메뉴 건너뛰기




Volumn 8, Issue , 2008, Pages

Fast dynamics perturbation analysis for prediction of protein functional sites

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 41449115497     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-8-5     Document Type: Article
Times cited : (33)

References (67)
  • 1
    • 26944480402 scopus 로고    scopus 로고
    • Beyond annotation transfer by homology: Novel protein-function prediction methods to assist drug discovery
    • 16243268
    • Beyond annotation transfer by homology: novel protein-function prediction methods to assist drug discovery. Y Ofran M Punta R Schneider B Rost, Drug Discov Today 2005 10 21 1475 1482 16243268
    • (2005) Drug Discov Today , vol.10 , Issue.21 , pp. 1475-1482
    • Ofran, Y.1    Punta, M.2    Schneider, R.3    Rost, B.4
  • 3
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • 16844972
    • CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. J Dundas Z Ouyang J Tseng A Binkowski Y Turpaz J Liang, Nucleic Acids Res 2006 34 Web Server issue W116 8 16844972
    • (2006) Nucleic Acids Res , vol.34 , Issue.WEB SERVER ISSUE , pp. 116-8
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 4
    • 0031370977 scopus 로고    scopus 로고
    • LIGSITE: Automatic and efficient detection of potential small molecule-binding sites in proteins
    • 9704298
    • LIGSITE: automatic and efficient detection of potential small molecule-binding sites in proteins. M Hendlich F Rippmann G Barnickel, J Mol Graph Model 1997 15 6 359 63, 389 9704298
    • (1997) J Mol Graph Model , vol.15 , Issue.6 , pp. 359-63
    • Hendlich, M.1    Rippmann, F.2    Barnickel, G.3
  • 6
    • 0028881975 scopus 로고
    • SURFNET: A program for visualizing molecular surfaces, cavities, and intermolecular interactions
    • 8603061
    • SURFNET: a program for visualizing molecular surfaces, cavities, and intermolecular interactions. RA Laskowski, J Mol Graph 1995 13 5 323 30, 307-8 8603061
    • (1995) J Mol Graph , vol.13 , Issue.5 , pp. 323-30
    • Laskowski, R.A.1
  • 7
    • 28644438570 scopus 로고    scopus 로고
    • An intuitive approach to measuring protein surface curvature
    • 16235263
    • An intuitive approach to measuring protein surface curvature. RG Coleman MA Burr DL Souvaine AC Cheng, Proteins 2005 61 4 1068 1074 16235263
    • (2005) Proteins , vol.61 , Issue.4 , pp. 1068-1074
    • Coleman, R.G.1    Burr, M.A.2    Souvaine, D.L.3    Cheng, A.C.4
  • 8
    • 33748102999 scopus 로고    scopus 로고
    • Travel depth, a new shape descriptor for macromolecules: Application to ligand binding
    • 16934837
    • Travel depth, a new shape descriptor for macromolecules: application to ligand binding. RG Coleman KA Sharp, J Mol Biol 2006 362 3 441 458 16934837
    • (2006) J Mol Biol , vol.362 , Issue.3 , pp. 441-458
    • Coleman, R.G.1    Sharp, K.A.2
  • 9
    • 0031616116 scopus 로고    scopus 로고
    • Surface solid angle-based site points for molecular docking
    • 9697192
    • Surface solid angle-based site points for molecular docking. DK Hendrix ID Kuntz, Pac Symp Biocomput 1998 317 326 9697192
    • (1998) Pac Symp Biocomput , pp. 317-326
    • Hendrix, D.K.1    Kuntz, I.D.2
  • 10
    • 33646757492 scopus 로고    scopus 로고
    • On the nature of cavities on protein surfaces: Application to the identification of drug-binding sites
    • 16477622
    • On the nature of cavities on protein surfaces: application to the identification of drug-binding sites. M Nayal B Honig, Proteins 2006 63 4 892 906 16477622
    • (2006) Proteins , vol.63 , Issue.4 , pp. 892-906
    • Nayal, M.1    Honig, B.2
  • 11
    • 34447645811 scopus 로고    scopus 로고
    • A robust and efficient algorithm for the shape description of protein structures and its application in predicting ligand binding sites
    • 17570152
    • A robust and efficient algorithm for the shape description of protein structures and its application in predicting ligand binding sites. L Xie PE Bourne, BMC Bioinformatics 2007 8 Suppl 4 S9 17570152
    • (2007) BMC Bioinformatics , vol.84 , pp. 9
