메뉴 건너뛰기




Volumn 67, Issue 2, 2007, Pages 385-399

Local motions in a benchmark of allosteric proteins

Author keywords

Allosteric protein structure; Conformational change; Protein crystal structure database; Protein flexibility; Protein motion

Indexed keywords

DNA BINDING PROTEIN; ENZYME; GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN KINASE; PROTEOME; REGULATOR PROTEIN;

EID: 33947419241     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21300     Document Type: Article
Times cited : (99)

References (67)
  • 2
    • 0000648204 scopus 로고
    • On the structure of native, denatured, and coagulated proteins
    • Mirsky AE, Pauling L. On the structure of native, denatured, and coagulated proteins. Proc Natl Acad Sci USA 1936;22:439-447.
    • (1936) Proc Natl Acad Sci USA , vol.22 , pp. 439-447
    • Mirsky, A.E.1    Pauling, L.2
  • 3
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. Principles that govern the folding of protein chains. Science 1973;181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 4
    • 73649152457 scopus 로고
    • Allosteric proteins and cellular control systems
    • Monod J, Changeux JP, Jacob F. Allosteric proteins and cellular control systems. J Mol Biol 1963;6:306-329.
    • (1963) J Mol Biol , vol.6 , pp. 306-329
    • Monod, J.1    Changeux, J.P.2    Jacob, F.3
  • 5
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J, Changeux JP. On the nature of allosteric transitions: a plausible model. J Mol Biol 1965;12:88-118.
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 6
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland DE, Jr, Nemethy G, Filmer D. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 1966;5:365-385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland Jr, D.E.1    Nemethy, G.2    Filmer, D.3
  • 7
    • 0030433170 scopus 로고    scopus 로고
    • Protein dynamics and conformational transitions in allosteric proteins
    • Jardetzky O. Protein dynamics and conformational transitions in allosteric proteins. Prog Biophys Mol Biol 1996;65:171-219.
    • (1996) Prog Biophys Mol Biol , vol.65 , pp. 171-219
    • Jardetzky, O.1
  • 8
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter IR, Wittinghofer A. The guanine nucleotide-binding switch in three dimensions. Science 2001;294:1299-1304.
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 9
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M, Kuriyan J. The conformational plasticity of protein kinases. Cell 2002;109:275-282.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 10
    • 0033970020 scopus 로고    scopus 로고
    • Folding and binding cascades: Dynamic landscapes and population shifts
    • Kumar S, Ma B, Tsai CJ, Sinha N, Nussinov R. Folding and binding cascades: dynamic landscapes and population shifts. Protein Sci 2000;9:10-19.
    • (2000) Protein Sci , vol.9 , pp. 10-19
    • Kumar, S.1    Ma, B.2    Tsai, C.J.3    Sinha, N.4    Nussinov, R.5
  • 11
    • 0036088602 scopus 로고    scopus 로고
    • The linkage between protein folding and functional cooperativity: Two sides of the same coin?
    • Luque I, Leavitt SA, Freire E. The linkage between protein folding and functional cooperativity: two sides of the same coin? Annu Rev Biophys Biomol Struct 2002;31:235-256.
    • (2002) Annu Rev Biophys Biomol Struct , vol.31 , pp. 235-256
    • Luque, I.1    Leavitt, S.A.2    Freire, E.3
  • 12
    • 6344219895 scopus 로고    scopus 로고
    • Is allostery an intrinsic property of all dynamic proteins?
    • Gunasekaran K, Ma B, Nussinov R. Is allostery an intrinsic property of all dynamic proteins? Proteins 2004;57:433-443.
    • (2004) Proteins , vol.57 , pp. 433-443
    • Gunasekaran, K.1    Ma, B.2    Nussinov, R.3
  • 13
    • 0028237708 scopus 로고
    • Structural determinants for activation of the α-subunit of a heterotrimeric G protein
    • Lambright DG, Noel JP, Hamm HE, Sigler PB. Structural determinants for activation of the α-subunit of a heterotrimeric G protein. Nature 1994;369:621-628.
