메뉴 건너뛰기




Volumn 16, Issue 8, 2007, Pages 1557-1568

Local quality assessment in homology models using statistical potentials and support vector machines

Author keywords

Homology modeling; Model evaluation; Protein model; Protein structure prediction; Similarity measure; Statistical potential; Support vector machine

Indexed keywords

ARTICLE; GEOMETRY; NONHUMAN; PERFORMANCE; PRIORITY JOURNAL; PROTEIN STRUCTURE; QUALITY CONTROL; SCORING SYSTEM; SEQUENCE HOMOLOGY; STATISTICAL ANALYSIS; STRUCTURE ANALYSIS; SUPPORT VECTOR MACHINE;

EID: 34547576789     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.072856307     Document Type: Article
Times cited : (31)

References (58)
  • 1
    • 0031560777 scopus 로고    scopus 로고
    • Contact area difference (CAD): A robust measure to evaluate accuracy of protein models
    • Abagyan, R.A. and Totrov, M.M. 1997. Contact area difference (CAD): A robust measure to evaluate accuracy of protein models. J. Mol. Biol. 268: 678-685.
    • (1997) J. Mol. Biol , vol.268 , pp. 678-685
    • Abagyan, R.A.1    Totrov, M.M.2
  • 2
    • 0345827706 scopus 로고    scopus 로고
    • ProVal: A protein-scoring function for the selection of native and near-native folds
    • Berglund, A., Head, R.D., Welsh, E.A., and Marshall, G.R. 2004. ProVal: A protein-scoring function for the selection of native and near-native folds. Proteins 54: 289-302.
    • (2004) Proteins , vol.54 , pp. 289-302
    • Berglund, A.1    Head, R.D.2    Welsh, E.A.3    Marshall, G.R.4
  • 3
    • 0346492919 scopus 로고    scopus 로고
    • Orientation-dependent coarse-grained potentials derived by statistical analysis of molecular structural databases
    • Buchete, N.V., Straub, J.E., and Thirumalai, D. 2004a. Orientation-dependent coarse-grained potentials derived by statistical analysis of molecular structural databases. Polymer 45: 597-608.
    • (2004) Polymer , vol.45 , pp. 597-608
    • Buchete, N.V.1    Straub, J.E.2    Thirumalai, D.3
  • 4
    • 1842454935 scopus 로고    scopus 로고
    • Orientational potentials extracted from protein structures improve native fold recognition
    • Buchete, N.V., Straub, J.E., and Thirumalai, D. 2004b. Orientational potentials extracted from protein structures improve native fold recognition. Protein Sci. 13: 862-874.
    • (2004) Protein Sci , vol.13 , pp. 862-874
    • Buchete, N.V.1    Straub, J.E.2    Thirumalai, D.3
  • 6
    • 0027180507 scopus 로고
    • Verification of protein structures - Patterns of nonbonded atomic interactions
    • Colovos, C. and Yeates, T.O. 1993. Verification of protein structures - Patterns of nonbonded atomic interactions. Protein Sci. 2: 1511-1519.
    • (1993) Protein Sci , vol.2 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 7
    • 84964203940 scopus 로고
    • Bootstrap methods for standard errors, confidence intervals, and other measures of statistical accuracy
    • Efron, B. and Tibshirani, R. 1986. Bootstrap methods for standard errors, confidence intervals, and other measures of statistical accuracy. Stat. Sci. 1: 54-75.
    • (1986) Stat. Sci , vol.1 , pp. 54-75
    • Efron, B.1    Tibshirani, R.2
  • 8
    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D: Assessment of protein models with three-dimensional profiles
    • Eisenberg, D., Luthy, R., and Bowie, J.U. 1997. VERIFY3D: Assessment of protein models with three-dimensional profiles. Methods Enzymol. 277: 396-404.
