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Volumn 61, Issue 1, 2005, Pages 115-126

Protein flexibility and rigidity predicted from sequence

Author keywords

Conformational switch; Enzyme active sites; Flexibility prediction; Multiple alignments; Protein dynamics; Protein function prediction; Protein motion; Protein structure prediction; Secondary structure prediction; Solvent accessibility

Indexed keywords

PROTEIN; SOLVENT;

EID: 24344503079     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20587     Document Type: Article
Times cited : (163)

References (89)
  • 1
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity-linking function and disorder
    • Dunker AK, Obradovic Z. The protein trinity-linking function and disorder. Nat Biotechnol 2001;19:805-806.
    • (2001) Nat Biotechnol , vol.19 , pp. 805-806
    • Dunker, A.K.1    Obradovic, Z.2
  • 2
    • 0036968309 scopus 로고    scopus 로고
    • Loopy proteins appear conserved in evolution
    • Liu J, Tan H, Rost B. Loopy proteins appear conserved in evolution. J Mol Biol 2002;322:53-64.
    • (2002) J Mol Biol , vol.322 , pp. 53-64
    • Liu, J.1    Tan, H.2    Rost, B.3
  • 4
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm
    • Wright PE, Dyson HJ. Intrinsically unstructured proteins: reassessing the protein structure-function paradigm. J Mol Biol 1999;293:321-331.
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 5
    • 0037316987 scopus 로고    scopus 로고
    • Flexibility analysis of enzyme active sites by crystallographic temperature factors
    • Yuan Z, Zhao J, Wang ZX. Flexibility analysis of enzyme active sites by crystallographic temperature factors. Protein Eng 2003;16: 109-114.
    • (2003) Protein Eng , vol.16 , pp. 109-114
    • Yuan, Z.1    Zhao, J.2    Wang, Z.X.3
  • 6
    • 0043123344 scopus 로고    scopus 로고
    • GTPase catalysis by Ras and other G-proteins: Insights from substrate directed superimposition
    • Kosloff M, Selinger Z. GTPase catalysis by Ras and other G-proteins: insights from substrate directed superimposition. J Mol Biol 2003;331:1157-1170.
    • (2003) J Mol Biol , vol.331 , pp. 1157-1170
    • Kosloff, M.1    Selinger, Z.2
  • 7
    • 0031571127 scopus 로고    scopus 로고
    • Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin
    • Carr PA, Erickson HP, Palmer AG III. Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin. Structure 1997;5:949-959.
    • (1997) Structure , vol.5 , pp. 949-959
    • Carr, P.A.1    Erickson, H.P.2    Palmer III, A.G.3
  • 8
    • 0031984752 scopus 로고    scopus 로고
    • Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain
    • Akke M, Liu J, Cavanagh J, Erickson HP, Palmer AG III. Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain. Nat Struct Biol 1998;5:55-59.
    • (1998) Nat Struct Biol , vol.5 , pp. 55-59
    • Akke, M.1    Liu, J.2    Cavanagh, J.3    Erickson, H.P.4    Palmer III, A.G.5
  • 9
    • 0037666888 scopus 로고    scopus 로고
    • Implications of protein flexibility for drug discovery
    • Teague SJ. Implications of protein flexibility for drug discovery. Nat Rev Drug Discov 2003;2:527-541.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 527-541
    • Teague, S.J.1
  • 12
    • 0036402827 scopus 로고    scopus 로고
    • Identification and functions of usefully disordered proteins
    • Dunker AK, Brown CJ, Obradovic Z. Identification and functions of usefully disordered proteins. Adv Protein Chem 2002;62:25-49.
    • (2002) Adv Protein Chem , vol.62 , pp. 25-49
    • Dunker, A.K.1    Brown, C.J.2    Obradovic, Z.3
  • 14
    • 0035096292 scopus 로고    scopus 로고
    • Recognition between flexible protein molecules: Induced and assisted folding
    • Demchenko AP. Recognition between flexible protein molecules: induced and assisted folding. J Mol Recognit 2001;14:42-61.
    • (2001) J Mol Recognit , vol.14 , pp. 42-61
    • Demchenko, A.P.1
  • 15
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P. Intrinsically unstructured proteins. Trends Biochem Sci 2002;27:527-533.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 16
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky VN. What does it mean to be natively unfolded? Eur J Biochem 2002;269:2-12.