    • (1994) Nature , vol.369 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 15
    • 0028144138 scopus 로고
    • Aspartate transcarbamylase from Escherichia coli: Activity and regulation
    • Lipscomb WN. Aspartate transcarbamylase from Escherichia coli: activity and regulation. Adv Enzymol Relat Areas Mol Biol 1994;68:67-151.
    • (1994) Adv Enzymol Relat Areas Mol Biol , vol.68 , pp. 67-151
    • Lipscomb, W.N.1
  • 16
    • 0026033985 scopus 로고
    • Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP
    • Barford D, Hu SH, Johnson LN. Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP. J Mol Biol 1991;218:233-260.
    • (1991) J Mol Biol , vol.218 , pp. 233-260
    • Barford, D.1    Hu, S.H.2    Johnson, L.N.3
  • 17
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz MF. Stereochemistry of cooperative effects in haemoglobin. Nature 1970;228:726-739.
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.F.1
  • 18
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single-domain signaling protein
    • Volkman BF, Lipson D, Wemmer DE, Kern D. Two-state allosteric behavior in a single-domain signaling protein. Science 2001; 291:2429-2433.
    • (2001) Science , vol.291 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.E.3    Kern, D.4
  • 20
    • 0346220393 scopus 로고    scopus 로고
    • The role of dynamics in allosteric regulation
    • Kern D, Zuiderweg ER. The role of dynamics in allosteric regulation. Curr Opin Struct Biol 2003;13:748-757.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 748-757
    • Kern, D.1    Zuiderweg, E.R.2
  • 21
    • 0016606973 scopus 로고
    • Structural invariants in protein folding
    • Chothia C. Structural invariants in protein folding. Nature 1975; 254:304-308.
    • (1975) Nature , vol.254 , pp. 304-308
    • Chothia, C.1
  • 22
    • 0025326950 scopus 로고
    • Relations between protein sequence and structure and their significance
    • Rooman MJ, Rodriguez J, Wodak SJ. Relations between protein sequence and structure and their significance. J Mol Biol 1990; 213:337-350.
    • (1990) J Mol Biol , vol.213 , pp. 337-350
    • Rooman, M.J.1    Rodriguez, J.2    Wodak, S.J.3
  • 23
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S, Thornton JM. Principles of protein-protein interactions. Proc Natl Acad Sci USA 1996;93:13-20.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 24
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L, Chothia C, Janin J. The atomic structure of protein-protein recognition sites. J Mol Biol 1999;285:2177-2198.
    • (1999) J Mol Biol , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 25
    • 0034656949 scopus 로고    scopus 로고
    • Side-chain flexibility in proteins upon ligand binding
    • Najmanovich R, Kuttner J, Sobolev V, Edelman M. Side-chain flexibility in proteins upon ligand binding. Proteins 2000;39: 261-268.
    • (2000) Proteins , vol.39 , pp. 261-268
    • Najmanovich, R.1    Kuttner, J.2    Sobolev, V.3    Edelman, M.4
  • 26
    • 0032897494 scopus 로고    scopus 로고
    • An analysis of conformational changes on protein-protein association: Implications for predictive docking
    • Betts MJ, Sternberg MJ. An analysis of conformational changes on protein-protein association: implications for predictive docking. Protein Eng 1999;12:271-283.
    • (1999) Protein Eng , vol.12 , pp. 271-283
    • Betts, M.J.1    Sternberg, M.J.2
  • 27
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein M, Lesk AM, Chothia C. Structural mechanisms for domain movements in proteins. Biochemistry 1994;33:6739-6749.
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 28
    • 0028826992 scopus 로고
    • Automatic analysis of protein conformational changes by multiple linkage clustering
    • Boutonnet NS, Rooman MJ, Wodak SJ. Automatic analysis of protein conformational changes by multiple linkage clustering. J Mol Biol 1995;253:633-647.
    • (1995) J Mol Biol , vol.253 , pp. 633-647
    • Boutonnet, N.S.1    Rooman, M.J.2    Wodak, S.J.3
  • 29
    • 0032530836 scopus 로고    scopus 로고
    • A database of macromolecular motions
    • Gerstein M, Krebs W. A database of macromolecular motions. Nucleic Acids Res 1998;26:4280-1290.