    • Xie, L.1    Bourne, P.E.2
  • 12
    • 18744394070 scopus 로고    scopus 로고
    • Q-SiteFinder: An energy-based method for the prediction of protein-ligand binding sites
    • 15701681
    • Q-SiteFinder: an energy-based method for the prediction of protein-ligand binding sites. AT Laurie RM Jackson, Bioinformatics 2005 21 9 1908 1916 15701681
    • (2005) Bioinformatics , vol.21 , Issue.9 , pp. 1908-1916
    • Laurie, A.T.1    Jackson, R.M.2
  • 13
    • 0035965145 scopus 로고    scopus 로고
    • Prediction of functionally important residues based solely on the computed energetics of protein structure
    • 11575940
    • Prediction of functionally important residues based solely on the computed energetics of protein structure. AH Elcock, J Mol Biol 2001 312 4 885 896 11575940
    • (2001) J Mol Biol , vol.312 , Issue.4 , pp. 885-896
    • Elcock, A.H.1
  • 14
    • 0035940421 scopus 로고    scopus 로고
    • THEMATICS: A simple computational predictor of enzyme function from structure
    • 11606719
    • THEMATICS: a simple computational predictor of enzyme function from structure. MJ Ondrechen JG Clifton D Ringe, Proc Natl Acad Sci U S A 2001 98 22 12473 12478 11606719
    • (2001) Proc Natl Acad Sci U S a , vol.98 , Issue.22 , pp. 12473-12478
    • Ondrechen, M.J.1    Clifton, J.G.2    Ringe, D.3
  • 15
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • 8609628
    • An evolutionary trace method defines binding surfaces common to protein families. O Lichtarge HR Bourne FE Cohen, J Mol Biol 1996 257 2 342 358 8609628
    • (1996) J Mol Biol , vol.257 , Issue.2 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 16
    • 33748267918 scopus 로고    scopus 로고
    • Rank information: A structure-independent measure of evolutionary trace quality that improves identification of protein functional sites
    • 16894615
    • Rank information: a structure-independent measure of evolutionary trace quality that improves identification of protein functional sites. H Yao I Mihalek O Lichtarge, Proteins 2006 65 1 111 123 16894615
    • (2006) Proteins , vol.65 , Issue.1 , pp. 111-123
    • Yao, H.1    Mihalek, I.2    Lichtarge, O.3
  • 17
    • 0030724039 scopus 로고    scopus 로고
    • TESS: A geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases. Application to enzyme active sites
    • 9385633
    • TESS: a geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases. Application to enzyme active sites. AC Wallace N Borkakoti JM Thornton, Protein Sci 1997 6 11 2308 2323 9385633
    • (1997) Protein Sci , vol.6 , Issue.11 , pp. 2308-2323
    • Wallace, A.C.1    Borkakoti, N.2    Thornton, J.M.3
  • 18
    • 2442614144 scopus 로고    scopus 로고
    • Recognition of functional sites in protein structures
    • 15147845
    • Recognition of functional sites in protein structures. A Shulman-Peleg R Nussinov HJ Wolfson, J Mol Biol 2004 339 3 607 633 15147845
    • (2004) J Mol Biol , vol.339 , Issue.3 , pp. 607-633
    • Shulman-Peleg, A.1    Nussinov, R.2    Wolfson, H.J.3
  • 19
    • 0041620372 scopus 로고    scopus 로고
    • Annotation in three dimensions. PINTS: Patterns in Non-homologous Tertiary Structures
    • 12824322
    • Annotation in three dimensions. PINTS: Patterns in Non-homologous Tertiary Structures. A Stark RB Russell, Nucleic Acids Res 2003 31 13 3341 3344 12824322
    • (2003) Nucleic Acids Res , vol.31 , Issue.13 , pp. 3341-3344
    • Stark, A.1    Russell, R.B.2
  • 20
    • 4143145197 scopus 로고    scopus 로고
    • Finding functional sites in structural genomics proteins
    • 15296734
    • Finding functional sites in structural genomics proteins. A Stark A Shkumatov RB Russell, Structure 2004 12 8 1405 1412 15296734
    • (2004) Structure , vol.12 , Issue.8 , pp. 1405-1412
    • Stark, A.1    Shkumatov, A.2    Russell, R.B.3
  • 21
    • 0043130640 scopus 로고    scopus 로고
    • Automated construction of structural motifs for predicting functional sites on protein structures
    • 12603029
    • Automated construction of structural motifs for predicting functional sites on protein structures. MP Liang DL Brutlag RB Altman, Pac Symp Biocomput 2003 204 215 12603029