    • (2002) Eur J Biochem , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 17
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky VN. Natively unfolded proteins: a point where biology waits for physics. Protein Sci 2002;11:739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 18
    • 0141861067 scopus 로고    scopus 로고
    • Protein folding revisited: A polypeptide chain at the folding-misfolding-nonfolding cross-roads: Which way to go?
    • Uversky VN. Protein folding revisited: a polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go? Cell Mol Life Sci 2003;60:1852-1871.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1852-1871
    • Uversky, V.N.1
  • 19
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson HJ, Wright PE. Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol 2002;12:54-60.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 20
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 2005;6:197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 21
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded protons and protein folding studied by NMR
    • Dyson HJ, Wright PE. Unfolded protons and protein folding studied by NMR. Chem Rev 2004;104:3607-3622.
    • (2004) Chem Rev , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 22
    • 0036174712 scopus 로고    scopus 로고
    • Continuum secondary structure captures protein flexibility
    • Andersen CAF, Palmer AG, Brunak S, Rost B. Continuum secondary structure captures protein flexibility. Structure 2002;10:175-185.
    • (2002) Structure , vol.10 , pp. 175-185
    • Andersen, C.A.F.1    Palmer, A.G.2    Brunak, S.3    Rost, B.4
  • 23
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky VN, Gillespie JR, Fink AL. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 2000;41:415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 24
    • 0032726594 scopus 로고    scopus 로고
    • Folding minimal sequences: The lower bound for sequence complexity of globular proteins
    • Romero P, Obradovic Z, Dunker AK. Folding minimal sequences: the lower bound for sequence complexity of globular proteins. FEBS Lett 1999;462:363-367.
    • (1999) FEBS Lett , vol.462 , pp. 363-367
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 26
    • 0242362157 scopus 로고    scopus 로고
    • Prediction of disordered regions in proteins from position specific score matrices
    • Jones DT, Ward JJ. Prediction of disordered regions in proteins from position specific score matrices. Proteins 2003;53(Suppl 6):573-578.
    • (2003) Proteins , vol.53 , Issue.SUPPL. 6 , pp. 573-578
    • Jones, D.T.1    Ward, J.J.2
  • 27
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 2004;337:635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 29
    • 0041620131 scopus 로고    scopus 로고
    • NORSp: Predictions of long regions without regular secondary structure
    • Liu J, Rost B. NORSp: predictions of long regions without regular secondary structure. Nucleic Acids Res 2003;31:3833-3835.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3833-3835
    • Liu, J.1    Rost, B.2
  • 35
    • 0028361031 scopus 로고
    • Accuracy of protein flexibility predictions
    • Vihinen M, Torkkila E, Riikonen P. Accuracy of protein flexibility predictions. Proteins 1994;19:141-149.
    • (1994) Proteins , vol.19 , pp. 141-149
    • Vihinen, M.1    Torkkila, E.2    Riikonen, P.3
  • 36
    • 0021918946 scopus 로고
    • Prediction of chain flexibility of peptide antigens
    • Karplus PA, Schultz GE. Prediction of chain flexibility of peptide antigens. Naturwissenchaften 1985;72:212-213.
    • (1985) Naturwissenchaften , vol.72 , pp. 212-213
    • Karplus, P.A.1    Schultz, G.E.2
  • 37
    • 0002518563 scopus 로고    scopus 로고
    • Knowledge-based B-factor restraints for the refinement of proteins
    • Tronrud DE. Knowledge-based B-factor restraints for the refinement of proteins. J Appl Crystallogr 1996;29:100-104.
    • (1996) J Appl Crystallogr , vol.29 , pp. 100-104
    • Tronrud, D.E.1
  • 38
  • 39
    • 0030853145 scopus 로고    scopus 로고
    • Correlation between side chain mobility and conformation in protein structures
    • Carugo O, Argos P. Correlation between side chain mobility and conformation in protein structures. Protein Eng 1997;10:777-787.
    • (1997) Protein Eng , vol.10 , pp. 777-787
    • Carugo, O.1    Argos, P.2
  • 42
    • 0037022347 scopus 로고    scopus 로고
    • Flexibility and packing in proteins
    • Halle B. Flexibility and packing in proteins. Proc Natl Acad Sci USA 2002;99:1274-1279.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1274-1279
    • Halle, B.1
  • 43
    • 13944277320 scopus 로고    scopus 로고
    • Prediction of protein B-factor profiles
    • Yuan Z, Bailey TL, Teasdale RD. Prediction of protein B-factor profiles. Proteins 2005;58:905-912.