    • (1998) Nucleic Acids Res , vol.26 , pp. 4280-1290
    • Gerstein, M.1    Krebs, W.2
  • 30
    • 1042275603 scopus 로고    scopus 로고
    • Exploring the range of protein flexibility, from a structural proteomics perspective
    • Gerstein M, Echols N. Exploring the range of protein flexibility, from a structural proteomics perspective. Curr Opin Chem Biol 2004;8:14-19.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 14-19
    • Gerstein, M.1    Echols, N.2
  • 32
    • 0037246863 scopus 로고    scopus 로고
    • MolMovDB: Analysis and visualization of conformational change and structural flexibility
    • Echols N, Milburn D, Gerstein M. MolMovDB: analysis and visualization of conformational change and structural flexibility. Nucleic Acids Res 2003;31:478-482.
    • (2003) Nucleic Acids Res , vol.31 , pp. 478-482
    • Echols, N.1    Milburn, D.2    Gerstein, M.3
  • 33
    • 33644873452 scopus 로고    scopus 로고
    • Flores S, Echols N, Milburn D, Hespenheide B, Keating K, Lu J, Wells S, Yu EZ, Thorpe M, Gerstein M. The database of macromolecular motions: new features added at the decade mark. Nucleic Acids Res 2006;34(Database issue):D296-D301.
    • Flores S, Echols N, Milburn D, Hespenheide B, Keating K, Lu J, Wells S, Yu EZ, Thorpe M, Gerstein M. The database of macromolecular motions: new features added at the decade mark. Nucleic Acids Res 2006;34(Database issue):D296-D301.
  • 34
    • 22444436454 scopus 로고    scopus 로고
    • The limit of accuracy of protein modeling: Influence of crystal packing on protein structure
    • Eyal E, Gerzon S, Potapov V, Edelman M, Sobolev V. The limit of accuracy of protein modeling: influence of crystal packing on protein structure. J Mol Biol 2005;351:431-442.
    • (2005) J Mol Biol , vol.351 , pp. 431-442
    • Eyal, E.1    Gerzon, S.2    Potapov, V.3    Edelman, M.4    Sobolev, V.5
  • 35
    • 33947426886 scopus 로고    scopus 로고
    • Delano WL. The PyMOL Molecular Graphics System (www. pymol.org). 2002.
    • (2002)
    • Delano, W.L.1
  • 36
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic ras proteins
    • Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH. Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. Science 1990;247:939-945.
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Tong, L.2    deVos, A.M.3    Brunger, A.4    Yamaizumi, Z.5    Nishimura, S.6    Kim, S.H.7
  • 37
    • 0029107760 scopus 로고
    • The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue
    • Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A. The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature 1995;375:554-560.
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Scherer, A.4    McCormick, F.5    Wittinghofer, A.6
  • 38
    • 0028810684 scopus 로고
    • Mechanism of corepressor-mediated specific DNA binding by the purine repressor
    • Schumacher MA, Choi KY, Lu F, Zalkin H, Brennan RG. Mechanism of corepressor-mediated specific DNA binding by the purine repressor. Cell 1995;83:147-155.
    • (1995) Cell , vol.83 , pp. 147-155
    • Schumacher, M.A.1    Choi, K.Y.2    Lu, F.3    Zalkin, H.4    Brennan, R.G.5
  • 39
    • 0025189804 scopus 로고
    • Structural basis of the allosteric behaviour of phosphofructokinase
    • Schirmer T, Evans PR. Structural basis of the allosteric behaviour of phosphofructokinase. Nature 1990;343:140-145.
    • (1990) Nature , vol.343 , pp. 140-145
    • Schirmer, T.1    Evans, P.R.2
  • 40
    • 0028209049 scopus 로고
    • Crystal structure of recombinant chicken triosephosphate isomerase- phosphoglycolohydroxamate complex at 1.8-Å resolution
    • Zhang Z, Sugio S, Komives EA, Liu KD, Knowles JR, Petsko GA, Ringe D. Crystal structure of recombinant chicken triosephosphate isomerase- phosphoglycolohydroxamate complex at 1.8-Å resolution. Biochemistry 1994;33:2830-2837.