    • (2003) Pac Symp Biocomput , pp. 204-215
    • Liang, M.P.1    Brutlag, D.L.2    Altman, R.B.3
  • 22
    • 0141850386 scopus 로고    scopus 로고
    • An algorithm for constraint-based structural template matching: Application to 3D templates with statistical analysis
    • 12967960
    • An algorithm for constraint-based structural template matching: application to 3D templates with statistical analysis. JA Barker JM Thornton, Bioinformatics 2003 19 13 1644 1649 12967960
    • (2003) Bioinformatics , vol.19 , Issue.13 , pp. 1644-1649
    • Barker, J.A.1    Thornton, J.M.2
  • 24
    • 25444527443 scopus 로고    scopus 로고
    • Improved prediction of critical residues for protein function based on network and phylogenetic analyses
    • 16124876
    • Improved prediction of critical residues for protein function based on network and phylogenetic analyses. B Thibert DE Bredesen G del Rio, BMC Bioinformatics 2005 6 213 16124876
    • (2005) BMC Bioinformatics , vol.6 , pp. 213
    • Thibert, B.1    Bredesen, D.E.2    Del Rio, G.3
  • 25
    • 34249308113 scopus 로고    scopus 로고
    • How accurate and statistically robust are catalytic site predictions based on closeness centrality?
    • 17498304
    • How accurate and statistically robust are catalytic site predictions based on closeness centrality? E Chea DR Livesay, BMC Bioinformatics 2007 8 153 17498304
    • (2007) BMC Bioinformatics , vol.8 , pp. 153
    • Chea, E.1    Livesay, D.R.2
  • 26
    • 33846662784 scopus 로고    scopus 로고
    • ISIS: Interaction sites identified from sequence
    • 17237081
    • ISIS: interaction sites identified from sequence. Y Ofran B Rost, Bioinformatics 2007 23 2 e13 6 17237081
    • (2007) Bioinformatics , vol.23 , Issue.2 , pp. 13-6
    • Ofran, Y.1    Rost, B.2
  • 27
    • 0042674397 scopus 로고    scopus 로고
    • Using a neural network and spatial clustering to predict the location of active sites in enzymes
    • 12850142
    • Using a neural network and spatial clustering to predict the location of active sites in enzymes. A Gutteridge GJ Bartlett JM Thornton, J Mol Biol 2003 330 4 719 734 12850142
    • (2003) J Mol Biol , vol.330 , Issue.4 , pp. 719-734
    • Gutteridge, A.1    Bartlett, G.J.2    Thornton, J.M.3
  • 28
    • 4444296254 scopus 로고    scopus 로고
    • Recognizing complex, asymmetric functional sites in protein structures using a Bayesian scoring function
    • 15290784
    • Recognizing complex, asymmetric functional sites in protein structures using a Bayesian scoring function. L Wei RB Altman, J Bioinform Comput Biol 2003 1 1 119 138 15290784
    • (2003) J Bioinform Comput Biol , vol.1 , Issue.1 , pp. 119-138
    • Wei, L.1    Altman, R.B.2
  • 29
    • 0035366379 scopus 로고    scopus 로고
    • Protein functional epitopes: Hot spots, dynamics and combinatorial libraries
    • 11406388
    • Protein functional epitopes: hot spots, dynamics and combinatorial libraries. B Ma HJ Wolfson R Nussinov, Curr Opin Struct Biol 2001 11 3 364 369 11406388
    • (2001) Curr Opin Struct Biol , vol.11 , Issue.3 , pp. 364-369
    • Ma, B.1    Wolfson, H.J.2    Nussinov, R.3
  • 30
    • 20444409186 scopus 로고    scopus 로고
    • Coupling between catalytic site and collective dynamics: A requirement for mechanochemical activity of enzymes
    • 15939021
    • Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymes. LW Yang I Bahar, Structure 2005 13 6 893 904 15939021
    • (2005) Structure , vol.13 , Issue.6 , pp. 893-904
    • Yang, L.W.1    Bahar, I.2
  • 31
    • 21244506296 scopus 로고    scopus 로고
    • How similar are protein folding and protein binding nuclei? Examination of vibrational motions of energy hot spots and conserved residues
    • 15596504
    • How similar are protein folding and protein binding nuclei? Examination of vibrational motions of energy hot spots and conserved residues. T Haliloglu O Keskin B Ma R Nussinov, Biophys J 2005 88 3 1552 1559 15596504
    • (2005) Biophys J , vol.88 , Issue.3 , pp. 1552-1559
    • Haliloglu, T.1    Keskin, O.2    Ma, B.3    Nussinov, R.4