    • (1997) Methods Enzymol , vol.277 , pp. 396-404
    • Eisenberg, D.1    Luthy, R.2    Bowie, J.U.3
  • 9
    • 33745726716 scopus 로고    scopus 로고
    • A composite score for predicting errors in protein structure models
    • Eramian, D., Shen, M.Y., Devos, D., Melo, F., Sali, A., and Marti-Renom, M.A. 2006. A composite score for predicting errors in protein structure models. Protein Sci. 15: 1653-1666.
    • (2006) Protein Sci , vol.15 , pp. 1653-1666
    • Eramian, D.1    Shen, M.Y.2    Devos, D.3    Melo, F.4    Sali, A.5    Marti-Renom, M.A.6
  • 10
    • 29144499905 scopus 로고    scopus 로고
    • Working set selection using the second order information for training SVM
    • Fan, R.E., Chen, P.H., and Lin, C.J. 2005. Working set selection using the second order information for training SVM. J. Mach. Learn. Res. 6: 1889-1918.
    • (2005) J. Mach. Learn. Res , vol.6 , pp. 1889-1918
    • Fan, R.E.1    Chen, P.H.2    Lin, C.J.3
  • 11
    • 19544371352 scopus 로고    scopus 로고
    • A consistent set of statistical potentials for quantifying local side-chain and backbone interactions
    • Fang, Q.J. and Shortle, D. 2005. A consistent set of statistical potentials for quantifying local side-chain and backbone interactions. Proteins 60: 90-96.
    • (2005) Proteins , vol.60 , pp. 90-96
    • Fang, Q.J.1    Shortle, D.2
  • 12
    • 0036836611 scopus 로고    scopus 로고
    • Evaluating CASP4 predictions with physical energy functions
    • Feig, M. and Brooks, C.L. 2002. Evaluating CASP4 predictions with physical energy functions. Proteins 49: 232-245.
    • (2002) Proteins , vol.49 , pp. 232-245
    • Feig, M.1    Brooks, C.L.2
  • 13
    • 0036681394 scopus 로고    scopus 로고
    • Distinguishing native conformations of proteins from decoys with an effective free energy estimator based on the OPLS all-atom force field and the surface generalized born solvent model
    • Felts, A.K., Gallicchio, E., Wallqvist, A., and Levy, R.M. 2002. Distinguishing native conformations of proteins from decoys with an effective free energy estimator based on the OPLS all-atom force field and the surface generalized born solvent model. Proteins 48: 404-422.
    • (2002) Proteins , vol.48 , pp. 404-422
    • Felts, A.K.1    Gallicchio, E.2    Wallqvist, A.3    Levy, R.M.4
  • 14
    • 14644400399 scopus 로고    scopus 로고
    • An amino acid has two sides: A new 2D measure provides a different view of solvent exposure
    • Hamelryck, T. 2005. An amino acid has two sides: A new 2D measure provides a different view of solvent exposure. Proteins 59: 38-48.
    • (2005) Proteins , vol.59 , pp. 38-48
    • Hamelryck, T.1
  • 15
    • 12844260161 scopus 로고    scopus 로고
    • Comparative protein structure modeling and its applications to drug discovery
    • Elsevier Academic Press Inc, San Diego, CA
    • Jacobson, M. and Sali, A. 2004. Comparative protein structure modeling and its applications to drug discovery. In Annual reports in medicinal chemistry, Vol. 39, pp. 259-276. Elsevier Academic Press Inc, San Diego, CA.
    • (2004) Annual reports in medicinal chemistry , vol.39 , pp. 259-276
    • Jacobson, M.1    Sali, A.2
  • 16
    • 0141978673 scopus 로고    scopus 로고
    • Comparative protein structure modeling by iterative alignment, model building, and model assessment
    • John, B. and Sali, A. 2003. Comparative protein structure modeling by iterative alignment, model building, and model assessment. Nucleic Acids Res. 31: 3982-3992.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3982-3992
    • John, B.1    Sali, A.2
  • 17
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on positionspecific scoring matrices
    • Jones, D.T. 1999. Protein secondary structure prediction based on positionspecific scoring matrices. J. Mol. Biol. 292: 195-202.