    • (2005) Proteins , vol.58 , pp. 905-912
    • Yuan, Z.1    Bailey, T.L.2    Teasdale, R.D.3
  • 44
    • 0032962457 scopus 로고    scopus 로고
    • Twilight zone of protein sequence alignments
    • Rost B. Twilight zone of protein sequence alignments. Protein Eng 1999;12:85-94.
    • (1999) Protein Eng , vol.12 , pp. 85-94
    • Rost, B.1
  • 45
    • 0043122933 scopus 로고    scopus 로고
    • UniqueProt: Creating representative protein sequence sets
    • Mika S, Rost B. UniqueProt: creating representative protein sequence sets. Nucleic Acids Res 2003;31:3789-3791.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3789-3791
    • Mika, S.1    Rost, B.2
  • 46
    • 0026030641 scopus 로고
    • Database of homology-derived structures and the structural meaning of sequence alignment
    • Sander C, Schneider R. Database of homology-derived structures and the structural meaning of sequence alignment. Proteins 1991;9:56-68.
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 48
    • 0036467068 scopus 로고    scopus 로고
    • Alignments grow, secondary structure prediction improves
    • Przybylski D, Rost B. Alignments grow, secondary structure prediction improves. Proteins 2002;46:195-205.
    • (2002) Proteins , vol.46 , pp. 195-205
    • Przybylski, D.1    Rost, B.2
  • 51
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • Palmer AG III, Kroenke CD, Loria JP. Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol 2001;339: 204-238.
    • (2001) Methods Enzymol , vol.339 , pp. 204-238
    • Palmer III, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 52
    • 4243155782 scopus 로고    scopus 로고
    • NMR characterization of the dynamics of biomacromolecules
    • Palmer AG III. NMR characterization of the dynamics of biomacromolecules. Chem Rev 2004;104:3623-3640.
    • (2004) Chem Rev , vol.104 , pp. 3623-3640
    • Palmer III, A.G.1
  • 53
    • 0034984208 scopus 로고    scopus 로고
    • NMR probes of molecular dynamics: Overview and comparison with other techniques
    • Palmer AG III. NMR probes of molecular dynamics: overview and comparison with other techniques. Annu Rev Biophys Biomol Struct 2001;30:129-155.
    • (2001) Annu Rev Biophys Biomol Struct , vol.30 , pp. 129-155
    • Palmer III, A.G.1
  • 54
    • 0033520723 scopus 로고    scopus 로고
    • Variability of the 15N chemical shift anisotropy in Escherichia coli ribonuclease H in solution
    • Kroenke CD, Rance M, Palmer AG III. Variability of the 15N chemical shift anisotropy in Escherichia coli ribonuclease H in solution. J Am Chem Soc 1999;121:10119-10125.
    • (1999) J Am Chem Soc , vol.121 , pp. 10119-10125
    • Kroenke, C.D.1    Rance, M.2    Palmer III, A.G.3
  • 55
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile based neural networks
    • Rost B. PHD: predicting one-dimensional protein structure by profile based neural networks. Meth Enzymol 1996;266:525-539.
    • (1996) Meth Enzymol , vol.266 , pp. 525-539
    • Rost, B.1
  • 56
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost B, Sander C. Prediction of protein secondary structure at better than 70% accuracy. J Mol Biol 1993;232:584-599.
    • (1993) J Mol Biol , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 57
    • 0028109886 scopus 로고
    • Conservation and prediction of solvent accessibility in protein families
    • Rost B. Conservation and prediction of solvent accessibility in protein families. Proteins 1994;20:216-226.
    • (1994) Proteins , vol.20 , pp. 216-226
    • Rost, B.1
  • 58
    • 0038356582 scopus 로고    scopus 로고
    • Predicted protein-protein interaction sites from local sequence information
    • Ofran Y, Rost B. Predicted protein-protein interaction sites from local sequence information. FEBS Lett 2003;544:236-239.
