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Volumn 8, Issue 5, 1998, Pages 631-639

Validation of protein models derived from experiment

Author keywords

[No Author keywords available]

Indexed keywords

LYSOZYME;

EID: 0031766271     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80156-5     Document Type: Article
Times cited : (156)

References (55)
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    • of outstanding interest. A powerful method for identifying regions where there are unusual atom - atom interactions, suggesting possible point errors in the structure. Can also detect misalignments in homology-built models and assess the model as a whole. Uses 'non-local energies' calculated from an atomic mean force potential and is available on the Web at http://www.fundp.ac.be/pub/ANOLEA.html
    • Melo F, Feytmans E. Assessing protein structures with a non-local atomic interaction energy. of outstanding interest J Mol Biol. 277:1998;1141-1152 A powerful method for identifying regions where there are unusual atom - atom interactions, suggesting possible point errors in the structure. Can also detect misalignments in homology-built models and assess the model as a whole. Uses 'non-local energies' calculated from an atomic mean force potential and is available on the Web at http://www.fundp.ac.be/pub/ANOLEA.html.
    • (1998) J Mol Biol , vol.277 , pp. 1141-1152
    • Melo, F.1    Feytmans, E.2
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    • Novel knowledge-based mean force potential at atomic level
    • Melo F, Feytmans E. Novel knowledge-based mean force potential at atomic level. J Mol Biol. 267:1997;207-222.
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    • Melo, F.1    Feytmans, E.2
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    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D: Assessment of protein models with three-dimensional profiles
    • of special interest. Describes the VERIFY3D program, which assesses whether a protein model is compatible with its sequence in terms of the local environments at each residue position. The program can be run via the Web at http://www.doe-mbi.ucla.edu/verify3d.html
    • Eisenberg D, Lüthy R, Bowie JU. VERIFY3D: assessment of protein models with three-dimensional profiles. of special interest Methods Enzymol. 277:1997;396-404 Describes the VERIFY3D program, which assesses whether a protein model is compatible with its sequence in terms of the local environments at each residue position. The program can be run via the Web at http://www.doe-mbi.ucla.edu/verify3d.html.
    • (1997) Methods Enzymol , vol.277 , pp. 396-404
    • Eisenberg, D.1    Lüthy, R.2    Bowie, J.U.3
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    • Validation of protein models from C-alpha coordinates alone
    • α-only structures. The program, MOLEMAN2, is available via the Web at http://alpha2.bmc.uu.se/~gerard/manuals/
    • α-only structures. The program, MOLEMAN2, is available via the Web at http://alpha2.bmc.uu.se/~gerard/manuals/.
    • (1997) J Mol Biol , vol.273 , pp. 371-376
    • Kleywegt, G.J.1
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    • 0030589514 scopus 로고    scopus 로고
    • Phi/psi-chology: Ramachandran revisited
    • Kleywegt GJ, Jones TA. Phi/psi-chology: Ramachandran revisited. Structure. 4:1996;1395-1400.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 54
    • 0030870075 scopus 로고    scopus 로고
    • Objectively judging the quality of a protein structure from a Ramachandran plot
    • of special interest. Provides a method for computing an 'objective score' for a protein structure, and for individual residues, according to where each residue falls on the Ramachandran plot based on observed Ramachandran distributions for each residue type. The method is incorporated into the WHAT_CHECK program [46].
    • Hooft RWW, Sander C, Vriend G. Objectively judging the quality of a protein structure from a Ramachandran plot. of special interest Comput Appl Biosci. 13:1997;425-430 Provides a method for computing an 'objective score' for a protein structure, and for individual residues, according to where each residue falls on the Ramachandran plot based on observed Ramachandran distributions for each residue type. The method is incorporated into the WHAT_CHECK program [46].
    • (1997) Comput Appl Biosci , vol.13 , pp. 425-430
    • Hooft, R.W.W.1    Sander, C.2    Vriend, G.3
  • 55
    • 0032215320 scopus 로고    scopus 로고
    • Databases in protein crystallography
    • building, refinement, validation and analysis in protein crystallography, including the HETZE program, which validates the geometry of hetero compounds of special interest
    • Kleywegt GJ, Jones TA. Databases in protein crystallography. of special interest Acta Crystallogr D - Biol Crystallogr. 54:1998; A summary of the use of databases for model-building, refinement, validation and analysis in protein crystallography, including the HETZE program, which validates the geometry of hetero compounds.
    • (1998) Acta Crystallogr D - Biol Crystallogr , vol.54
    • Kleywegt, G.J.1    Jones, T.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.