    • (1994) Biochemistry , vol.33 , pp. 2830-2837
    • Zhang, Z.1    Sugio, S.2    Komives, E.A.3    Liu, K.D.4    Knowles, J.R.5    Petsko, G.A.6    Ringe, D.7
  • 41
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983;22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 42
    • 33947429409 scopus 로고    scopus 로고
    • Hubbard SJ, Thornton JM. NACCESS. London: Department of Biochemistry and Molecular Biology, University College; 1993.
    • Hubbard SJ, Thornton JM. NACCESS. London: Department of Biochemistry and Molecular Biology, University College; 1993.
  • 43
    • 0021658956 scopus 로고
    • Allostery without conformational change. A plausible model
    • Cooper A, Dryden DT. Allostery without conformational change. A plausible model. Eur Biophys J 1984;11:103-109.
    • (1984) Eur Biophys J , vol.11 , pp. 103-109
    • Cooper, A.1    Dryden, D.T.2
  • 44
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    • Bahar I, Atilgan AR, Erman B. Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential. Fold Des 1997;2:173-181.
    • (1997) Fold Des , vol.2 , pp. 173-181
    • Bahar, I.1    Atilgan, A.R.2    Erman, B.3
  • 46
    • 0035427398 scopus 로고    scopus 로고
    • Protein flexibility predictions using graph theory
    • Jacobs DJ, Rader AJ, Kuhn LA, Thorpe MF. Protein flexibility predictions using graph theory. Proteins 2001;44:150-165.
    • (2001) Proteins , vol.44 , pp. 150-165
    • Jacobs, D.J.1    Rader, A.J.2    Kuhn, L.A.3    Thorpe, M.F.4
  • 47
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland DE. Application of a theory of enzyme specificity to protein synthesis. Proc Natl Acad Sci USA 1958;44:98-104.
    • (1958) Proc Natl Acad Sci USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 48
    • 0035859857 scopus 로고    scopus 로고
    • Propagating conformational changes over long (and short) distances in proteins
    • Yu EW, Koshland DE, Jr. Propagating conformational changes over long (and short) distances in proteins. Proc Natl Acad Sci USA 2001;98:9517-9520.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9517-9520
    • Yu, E.W.1    Koshland Jr., D.E.2
  • 49
    • 33646776723 scopus 로고    scopus 로고
    • Reconciling the "old" and "new" views of protein allostery: A molecular simulation study of chemotaxis Y protein (CheY)
    • Formaneck MS, Ma L, Cui Q. Reconciling the "old" and "new" views of protein allostery: a molecular simulation study of chemotaxis Y protein (CheY). Proteins 2006;63:846-867.
    • (2006) Proteins , vol.63 , pp. 846-867
    • Formaneck, M.S.1    Ma, L.2    Cui, Q.3
  • 50
    • 0030729453 scopus 로고    scopus 로고
    • Efficient characterization of collective motions and interresidue correlations in proteins by low-resolution simulations
    • Bahar I, Erman B, Haliloglu T, Jernigan RL. Efficient characterization of collective motions and interresidue correlations in proteins by low-resolution simulations. Biochemistry 1997;36:13512-13523.
    • (1997) Biochemistry , vol.36 , pp. 13512-13523
    • Bahar, I.1    Erman, B.2    Haliloglu, T.3    Jernigan, R.L.4
  • 51
    • 0030580089 scopus 로고    scopus 로고
    • Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors
    • Hilser VJ, Freire E. Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. J Mol Biol 1996;262:756-772.
    • (1996) J Mol Biol , vol.262 , pp. 756-772
    • Hilser, V.J.1    Freire, E.2
  • 52
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel GM, Lockless SW, Wall MA, Ranganathan R. Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nat Struct Biol 2003;10:59-69.
    • (2003) Nat Struct Biol , vol.10 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 54
    • 22444450449 scopus 로고    scopus 로고
    • Intramolecular signaling pathways revealed by modeling anisotropic thermal diffusion
    • Ota N, Agard DA. Intramolecular signaling pathways revealed by modeling anisotropic thermal diffusion. J Mol Biol 2005;351:345-354.