    • (1999) J. Mol. Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 18
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. 1983. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 20
    • 0037470581 scopus 로고    scopus 로고
    • An orientation-dependent hydrogen bonding potential improves prediction of specificity and structure for proteins and protein-protein complexes
    • Kortemme, T., Morozov, A.V., and Baker, D. 2003. An orientation-dependent hydrogen bonding potential improves prediction of specificity and structure for proteins and protein-protein complexes. J. Mol. Biol. 326: 1239-1259.
    • (2003) J. Mol. Biol , vol.326 , pp. 1239-1259
    • Kortemme, T.1    Morozov, A.V.2    Baker, D.3
  • 21
    • 0033531959 scopus 로고    scopus 로고
    • Discrimination of the native from misfolded protein models with an energy function including implicit solvation
    • Lazaridis, T. and Karplus, M. 1999. Discrimination of the native from misfolded protein models with an energy function including implicit solvation. J. Mol. Biol. 288: 477-487.
    • (1999) J. Mol. Biol , vol.288 , pp. 477-487
    • Lazaridis, T.1    Karplus, M.2
  • 22
    • 2442480826 scopus 로고    scopus 로고
    • Distinguish protein decoys by using a scoring function based on a new AMBER force field, short molecular dynamics simulations, and the generalized born solvent model
    • Lee, M.C. and Duan, Y. 2004. Distinguish protein decoys by using a scoring function based on a new AMBER force field, short molecular dynamics simulations, and the generalized born solvent model. Proteins 55: 620-634.
    • (2004) Proteins , vol.55 , pp. 620-634
    • Lee, M.C.1    Duan, Y.2
  • 23
    • 25444498862 scopus 로고    scopus 로고
    • Assessing local structural perturbations in proteins
    • doi: 10.1186/1471-2105-6-226
    • Lema, M.A. and Echave, J. 2005. Assessing local structural perturbations in proteins. BMC Bioinformatics doi: 10.1186/1471-2105-6-226.
    • (2005) BMC Bioinformatics
    • Lema, M.A.1    Echave, J.2
  • 25
    • 0035882533 scopus 로고    scopus 로고
    • A distance-dependent atomic knowledge-based potential for improved protein structure selection
    • Lu, H. and Skolnick, J. 2001. A distance-dependent atomic knowledge-based potential for improved protein structure selection. Proteins 44: 223-232.
    • (2001) Proteins , vol.44 , pp. 223-232
    • Lu, H.1    Skolnick, J.2
  • 26
    • 0026610767 scopus 로고
    • Assessment of protein models with 3-dimensional profiles
    • Luthy, R., Bowie, J.U., and Eisenberg, D. 1992. Assessment of protein models with 3-dimensional profiles. Nature 356: 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 27
    • 0031842640 scopus 로고    scopus 로고
    • Energy strain in three-dimensional protein structures
    • Maiorov, V. and Abagyan, R. 1998. Energy strain in three-dimensional protein structures. Folding Des. 3: 259-269.
    • (1998) Folding Des , vol.3 , pp. 259-269
    • Maiorov, V.1    Abagyan, R.2
  • 28
    • 0036122662 scopus 로고    scopus 로고
    • Reliability of assessment of protein structure prediction methods
    • Marti-Renom, M.A., Madhusudhan, M.S., Fiser, A., Rost, B., and Sali, A. 2002. Reliability of assessment of protein structure prediction methods. Structure 10: 435-440.
    • (2002) Structure , vol.10 , pp. 435-440
    • Marti-Renom, M.A.1    Madhusudhan, M.S.2    Fiser, A.3    Rost, B.4    Sali, A.5
  • 29
    • 0037452894 scopus 로고    scopus 로고
    • Discrimination of native protein structures using atom-atom contact scoring
    • McConkey, B.J., Sobolev, V., and Edelman, M. 2003. Discrimination of native protein structures using atom-atom contact scoring. Proc. Natl. Acad. Sci. 100: 3215-3220.