  • 33
    • 34248332629 scopus 로고    scopus 로고
    • Functional residues serve a dominant role in mediating the cooperativity of the protein ensemble
    • 17360527
    • Functional residues serve a dominant role in mediating the cooperativity of the protein ensemble. T Liu ST Whitten VJ Hilser, Proc Natl Acad Sci U S A 2007 104 11 4347 4352 17360527
    • (2007) Proc Natl Acad Sci U S a , vol.104 , Issue.11 , pp. 4347-4352
    • Liu, T.1    Whitten, S.T.2    Hilser, V.J.3
  • 34
    • 33749336161 scopus 로고    scopus 로고
    • Localization of binding sites in protein structures by optimization of a composite scoring function
    • 16963645
    • Localization of binding sites in protein structures by optimization of a composite scoring function. A Rossi MA Marti-Renom A Sali, Protein Sci 2006 15 10 2366 2380 16963645
    • (2006) Protein Sci , vol.15 , Issue.10 , pp. 2366-2380
    • Rossi, A.1    Marti-Renom, M.A.2    Sali, A.3
  • 35
    • 33746950964 scopus 로고    scopus 로고
    • Prediction of catalytic residues using Support Vector Machine with selected protein sequence and structural properties
    • 16790052
    • Prediction of catalytic residues using Support Vector Machine with selected protein sequence and structural properties. NV Petrova CH Wu, BMC Bioinformatics 2006 7 312 16790052
    • (2006) BMC Bioinformatics , vol.7 , pp. 312
    • Petrova, N.V.1    Wu, C.H.2
  • 36
    • 18844409482 scopus 로고    scopus 로고
    • Quantifying allosteric effects in proteins
    • 15822100
    • Quantifying allosteric effects in proteins. D Ming ME Wall, Proteins 2005 59 4 697 707 15822100
    • (2005) Proteins , vol.59 , Issue.4 , pp. 697-707
    • Ming, D.1    Wall, M.E.2
  • 37
    • 28844456158 scopus 로고    scopus 로고
    • Allostery in a coarse-grained model of protein dynamics
    • 16384030
    • Allostery in a coarse-grained model of protein dynamics. D Ming ME Wall, Phys Rev Lett 2005 95 198103 16384030
    • (2005) Phys Rev Lett , vol.95 , pp. 198103
    • Ming, D.1    Wall, M.E.2
  • 38
    • 33645102817 scopus 로고    scopus 로고
    • Interactions in native binding sites cause a large change in protein dynamics
    • 16513135
    • Interactions in native binding sites cause a large change in protein dynamics. D Ming ME Wall, J Mol Biol 2006 358 213 223 16513135
    • (2006) J Mol Biol , vol.358 , pp. 213-223
    • Ming, D.1    Wall, M.E.2
  • 39
    • 33846234709 scopus 로고    scopus 로고
    • Ligand binding, protein fluctuations, and allosteric free energy
    • Ligand binding, protein fluctuations, and allosteric free energy. ME Wall, AIP Conf Proc 2006 851 16 33
    • (2006) AIP Conf Proc , vol.851 , pp. 16-33
    • Wall, M.E.1
  • 40
    • 0015528157 scopus 로고
    • Ligand binding and internal equilibria in proteins
    • 5059892
    • Ligand binding and internal equilibria in proteins. G Weber, Biochemistry 1972 11 5 864 878 5059892
    • (1972) Biochemistry , vol.11 , Issue.5 , pp. 864-878
    • Weber, G.1
  • 41
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • 14343300
    • On the nature of allosteric transitions: a plausible model. J Monod J Wyman JP Changeux, J Mol Biol 1965 12 88 118 14343300
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 42
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • 5938952
    • Comparison of experimental binding data and theoretical models in proteins containing subunits. DE Koshland Jr. G Nemethy D Filmer, Biochemistry 1966 5 1 365 385 5938952
    • (1966) Biochemistry , vol.5 , Issue.1 , pp. 365-385
    • Koshland Jr., D.E.1    Nemethy, G.2    Filmer, D.3
  • 43
    • 0034710950 scopus 로고    scopus 로고
    • Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble
    • 11035796
    • Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble. H Pan JC Lee VJ Hilser, Proc Natl Acad Sci U S A 2000 97 22 12020 12025 11035796
    • (2000) Proc Natl Acad Sci U S a , vol.97 , Issue.22 , pp. 12020-12025
    • Pan, H.1    Lee, J.C.2    Hilser, V.J.3
  • 44
    • 6344219895 scopus 로고    scopus 로고
    • Is allostery an intrinsic property of all dynamic proteins?