    • (2005) J Mol Biol , vol.351 , pp. 345-354
    • Ota, N.1    Agard, D.A.2
  • 55
    • 0030310317 scopus 로고    scopus 로고
    • Assessing the performance of fold recognition methods by means of a comprehensive benchmark
    • Fischer D, Elofsson A, Rice D, Eisenberg D. Assessing the performance of fold recognition methods by means of a comprehensive benchmark. Pac Symp Biocomput 1996:300-318.
    • (1996) Pac Symp Biocomput , pp. 300-318
    • Fischer, D.1    Elofsson, A.2    Rice, D.3    Eisenberg, D.4
  • 58
    • 0038687151 scopus 로고    scopus 로고
    • Identification of substrate contact residues important for the allosteric regulation of phosphofructokinase from Eschericia coli
    • Fenton AW, Paricharttanakul NM, Reinhart GD. Identification of substrate contact residues important for the allosteric regulation of phosphofructokinase from Eschericia coli. Biochemistry 2003;42:6453-6459.
    • (2003) Biochemistry , vol.42 , pp. 6453-6459
    • Fenton, A.W.1    Paricharttanakul, N.M.2    Reinhart, G.D.3
  • 60
    • 0038161052 scopus 로고    scopus 로고
    • Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations
    • Gray JJ, Moughon S, Wang C, Schueler-Furman O, Kuhlman B, Rohl CA, Baker D. Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations. J Mol Biol 2003;331:281-299.
    • (2003) J Mol Biol , vol.331 , pp. 281-299
    • Gray, J.J.1    Moughon, S.2    Wang, C.3    Schueler-Furman, O.4    Kuhlman, B.5    Rohl, C.A.6    Baker, D.7
  • 61
    • 33645792604 scopus 로고    scopus 로고
    • Physically realistic homology models built with ROSETTA can be more accurate than their templates
    • Misura KM, Chivian D, Rohl CA, Kim DE, Baker D. Physically realistic homology models built with ROSETTA can be more accurate than their templates. Proc Natl Acad Sci USA 2006; 103:5361-5366.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 5361-5366
    • Misura, K.M.1    Chivian, D.2    Rohl, C.A.3    Kim, D.E.4    Baker, D.5
  • 62
    • 24944493938 scopus 로고    scopus 로고
    • Toward high-resolution de novo structure prediction for small proteins
    • Bradley P, Misura KM, Baker D. Toward high-resolution de novo structure prediction for small proteins. Science 2005;309:1868-1871.
    • (2005) Science , vol.309 , pp. 1868-1871
    • Bradley, P.1    Misura, K.M.2    Baker, D.3
  • 65
    • 0030883755 scopus 로고    scopus 로고
    • Protein domain movements: Detection of rigid domains and visualization of hinges in comparisons of atomic coordinates
    • Wriggers W, Schulten K. Protein domain movements: detection of rigid domains and visualization of hinges in comparisons of atomic coordinates. Proteins 1997;29:1-14.
    • (1997) Proteins , vol.29 , pp. 1-14
    • Wriggers, W.1    Schulten, K.2
  • 66
    • 33744807436 scopus 로고    scopus 로고
    • Gaussian-weighted RMSD superposition of proteins: A structural comparison for flexible proteins and predicted protein structures
    • Damm KL, Carlson HA. Gaussian-weighted RMSD superposition of proteins: a structural comparison for flexible proteins and predicted protein structures. Biophys J 2006;90(12):4558-4573.
    • (2006) Biophys J , vol.90 , Issue.12 , pp. 4558-4573
    • Damm, K.L.1    Carlson, H.A.2
  • 67
    • 0035874146 scopus 로고    scopus 로고
    • Analysis of a data set of paired uncomplexed protein structures: New metrics for side-chain flexibility and model evaluation
    • Zhao S, Goodsell DS, Olson AJ. Analysis of a data set of paired uncomplexed protein structures: new metrics for side-chain flexibility and model evaluation. Proteins 2001;43:271-279.
    • (2001) Proteins , vol.43 , pp. 271-279
    • Zhao, S.1    Goodsell, D.S.2    Olson, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.