    • (2003) Proc. Natl. Acad. Sci , vol.100 , pp. 3215-3220
    • McConkey, B.J.1    Sobolev, V.2    Edelman, M.3
  • 30
    • 0032540222 scopus 로고    scopus 로고
    • Assessing protein structures with a non-local atomic interaction energy
    • Melo, F. and Feytmans, E. 1998. Assessing protein structures with a non-local atomic interaction energy. J. Mol. Biol. 277: 1141-1152.
    • (1998) J. Mol. Biol , vol.277 , pp. 1141-1152
    • Melo, F.1    Feytmans, E.2
  • 31
    • 0037485769 scopus 로고    scopus 로고
    • Combining inference from evolution and geometric probability in protein structure evaluation
    • Mihalek, I., Res, I., Yao, H., and Lichtarge, O. 2003. Combining inference from evolution and geometric probability in protein structure evaluation. J. Mol. Biol. 331: 263-279.
    • (2003) J. Mol. Biol , vol.331 , pp. 263-279
    • Mihalek, I.1    Res, I.2    Yao, H.3    Lichtarge, O.4
  • 32
    • 0242267517 scopus 로고    scopus 로고
    • Critical assessment of methods of protein structure prediction (CASP) - Round V
    • Moult, J., Fidelis, K., Zemla, A., and Hubbard, T. 2003. Critical assessment of methods of protein structure prediction (CASP) - Round V. Proteins 53: 334-339.
    • (2003) Proteins , vol.53 , pp. 334-339
    • Moult, J.1    Fidelis, K.2    Zemla, A.3    Hubbard, T.4
  • 33
    • 30344459116 scopus 로고    scopus 로고
    • Critical assessment of methods of protein structure prediction (CASP) - Round 6
    • Moult, J., Fidelis, K., Rost, B., Hubbard, T., and Tramontano, A. 2005. Critical assessment of methods of protein structure prediction (CASP) - Round 6. Proteins 61: 3-7.
    • (2005) Proteins , vol.61 , pp. 3-7
    • Moult, J.1    Fidelis, K.2    Rost, B.3    Hubbard, T.4    Tramontano, A.5
  • 34
    • 0001731773 scopus 로고
    • Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in the ECEPP/3 algorithm, with application to proline-containing peptides
    • Nemethy, G., Gibson, K.D., Palmer, K.A., Yoon, C.N., Paterlini, G., Zagari, A., Rumsey, S., and Scheraga, H.A. 1992. Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in the ECEPP/3 algorithm, with application to proline-containing peptides. J. Phys. Chem. 96: 6472-6484.
    • (1992) J. Phys. Chem , vol.96 , pp. 6472-6484
    • Nemethy, G.1    Gibson, K.D.2    Palmer, K.A.3    Yoon, C.N.4    Paterlini, G.5    Zagari, A.6    Rumsey, S.7    Scheraga, H.A.8
  • 35
    • 0031557390 scopus 로고    scopus 로고
    • Factors affecting the ability of energy functions to discriminate correct from incorrect folds
    • Park, B.H., Huang, E.S., and Levitt, M. 1997. Factors affecting the ability of energy functions to discriminate correct from incorrect folds. J. Mol. Biol. 266: 831-846.
    • (1997) J. Mol. Biol , vol.266 , pp. 831-846
    • Park, B.H.1    Huang, E.S.2    Levitt, M.3
  • 36
    • 0034486196 scopus 로고    scopus 로고
    • Free energy determinants of tertiary structure and the evaluation of protein models
    • Petrey, D. and Honig, B. 2000. Free energy determinants of tertiary structure and the evaluation of protein models. Protein Sci. 9: 2181-2191.
    • (2000) Protein Sci , vol.9 , pp. 2181-2191
    • Petrey, D.1    Honig, B.2
  • 37
    • 29144526714 scopus 로고    scopus 로고
    • Protein structure prediction: Inroads to biology
    • Petrey, D. and Honig, B. 2005. Protein structure prediction: Inroads to biology. Mol. Cell 20: 811-819.
