamer library
    • Bower M, Cohen FE, Dunbrack RLJ. Homology modeling with a backbone-dependent rotamer library. J Mol Biol 1997;267:1268-1282.
    • (1997) J Mol Biol , vol.267 , pp. 1268-1282
    • Bower, M.1    Cohen, F.E.2    Dunbrack, R.L.J.3
  • 9
    • 0027160197 scopus 로고
    • Backbone-dependent rotamer library for proteins: Application to sidechain prediction
    • Dunbrack RL, Jr, Karplus M. Backbone-dependent rotamer library for proteins: application to sidechain prediction. J Mol Biol 1993;230:543-571.
    • (1993) J Mol Biol , vol.230 , pp. 543-571
    • Dunbrack R.L., Jr.1    Karplus, M.2
  • 10
    • 0028429178 scopus 로고
    • Conformational analysis of the backbone-dependent rotamer preferences of protein sidechains
    • Dunbrack RL, Jr, Karplus M. Conformational analysis of the backbone-dependent rotamer preferences of protein sidechains. Nat Struct Biol 1994;1:334-340.
    • (1994) Nat Struct Biol , vol.1 , pp. 334-340
    • Dunbrack R.L., Jr.1    Karplus, M.2
  • 11
    • 1842326139 scopus 로고    scopus 로고
    • Bayesian statistical analysis of protein sidechain rotamer preferences
    • Dunbrack RL, Cohen FE. Bayesian statistical analysis of protein sidechain rotamer preferences. Protein Sci 1997;6:1661-1681.
    • (1997) Protein Sci , vol.6 , pp. 1661-1681
    • Dunbrack, R.L.1    Cohen, F.E.2
  • 12
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 14
    • 0029921425 scopus 로고    scopus 로고
    • A surface of minimum area metric for the structural comparison of proteins
    • Falicov A, Cohen FE. A surface of minimum area metric for the structural comparison of proteins. J Mol Biol 1996;258:871-892.
    • (1996) J Mol Biol , vol.258 , pp. 871-892
    • Falicov, A.1    Cohen, F.E.2
  • 15
    • 0031301954 scopus 로고    scopus 로고
    • Criteria for evaluating protein structures derived from comparative modeling
    • Venclovas C, Zemla A, Fidelis K, Moult J. Criteria for evaluating protein structures derived from comparative modeling. Proteins Suppl 1997;1:7-13.
    • (1997) Proteins Suppl , vol.1 , pp. 7-13
    • Venclovas, C.1    Zemla, A.2    Fidelis, K.3    Moult, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.