메뉴 건너뛰기




Volumn 277, Issue 5, 1998, Pages 1141-1152

Assessing protein structures with a non-local atomic interaction energy

Author keywords

Comparative modeling; Homology modeling; Knowledge based mean force potentials; Protein structure prediction; Three dimensional energy profiles

Indexed keywords

PROTEIN;

EID: 0032540222     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1665     Document Type: Article
Times cited : (432)

References (32)
  • 1
    • 0031560777 scopus 로고    scopus 로고
    • Contact area difference (CAD) a robust measure to evaluate accuracy of protein models
    • Abagyan R.A., Totrov M.M. Contact area difference (CAD) a robust measure to evaluate accuracy of protein models. J. Mol. Biol. 268:1997;678-685
    • (1997) J. Mol. Biol. , vol.268 , pp. 678-685
    • Abagyan, R.A.1    Totrov, M.M.2
  • 3
    • 0001644632 scopus 로고
    • Between objectivity and subjectivity
    • Brandén C.-I., Jones T.A. Between objectivity and subjectivity. Nature. 343:1990;687-689
    • (1990) Nature , vol.343 , pp. 687-689
    • Brandén, C.-I.1    Jones, T.A.2
  • 6
    • 0030627637 scopus 로고    scopus 로고
    • Meeting review: The second meeting on the critical assessment of techniques for protein structure prediction (CASP2)
    • Asilomar, California, December 13-16, 1996
    • Dunbrack R.L., Gerloff D.L., Bower M., Chen X., Lichtarge O., Cohen F.E. Meeting review the second meeting on the critical assessment of techniques for protein structure prediction (CASP2). Folding Des. 2:1997;R27-R42. Asilomar, California, December 13-16, 1996
    • (1997) Folding Des. , vol.2
    • Dunbrack, R.L.1    Gerloff, D.L.2    Bower, M.3    Chen, X.4    Lichtarge, O.5    Cohen, F.E.6
  • 8
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm U., Sander C. Enlarged representative set of protein structures. Protein Sci. 3:1994;522
    • (1994) Protein Sci. , vol.3 , pp. 522
    • Hobohm, U.1    Sander, C.2
  • 10
    • 0026505184 scopus 로고
    • Evaluation of protein models by atomic solvation preference
    • Holm L., Sander C. Evaluation of protein models by atomic solvation preference. J. Mol. Biol. 225:1992;93-105
    • (1992) J. Mol. Biol. , vol.225 , pp. 93-105
    • Holm, L.1    Sander, C.2
  • 11
    • 0029644940 scopus 로고
    • Where freedom is given, liberties are taken
    • Kleywegt G.J., Jones T.A. Where freedom is given, liberties are taken. Structure. 3:1995;535-540
    • (1995) Structure , vol.3 , pp. 535-540
    • Kleywegt, G.J.1    Jones, T.A.2
  • 12
    • 0030512814 scopus 로고    scopus 로고
    • A re-evaluation of the crystal structure of chloromuconate cycloisomerase
    • Kleywegt G.J., Hoier H., Jones T.A. A re-evaluation of the crystal structure of chloromuconate cycloisomerase. Acta Crystallog. Sect. D. 52:1996;858-863
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 858-863
    • Kleywegt, G.J.1    Hoier, H.2    Jones, T.A.3
  • 13
    • 0028169501 scopus 로고
    • Torsion angle differences as a means of pinpointing local polypeptide chain trajectory changes for identical proteins in different conformational states
    • Korn A., Rose D.R. Torsion angle differences as a means of pinpointing local polypeptide chain trajectory changes for identical proteins in different conformational states. Protein Eng. 7:1994;961-967
    • (1994) Protein Eng. , vol.7 , pp. 961-967
    • Korn, A.1    Rose, D.R.2
  • 15
    • 0028818340 scopus 로고
    • Protein structure prediction by threading methods: Evaluation of current techniques
    • Lemer C.M.R., Rooman M.J., Wodak S. Protein structure prediction by threading methods evaluation of current techniques. Proteins Struct. Funct. Genet. 23:1995;337-355
    • (1995) Proteins Struct. Funct. Genet. , vol.23 , pp. 337-355
    • Lemer, C.M.R.1    Rooman, M.J.2    Wodak, S.3
  • 16
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R., Bowie J.U., Eisenberg D. Assessment of protein models with three-dimensional profiles. Nature. 356:1992;83-85