    • 15382234
    • Is allostery an intrinsic property of all dynamic proteins? K Gunasekaran B Ma R Nussinov, Proteins 2004 57 433 443 15382234
    • (2004) Proteins , vol.57 , pp. 433-443
    • Gunasekaran, K.1    Ma, B.2    Nussinov, R.3
  • 45
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
    • 17494761
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. VJ Hilser EB Thompson, Proc Natl Acad Sci U S A 2007 104 20 8311 8315 17494761
    • (2007) Proc Natl Acad Sci U S a , vol.104 , Issue.20 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 46
    • 0021796467 scopus 로고
    • Rate theories and puzzles of hemeprotein kinetics
    • 4012322
    • Rate theories and puzzles of hemeprotein kinetics. H Frauenfelder PG Wolynes, Science 1985 229 4711 337 345 4012322
    • (1985) Science , vol.229 , Issue.4711 , pp. 337-345
    • Frauenfelder, H.1    Wolynes, P.G.2
  • 49
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • 9126849
    • Development and validation of a genetic algorithm for flexible docking. G Jones P Willett RC Glen AR Leach R Taylor, J Mol Biol 1997 267 3 727 748 9126849
    • (1997) J Mol Biol , vol.267 , Issue.3 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 50
    • 0030773794 scopus 로고    scopus 로고
    • X-ray structure of turkey-egg lysozyme complex with tri-N- acetylchitotriose. Lack of binding ability at subsite a
    • 15299852
    • X-ray structure of turkey-egg lysozyme complex with tri-N- acetylchitotriose. Lack of binding ability at subsite A. K Harata M Muraki, Acta Crystallogr D Biol Crystallogr 1997 53 Pt 6 650 657 15299852
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.PART 6 , pp. 650-657
    • Harata, K.1    Muraki, M.2
  • 52
    • 0037470597 scopus 로고    scopus 로고
    • Automatic methods for predicting functionally important residues
    • 12589769
    • Automatic methods for predicting functionally important residues. A del Sol Mesa F Pazos A Valencia, J Mol Biol 2003 326 4 1289 1302 12589769
    • (2003) J Mol Biol , vol.326 , Issue.4 , pp. 1289-1302
    • Del Sol Mesa, A.1    Pazos, F.2    Valencia, A.3
  • 53
    • 37649030523 scopus 로고    scopus 로고
    • Distances and classification of amino acids for different protein secondary structures
    • Distances and classification of amino acids for different protein secondary structures. X Liu LM Zhang S Guan WM Zheng, Phys Rev E Stat Nonlin Soft Matter Phys 2003 67 5 Pt 1 51927
    • (2003) Phys Rev e Stat Nonlin Soft Matter Phys , vol.67 , Issue.5 PART 1 , pp. 51927
    • Liu, X.1    Zhang, L.M.2    Guan, S.3    Zheng, W.M.4
  • 54
    • 6344225693 scopus 로고    scopus 로고
    • The evolutionary repertoires of the eukaryotic-type ABC transporters in terms of the phylogeny of ATP-binding domains in eukaryotes and prokaryotes
    • 15297601
    • The evolutionary repertoires of the eukaryotic-type ABC transporters in terms of the phylogeny of ATP-binding domains in eukaryotes and prokaryotes. Y Igarashi KF Aoki H Mamitsuka K Kuma M Kanehisa, Mol Biol Evol 2004 21 11 2149 2160 15297601
    • (2004) Mol Biol Evol , vol.21 , Issue.11 , pp. 2149-2160
    • Igarashi, Y.1    Aoki, K.F.2    Mamitsuka, H.3    Kuma, K.4    Kanehisa, M.5
  • 55
    • 33748543961 scopus 로고    scopus 로고
    • Information-theoretic identification of predictive SNPs and supervised visualization of genome-wide association studies
