메뉴 건너뛰기




Volumn 268, Issue 3, 1997, Pages 678-685

Contact area difference (CAD): A robust measure to evaluate accuracy of protein models

Author keywords

Loop modeling; Modeling by homology; Protein structure prediction; Side chain placement; Structure evaluation

Indexed keywords

PROTEIN;

EID: 0031560777     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.0994     Document Type: Article
Times cited : (79)

References (25)
  • 1
    • 0026681839 scopus 로고
    • Optimal protocol and trajectory visualization for conformational searches of peptides and proteins
    • Abagyan R. A., Argos P. Optimal protocol and trajectory visualization for conformational searches of peptides and proteins. J. Mol. Biol. 225:1992;519-532.
    • (1992) J. Mol. Biol. , vol.225 , pp. 519-532
    • Abagyan, R.A.1    Argos, P.2
  • 2
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
    • Abagyan R. A., Totrov M. M. Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins. J. Mol. Biol. 235:1994;983-1002.
    • (1994) J. Mol. Biol. , vol.235 , pp. 983-1002
    • Abagyan, R.A.1    Totrov, M.M.2
  • 3
    • 84986522918 scopus 로고
    • ICM: A new method for structure modeling and design: Applications to docking and structure prediction from the distorted native conformation
    • Abagyan R. A., Totrov M. M., Kuznetsov D. A. ICM: a new method for structure modeling and design: applications to docking and structure prediction from the distorted native conformation. J. Comput. Chem. 15:1994;488-506.
    • (1994) J. Comput. Chem. , vol.15 , pp. 488-506
    • Abagyan, R.A.1    Totrov, M.M.2    Kuznetsov, D.A.3
  • 5
    • 0020598457 scopus 로고
    • Representation of short and long-range handedness in protein structures by signed distance maps
    • Braun W. Representation of short and long-range handedness in protein structures by signed distance maps. J. Mol. Biol. 163:1983;613-621.
    • (1983) J. Mol. Biol. , vol.163 , pp. 613-621
    • Braun, W.1
  • 6
    • 0024373407 scopus 로고
    • Conservation of residue interactions in a family of Ca binding proteins
    • Godzik A., Sander C. Conservation of residue interactions in a family of Ca binding proteins. Protein Eng. 2:1989;589-596.
    • (1989) Protein Eng. , vol.2 , pp. 589-596
    • Godzik, A.1    Sander, C.2
  • 8
    • 0029010695 scopus 로고
    • Kinetics of protein folding: Nucleation mechanism, time scales and pathways
    • Guo Z., Thirumalai D. Kinetics of protein folding: nucleation mechanism, time scales and pathways. Biopolymers. 36:1995;83-102.
    • (1995) Biopolymers , vol.36 , pp. 83-102
    • Guo, Z.1    Thirumalai, D.2
  • 9
    • 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;92-105.
    • (1992) J. Mol. Biol. , vol.225 , pp. 92-105
    • Holm, L.1    Sander, C.2
  • 10
    • 0030501419 scopus 로고    scopus 로고
    • Use of Non-crystallographic Symmetry in Protein Structure Refinement
    • Kleywegt G. J. Use of Non-crystallographic Symmetry in Protein Structure Refinement. Acta Crystallog. 52:1996;842-857.
    • (1996) Acta Crystallog. , vol.52 , pp. 842-857
    • Kleywegt, G.J.1
  • 11
    • 0016860272 scopus 로고
    • An approach to the tertiary structure of globular proteins
    • Kuntz I. D. An approach to the tertiary structure of globular proteins. J. Am. Chem. Soc. 97:1975;4362-4366.
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 4362-4366
    • Kuntz, I.D.1
  • 12
    • 0028818340 scopus 로고
    • Protein structure prediction by threading methods: Evaluation of current techniques
    • Lemer C. M.-R., Rooman M. J., Wodak S. J. 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.J.3
  • 14
    • 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
  • 17
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman S. B., Wunch C. D. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48:1970;443-453.
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunch, C.D.2
  • 18
    • 0015949278 scopus 로고
    • Comparison of homologous tertiary structures of proteins
    • Nishikawa K., Ooi T. Comparison of homologous tertiary structures of proteins. J. Theoret. Biol. 43:1974;351-374.
    • (1974) J. Theoret. Biol. , vol.43 , pp. 351-374
    • Nishikawa, K.1    Ooi, T.2
  • 19
    • 0014898597 scopus 로고
    • The development of crystallographic enzymology
    • Phillips D. C. The development of crystallographic enzymology. Biochem. Soc Symp. 31:1970;11-28.
    • (1970) Biochem. Soc Symp. , vol.31 , pp. 11-28
    • Phillips, D.C.1
  • 20
    • 0016255253 scopus 로고
    • Recognition of structural domains in globular proteins
    • Rossmann M. G., Liljas A. Recognition of structural domains in globular proteins. J. Mol. Biol. 85:1974;177-181.
    • (1974) J. Mol. Biol. , vol.85 , pp. 177-181
    • Rossmann, M.G.1    Liljas, A.2
  • 21
    • 0028081403 scopus 로고
    • Structural features can be unconserved in proteins with similar folds. An analysis of side-chain to side-chaincontacts secondary structure and accessibility
    • Russell R. B., Barton G. J. Structural features can be unconserved in proteins with similar folds. An analysis of side-chain to side-chaincontacts secondary structure and accessibility. J. Mol. Biol. 244:1994;332-350.
    • (1994) J. Mol. Biol. , vol.244 , pp. 332-350
    • Russell, R.B.1    Barton, G.J.2
  • 23
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms. Lysozyme and Insulin
    • Shrake A., Rupley J. A. Environment and exposure to solvent of protein atoms. Lysozyme and Insulin. J. Mol. Biol. 79:1973;351-371.
    • (1973) J. Mol. Biol. , vol.79 , pp. 351-371
    • Shrake, A.1    Rupley, J.A.2
  • 24
    • 0025608908 scopus 로고
    • Simulations of the folding of a globular protein
    • Skolnick J., Kolinski A. Simulations of the folding of a globular protein. Science. 250:1990;1121-1125.
    • (1990) Science , vol.250 , pp. 1121-1125
    • Skolnick, J.1    Kolinski, A.2
  • 25
    • 0026179489 scopus 로고
    • A new approach to the rapid determination of protein side chain conformations
    • Tuffery P., Etchebest C., Hazout S., Lavery R. A new approach to the rapid determination of protein side chain conformations. J. Biomol. Struct. Dynam. 8:1991;1267-1289.
    • (1991) J. Biomol. Struct. Dynam. , vol.8 , pp. 1267-1289
    • Tuffery, P.1    Etchebest, C.2    Hazout, S.3    Lavery, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.