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 17
    • 0001118230 scopus 로고
    • Some thoughts on choosing the correct space group
    • Marsh R.E. Some thoughts on choosing the correct space group. Acta Crystallog. sect. B,. 51:1995;897-907
    • (1995) Acta Crystallog. Sect. B , vol.51 , pp. 897-907
    • Marsh, R.E.1
  • 18
    • 0031582083 scopus 로고    scopus 로고
    • 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
    • (1997) J. Mol. Biol. , vol.267 , pp. 207-222
    • Melo, F.1    Feytmans, E.2
  • 19
    • 0028864205 scopus 로고
    • A critical assessment of comparative molecular modeling of tertiary structures of proteins
    • Mosimann S., Meleshko R., James M.N.G. A critical assessment of comparative molecular modeling of tertiary structures of proteins. Proteins Struct. Funct. Genet. 23:1995;301-317
    • (1995) Proteins Struct. Funct. Genet. , vol.23 , pp. 301-317
    • Mosimann, S.1    Meleshko, R.2    James, M.N.G.3
  • 22
    • 0031557390 scopus 로고    scopus 로고
    • Factors affecting the ability of energy functions to discriminate correct from incorrect folds
    • Park B.H., Huang E.S., Levitt M. Factors affecting the ability of energy functions to discriminate correct from incorrect folds. J. Mol. Biol. 266:1997;831-846
    • (1997) J. Mol. Biol. , vol.266 , pp. 831-846
    • Park, B.H.1    Huang, E.S.2    Levitt, M.3
  • 23
    • 0030598343 scopus 로고    scopus 로고
    • Deviations from standard atomic volumes as a quality measure for protein crystal structures
    • Pontius J., Richelle J., Wodak S.J. Deviations from standard atomic volumes as a quality measure for protein crystal structures. J. Mol. Biol. 264:1996;121-136
    • (1996) J. Mol. Biol. , vol.264 , pp. 121-136
    • Pontius, J.1    Richelle, J.2    Wodak, S.J.3
  • 24
    • 0021766631 scopus 로고
    • Critical evaluation of comparative model-building of Streptomyces griseus trypsin
    • Read R.J., Brayer G.D., Jurasek L., James M.N.G. Critical evaluation of comparative model-building of Streptomyces griseus trypsin. Biochemistry. 23:1984;6570-6575
    • (1984) Biochemistry , vol.23 , pp. 6570-6575
    • Read, R.J.1    Brayer, G.D.2    Jurasek, L.3    James, M.N.G.4
  • 25
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 28
    • 0025341310 scopus 로고
    • Calculation of conformational ensembles from potentials of mean force
    • Sippl M.J. Calculation of conformational ensembles from potentials of mean force. J. Mol. Biol. 213:1990;859-883
    • (1990) J. Mol. Biol. , vol.213 , pp. 859-883
    • Sippl, M.J.1
  • 29
    • 0027650879 scopus 로고
    • Boltzmann's principle, knowledge-based mean fields and protein folding. An approach to the computational determination of protein structures
    • Sippl M.J. Boltzmann's principle, knowledge-based mean fields and protein folding. An approach to the computational determination of protein structures. J-CAMD. 7:1993;473-501
    • (1993) J-CAMD , vol.7 , pp. 473-501
    • Sippl, M.J.1
  • 30
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl M.J. Recognition of errors in three-dimensional structures of proteins. Proteins Struct. Funct. Genet. 17:1993;355-362
    • (1993) Proteins Struct. Funct. Genet. , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 31
    • 0029000696 scopus 로고
    • Knowledge-based potentials for proteins
    • Sippl M.J. Knowledge-based potentials for proteins. Curr. Opin. Struct. Biol. 5:1995;229-235
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 229-235
    • Sippl, M.J.1
  • 32
    • 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
    • Sippl M.J., Weitckus S. Detection of native-like models for amino acid sequences of unknown three-dimensional structure in a data base of known protein conformations. Proteins: Struct. Funct. Genet. 13:1992;258-271
    • (1992) Proteins: Struct. Funct. Genet. , vol.13 , pp. 258-271
    • Sippl, M.J.1    Weitckus, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.