    • 16899448
    • Information-theoretic identification of predictive SNPs and supervised visualization of genome-wide association studies. K Bhasi L Zhang D Brazeau A Zhang M Ramanathan, Nucleic Acids Res 2006 34 14 e101 16899448
    • (2006) Nucleic Acids Res , vol.34 , Issue.14 , pp. 101
    • Bhasi, K.1    Zhang, L.2    Brazeau, D.3    Zhang, A.4    Ramanathan, M.5
  • 56
    • 35948961101 scopus 로고    scopus 로고
    • Predicting and Annotating Catalytic Residues: An Information Theoretic Approach
    • 17887954
    • Predicting and Annotating Catalytic Residues: An Information Theoretic Approach. B Sterner R Singh B Berger, J Comput Biol 2007 14 1058 1073 17887954
    • (2007) J Comput Biol , vol.14 , pp. 1058-1073
    • Sterner, B.1    Singh, R.2    Berger, B.3
  • 57
    • 0035305311 scopus 로고    scopus 로고
    • Relative entropy: Free energy associated with equilibrium fluctuations and nonequilibrium deviations
    • Relative entropy: free energy associated with equilibrium fluctuations and nonequilibrium deviations. H Qian, Phys Rev E 2001 63 4 Pt 1 42103
    • (2001) Phys Rev e , vol.63 , Issue.4 PART 1 , pp. 42103
    • Qian, H.1
  • 58
    • 0000197372 scopus 로고    scopus 로고
    • Large amplitude elastic motions in proteins from a single-parameter, atomic analysis
    • 10063201
    • Large amplitude elastic motions in proteins from a single-parameter, atomic analysis. MM Tirion, Physical Review Letters 1996 77 9 1905 1908 10063201
    • (1996) Physical Review Letters , vol.77 , Issue.9 , pp. 1905-1908
    • Tirion, M.M.1
  • 59
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    • 9218955
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential. I Bahar AR Atilgan B Erman, Fold Des 1997 2 3 173 181 9218955
    • (1997) Fold des , vol.2 , Issue.3 , pp. 173-181
    • Bahar, I.1    Atilgan, A.R.2    Erman, B.3
  • 60
    • 0032533790 scopus 로고    scopus 로고
    • Analysis of domain motions by approximate normal mode calculations
    • 9829700
    • Analysis of domain motions by approximate normal mode calculations. K Hinsen, Proteins 1998 33 3 417 429 9829700
    • (1998) Proteins , vol.33 , Issue.3 , pp. 417-429
    • Hinsen, K.1
  • 61
  • 62
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • 8906967
    • Reduced surface: an efficient way to compute molecular surfaces. MF Sanner AJ Olson JC Spehner, Biopolymers 1996 38 3 305 320 8906967
    • (1996) Biopolymers , vol.38 , Issue.3 , pp. 305-320
    • Sanner, M.F.1    Olson, A.J.2    Spehner, J.C.3
  • 64
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • 7723011
    • SCOP: a structural classification of proteins database for the investigation of sequences and structures. AG Murzin SE Brenner T Hubbard C Chothia, J Mol Biol 1995 247 4 536 540 7723011
    • (1995) J Mol Biol , vol.247 , Issue.4 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 67
    • 0024588901 scopus 로고
    • Structural origins of high-affinity biotin binding to streptavidin
    • 2911722
    • Structural origins of high-affinity biotin binding to streptavidin. PC Weber DH Ohlendorf JJ Wendoloski FR Salemme, Science 1989 243 4887 85 88 2911722
    • (1989) Science , vol.243 , Issue.4887 , pp. 85-88
    • Weber, P.C.1    Ohlendorf, D.H.2    Wendoloski, J.J.3    Salemme, F.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.