    • (2003) FEBS Lett , vol.544 , pp. 236-239
    • Ofran, Y.1    Rost, B.2
  • 59
    • 0344118117 scopus 로고    scopus 로고
    • Better prediction of sub-cellular localization through evolution and structure
    • Nair R, Rost B. Better prediction of sub-cellular localization through evolution and structure. Proteins 2003;53:917-930.
    • (2003) Proteins , vol.53 , pp. 917-930
    • Nair, R.1    Rost, B.2
  • 60
    • 16244363308 scopus 로고    scopus 로고
    • How to use protein 1D structure predicted by PROFphd
    • Walker JE, editor. Totowa, NJ: Humana
    • Rost B. How to use protein 1D structure predicted by PROFphd. In: Walker JE, editor. The proteomics protocols handbook: methods in molecular biology. Totowa, NJ: Humana; 2005. p 875-901.
    • (2005) The Proteomics Protocols Handbook: Methods in Molecular Biology , pp. 875-901
    • Rost, B.1
  • 61
    • 0035782925 scopus 로고    scopus 로고
    • Protein secondary structure prediction continues to rise
    • Rost B. Protein secondary structure prediction continues to rise. J Struct Biol 2001;134:204-218.
    • (2001) J Struct Biol , vol.134 , pp. 204-218
    • Rost, B.1
  • 62
    • 0033957834 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000
    • Bairoch A, Apweiler R. The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000. Nucleic Acids Res 2000;28:45-48.
    • (2000) Nucleic Acids Res , vol.28 , pp. 45-48
    • Bairoch, A.1    Apweiler, R.2
  • 63
    • 0037229456 scopus 로고    scopus 로고
    • Analysing six types of protein-protein interfaces
    • Ofran Y, Rost B. Analysing six types of protein-protein interfaces. J Mol Biol 2003;325:377-387.
    • (2003) J Mol Biol , vol.325 , pp. 377-387
    • Ofran, Y.1    Rost, B.2
  • 66
    • 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;12:2577-2637.
    • (1983) Biopolymers , vol.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 68
    • 0032080521 scopus 로고    scopus 로고
    • Accessibility to internal cavities and ligand binding sites monitored by protein crystallographic thermal factors
    • Carugo O, Argos P. Accessibility to internal cavities and ligand binding sites monitored by protein crystallographic thermal factors. Proteins 1998;31:201-213.
    • (1998) Proteins , vol.31 , pp. 201-213
    • Carugo, O.1    Argos, P.2
  • 70
    • 0033769529 scopus 로고    scopus 로고
    • Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI
    • Goedken ER, Keck JL, Berger JM, Marqusee S. Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI. Protein Sci 2000;9:1914-1921.
    • (2000) Protein Sci , vol.9 , pp. 1914-1921
    • Goedken, E.R.1    Keck, J.L.2    Berger, J.M.3    Marqusee, S.4
  • 71
    • 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
  • 72
    • 0031283407 scopus 로고    scopus 로고
    • G proteins, effectors and GAPs: Structure and mechanism
    • Sprang SR. G proteins, effectors and GAPs: structure and mechanism. Curr Opin Struct Biol 1997;7:849-856.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 849-856
    • Sprang, S.R.1
  • 73
    • 0033522446 scopus 로고    scopus 로고
    • Tachylectin-2: Crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus
    • Beisel HG, Kawabata S, Iwanaga S, Huber R, Bode W. Tachylectin-2: crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus. EMBO J 1999;18:2313-2322.
    • (1999) EMBO J , vol.18 , pp. 2313-2322
    • Beisel, H.G.1    Kawabata, S.2    Iwanaga, S.3    Huber, R.4    Bode, W.5
  • 76
    • 0029156702 scopus 로고
    • Molecular dynamics simulation of the solution structures of Ha-ras-p21 GDP and GTP complexes: Flexibility, possible hinges, and levers of the conformational transition
    • Diaz JF, Wroblowski B, Engelborghs Y. Molecular dynamics simulation of the solution structures of Ha-ras-p21 GDP and GTP complexes: flexibility, possible hinges, and levers of the conformational transition. Biochemistry 1995;34:12038-12047.
    • (1995) Biochemistry , vol.34 , pp. 12038-12047
    • Diaz, J.F.1    Wroblowski, B.2    Engelborghs, Y.3
  • 77
    • 0030700726 scopus 로고    scopus 로고
    • Ligand-induced conformational changes in ras p21: A normal mode and energy minimization analysis
    • Ma J, Karplus M. Ligand-induced conformational changes in ras p21: a normal mode and energy minimization analysis. J Mol Biol 1997;274:114-131.