    • (2005) Mol. Cell , vol.20 , pp. 811-819
    • Petrey, D.1    Honig, B.2
  • 39
    • 24144437430 scopus 로고    scopus 로고
    • Improving sequence-based fold recognition by using 3D model quality assessment
    • Pettitt, C.S., McGuffin, L.J., and Jones, D.T. 2005. Improving sequence-based fold recognition by using 3D model quality assessment. Bioinformatics 21: 3509-3515.
    • (2005) Bioinformatics , vol.21 , pp. 3509-3515
    • Pettitt, C.S.1    McGuffin, L.J.2    Jones, D.T.3
  • 40
    • 0033168866 scopus 로고    scopus 로고
    • Knowledge-based interaction potentials for proteins
    • Rojnuckarin, A. and Subramaniam, S. 1999. Knowledge-based interaction potentials for proteins. Proteins 36: 54-67.
    • (1999) Proteins , vol.36 , pp. 54-67
    • Rojnuckarin, A.1    Subramaniam, S.2
  • 41
    • 0027136282 scopus 로고
    • Comparative modelling by satisfaction of spatial constraints
    • Sali, A. and Blundell, T.L. 1993. Comparative modelling by satisfaction of spatial constraints. J. Mol. Biol. 234: 779-815.
    • (1993) J. Mol. Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 42
    • 0032488962 scopus 로고    scopus 로고
    • An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction
    • Samudrala, R. and Moult, J. 1998. An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction. J. Mol. Biol. 275: 895-916.
    • (1998) J. Mol. Biol , vol.275 , pp. 895-916
    • Samudrala, R.1    Moult, J.2
  • 43
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov, I.N. and Bourne, P.E. 1998. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11: 739-747.
    • (1998) Protein Eng , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 44
    • 0033670439 scopus 로고    scopus 로고
    • MaxSub: An automated measure for the assessment of protein structure prediction quality
    • Siew, N., Elofsson, A., Rychlewski, L., and Fischer, D. 2000. MaxSub: An automated measure for the assessment of protein structure prediction quality. Bioinformatics 16: 776-785.
    • (2000) Bioinformatics , vol.16 , pp. 776-785
    • Siew, N.1    Elofsson, A.2    Rychlewski, L.3    Fischer, D.4
  • 45
    • 0027490731 scopus 로고
    • Recognition of errors in 3-dimensional structures of proteins
    • Sippl, M.J. 1993. Recognition of errors in 3-dimensional structures of proteins. Proteins 17: 355-362.
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 46
    • 0029000696 scopus 로고
    • Knowledge-based potentials for proteins
    • Sippl, M.J. 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
  • 47
    • 24644464131 scopus 로고    scopus 로고
    • An atomic environment potential for use in protein structure prediction
    • Summa, C.M., Levitt, M., and DeGrado, W.F. 2005. An atomic environment potential for use in protein structure prediction. J. Mol. Biol. 352: 986-1001.
    • (2005) J. Mol. Biol , vol.352 , pp. 986-1001
    • Summa, C.M.1    Levitt, M.2    DeGrado, W.F.3
  • 48
    • 28144448406 scopus 로고    scopus 로고
    • The Victor/FRST function for model quality estimation
    • Tosatto, S.C.E. 2005. The Victor/FRST function for model quality estimation. J. Comput. Biol. 12: 1316-1327.
    • (2005) J. Comput. Biol , vol.12 , pp. 1316-1327
    • Tosatto, S.C.E.1
  • 49
    • 0037233516 scopus 로고    scopus 로고
    • Testing similarity measures with continuous and discrete protein models
    • Wallin, S., Farwer, J., and Bastolla, U. 2003. Testing similarity measures with continuous and discrete protein models. Proteins 50: 144-157.
    • (2003) Proteins , vol.50 , pp. 144-157
    • Wallin, S.1    Farwer, J.2    Bastolla, U.3
  • 50
    • 0037406141 scopus 로고    scopus 로고
    • Can correct protein models be identified?