    • (1997) J Mol Biol , vol.274 , pp. 114-131
    • Ma, J.1    Karplus, M.2
  • 79
    • 0034480099 scopus 로고    scopus 로고
    • Structural changes induced in p21Ras upon GAP-334 complexation as probed by ESEEM spectroscopy and molecular-dynamics simulation
    • Farrar CT, Ma J, Singel DJ, Halkides CJ. Structural changes induced in p21Ras upon GAP-334 complexation as probed by ESEEM spectroscopy and molecular-dynamics simulation. Structure 2000;8:1279-1287.
    • (2000) Structure , vol.8 , pp. 1279-1287
    • Farrar, C.T.1    Ma, J.2    Singel, D.J.3    Halkides, C.J.4
  • 80
    • 0027297116 scopus 로고
    • Mechanism of GTP hydrolysis by p21N-ras catalyzed by GAP: Studies with a fluorescent GTP analogue
    • Moore KJ, Webb MR, Eccleston JF. Mechanism of GTP hydrolysis by p21N-ras catalyzed by GAP: studies with a fluorescent GTP analogue. Biochemistry 1993;32:7451-7459.
    • (1993) Biochemistry , vol.32 , pp. 7451-7459
    • Moore, K.J.1    Webb, M.R.2    Eccleston, J.F.3
  • 81
    • 0031013031 scopus 로고    scopus 로고
    • Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain
    • Springer TA. Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain. Proc Natl Acad Sci USA 1997;94:65-72.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 65-72
    • Springer, T.A.1
  • 82
    • 0242558716 scopus 로고    scopus 로고
    • Beta propellers: Structural rigidity and functional diversity
    • Fulop V, Jones, D.T. Beta propellers: structural rigidity and functional diversity. Curr Opin Struct Biol 1999;9:715-721.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 715-721
    • Fulop, V.1    Jones, D.T.2
  • 84
    • 0036776124 scopus 로고    scopus 로고
    • Sequence and structural differences between enzyme and nonenzyme homologs
    • Todd AE, Orengo CA, Thornton JM. Sequence and structural differences between enzyme and nonenzyme homologs. Structure 2002;10:1435-1451.
    • (2002) Structure , vol.10 , pp. 1435-1451
    • Todd, A.E.1    Orengo, C.A.2    Thornton, J.M.3
  • 85
    • 0024046461 scopus 로고
    • Analysis and prediction of the location of catalytic residues in enzymes
    • Zvelebil MJ, Sternberg MJ. Analysis and prediction of the location of catalytic residues in enzymes. Protein Eng 1988;2:127-138.
    • (1988) Protein Eng , vol.2 , pp. 127-138
    • Zvelebil, M.J.1    Sternberg, M.J.2
  • 87
    • 0032749098 scopus 로고    scopus 로고
    • Structure-based analysis of protein dynamics: Comparison of theoretical results for hen lysozyme with X-ray diffraction and NMR relaxation data
    • Haliloglu T, Bahar I. Structure-based analysis of protein dynamics: comparison of theoretical results for hen lysozyme with X-ray diffraction and NMR relaxation data. Proteins 1999;37:654-667.
    • (1999) Proteins , vol.37 , pp. 654-667
    • Haliloglu, T.1    Bahar, I.2
  • 88
    • 4344592803 scopus 로고    scopus 로고
    • Dynamics of ATP-binding cassette contribute to allosteric control, nucleotide binding and energy transduction in ABC transporters
    • Wang C, Karpowich N, Hunt JF, Rance M, Palmer AG. Dynamics of ATP-binding cassette contribute to allosteric control, nucleotide binding and energy transduction in ABC transporters. J Mol Biol 2004;342:525-537.
    • (2004) J Mol Biol , vol.342 , pp. 525-537
    • Wang, C.1    Karpowich, N.2    Hunt, J.F.3    Rance, M.4    Palmer, A.G.5
  • 89
    • 0035131438 scopus 로고    scopus 로고
    • Roles of partly unfolded conformations in macromolecular self-assembly
    • Namba K. Roles of partly unfolded conformations in macromolecular self-assembly. Genes Cells 2001;6:1-12.
    • (2001) Genes Cells , vol.6 , pp. 1-12
    • Namba, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.