    • Wallner, B. and Elofsson, A. 2003. Can correct protein models be identified? Protein Sci. 12: 1073-1086.
    • (2003) Protein Sci , vol.12 , pp. 1073-1086
    • Wallner, B.1    Elofsson, A.2
  • 51
    • 33645504195 scopus 로고    scopus 로고
    • Identification of correct regions in protein models using structural, alignment and consensus information
    • Wallner, B. and Elofsson, A. 2006. Identification of correct regions in protein models using structural, alignment and consensus information. Protein Sci. 15: 900-913.
    • (2006) Protein Sci , vol.15 , pp. 900-913
    • Wallner, B.1    Elofsson, A.2
  • 52
    • 1442322419 scopus 로고    scopus 로고
    • Detecting native protein folds among large decoy sets with the OPLS all-atom potential and the surface generalized born solvent model
    • John Wiley & Sons, New York
    • Wallqvist, A., Gallicchio, E., Felts, A.K., and Levy, R.M. 2002. Detecting native protein folds among large decoy sets with the OPLS all-atom potential and the surface generalized born solvent model. In Computational methods for protein folding, pp. 459-486. John Wiley & Sons, New York.
    • (2002) Computational methods for protein folding , pp. 459-486
    • Wallqvist, A.1    Gallicchio, E.2    Felts, A.K.3    Levy, R.M.4
  • 53
    • 0042622381 scopus 로고    scopus 로고
    • LGA: A method for finding 3D similarities in protein structures
    • Zemla, A. 2003. LGA: A method for finding 3D similarities in protein structures. Nucleic Acids Res. 31: 3370-3374.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3370-3374
    • Zemla, A.1
  • 54
    • 10344232638 scopus 로고    scopus 로고
    • Scoring function for automated assessment of protein structure template quality
    • Zhang, Y. and Skolnick, J. 2004. Scoring function for automated assessment of protein structure template quality. Proteins 57: 702-710.
    • (2004) Proteins , vol.57 , pp. 702-710
    • Zhang, Y.1    Skolnick, J.2
  • 55
    • 0036838311 scopus 로고    scopus 로고
    • Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction
    • Zhou, H.Y. and Zhou, Y.Q. 2002. Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction. Protein Sci. 11: 2714-2726.
    • (2002) Protein Sci , vol.11 , pp. 2714-2726
    • Zhou, H.Y.1    Zhou, Y.Q.2
  • 56
    • 2542631929 scopus 로고    scopus 로고
    • Single-body residue-level knowledge-based energy score combined with sequence-profile and secondary structure information for fold recognition
    • Zhou, H.Y. and Zhou, Y.Q. 2004. Single-body residue-level knowledge-based energy score combined with sequence-profile and secondary structure information for fold recognition. Proteins 55: 1005-1013.
    • (2004) Proteins , vol.55 , pp. 1005-1013
    • Zhou, H.Y.1    Zhou, Y.Q.2
  • 57
    • 11344292852 scopus 로고    scopus 로고
    • Fold recognition by combining sequence profiles derived from evolution and from depth-dependent structural alignment of fragments
    • Zhou, H.Y. and Zhou, Y.Q. 2005. Fold recognition by combining sequence profiles derived from evolution and from depth-dependent structural alignment of fragments. Proteins 58: 321-328.
    • (2005) Proteins , vol.58 , pp. 321-328
    • Zhou, H.Y.1    Zhou, Y.Q.2
  • 58
    • 33749037718 scopus 로고    scopus 로고
    • Structural refinement of protein segments containing secondary structure elements: Local sampling, knowledge-based potentials, and clustering
    • Zhu, J., Xie, L., and Honig, B. 2006. Structural refinement of protein segments containing secondary structure elements: Local sampling, knowledge-based potentials, and clustering. Proteins 65: 463-479.
    • (2006) Proteins , vol.65 , pp. 463-479
    • Zhu, J.1    Xie, L.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.