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Volumn 6, Issue 4, 2010, Pages

On the conservation of the slow conformational dynamics within the amino acid kinase family: NAGK the paradigm

Author keywords

[No Author keywords available]

Indexed keywords

DYNAMICS; ENZYMES; MARKOV PROCESSES; SIGNAL TRANSDUCTION;

EID: 77954614766     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1000738     Document Type: Article
Times cited : (36)

References (64)
  • 1
    • 20344370764 scopus 로고    scopus 로고
    • Allosteric mechanisms of signal transduction
    • Changeux JP, Edelstein SJ (2005) Allosteric mechanisms of signal transduction. Science 308: 1424-1428.
    • (2005) Science , vol.308 , pp. 1424-1428
    • Changeux, J.P.1    Edelstein, S.J.2
  • 2
    • 30044434744 scopus 로고    scopus 로고
    • Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state
    • USA
    • Tobi D, Bahar I (2005) Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state. Proc Natl Acad Sci U S A 102: 18908-18913.
    • (2005) Proc Natl Acad Sci , vol.102 , pp. 18908-18913
    • Tobi, D.1    Bahar, I.2
  • 3
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • Henzler-Wildman K, Kern D (2007) Dynamic personalities of proteins. Nature 450: 964-972.
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 4
    • 45849131354 scopus 로고    scopus 로고
    • Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution
    • Lange OF, Lakomek NA, Fares C, Schroder GF, Walter KFA, et al. (2008) Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution. Science 320: 1471-1475.
    • (2008) Science , vol.320 , pp. 1471-1475
    • Lange, O.F.1    Lakomek, N.A.2    Fares, C.3    Schroder, G.F.4    Walter, K.F.A.5
  • 5
    • 70149090164 scopus 로고    scopus 로고
    • The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding
    • USA
    • Bakan A, Bahar I (2009) The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding. Proc Natl Acad Sci U S A 106: 14349-14354.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 14349-14354
    • Bakan, A.1    Bahar, I.2
  • 6
    • 38949218425 scopus 로고    scopus 로고
    • Close correspondence between the motions from principal component analysis of multiple HIV-1 protease structures and elastic network modes
    • Yang L, Song G, Carriquiry A, Jernigan RL (2008) Close correspondence between the motions from principal component analysis of multiple HIV-1 protease structures and elastic network modes. Structure 16: 321-330.
    • (2008) Structure , vol.16 , pp. 321-330
    • Yang, L.1    Song, G.2    Carriquiry, A.3    Jernigan, R.L.4
  • 7
    • 61449106774 scopus 로고    scopus 로고
    • Principal component analysis of native ensembles of biomolecular structures (PCA_NEST): Insights into functional dynamics
    • Yang LW, Eyal E, Bahar I, Kitao A (2009) Principal component analysis of native ensembles of biomolecular structures (PCA_NEST): insights into functional dynamics. Bioinformatics 25: 606-614.
    • (2009) Bioinformatics , vol.25 , pp. 606-614
    • Yang, L.W.1    Eyal, E.2    Bahar, I.3    Kitao, A.4
  • 8
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • USA
    • Koshland DE (1958) Application of a theory of enzyme specificity to protein synthesis. Proc Natl Acad Sci U S A 44: 98-104.
    • (1958) Proc Natl Acad Sci , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 9
    • 78651189765 scopus 로고
    • On nature of allosteric transitions - A plausible model
    • Monod J, Wyman J, Changeux JP (1965) On nature of allosteric transitions - A plausible model. J Mol Biol 12: 88-&.
    • (1965) J Mol Biol , vol.12 , pp. 88
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 10
    • 49649084492 scopus 로고    scopus 로고
    • Dynamic energy landscape view of coupled binding and protein conformational change: Induced-fit versus population-shift mechanisms
    • USA
    • Okazaki KI, Takada S (2008) Dynamic energy landscape view of coupled binding and protein conformational change: Induced-fit versus population-shift mechanisms. Proc Natl Acad Sci U S A 105: 11182-11187.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 11182-11187
    • Okazaki, K.I.1    Takada, S.2
  • 13
    • 0035940264 scopus 로고    scopus 로고
    • Energetics and dynamics of enzymatic reactions
    • Villa J, Warshel A (2001) Energetics and dynamics of enzymatic reactions. J Phys Chem B 105: 7887-7907.
    • (2001) J Phys Chem B , vol.105 , pp. 7887-7907
    • Villa, J.1    Warshel, A.2
  • 15
    • 24644521419 scopus 로고    scopus 로고
    • Structure and kinetics of a transient antibody binding intermediate reveal a kinetic discrimination mechanism in antigen recognition
    • USA
    • James LC, Tawfik DS (2005) Structure and kinetics of a transient antibody binding intermediate reveal a kinetic discrimination mechanism in antigen recognition. Proc Natl Acad Sci U S A 102: 12730-12735.
    • (2005) Proc Natl Acad Sci , vol.102 , pp. 12730-12735
    • James, L.C.1    Tawfik, D.S.2
  • 16
    • 52949089027 scopus 로고    scopus 로고
    • Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection
    • USA
    • Sullivan SM, Holyoak T (2008) Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection. Proc Natl Acad Sci U S A 105: 13829-13834.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 13829-13834
    • Sullivan, S.M.1    Holyoak, T.2
  • 17
    • 25844431698 scopus 로고    scopus 로고
    • Coarse-grained normal mode analysis in structural biology
    • Bahar I, Rader AJ (2005) Coarse-grained normal mode analysis in structural biology. Curr Opin Struct Biol 15: 586-592.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 586-592
    • Bahar, I.1    Rader, A.J.2
  • 18
    • 33644559358 scopus 로고    scopus 로고
    • Enzymes: An integrated view of structure, dynamics and function
    • Agarwal PK (2006) Enzymes: An integrated view of structure, dynamics and function. Microb Cell Fact 5.
    • (2006) Microb Cell Fact , pp. 5
    • Agarwal, P.K.1
  • 19
    • 33646742004 scopus 로고    scopus 로고
    • Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variations
    • USA
    • Zheng WJ, Brooks BR, Thirumalai D (2006) Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variations. Proc Natl Acad Sci U S A 103: 7664-7669.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 7664-7669
    • Zheng, W.J.1    Brooks, B.R.2    Thirumalai, D.3
  • 20
    • 67650745346 scopus 로고    scopus 로고
    • Using dynamics-based comparisons to predict nucleic acid binding sites in proteins: An application to OB-fold domains
    • Zen A, de Chiara C, Pastore A, Micheletti C (2009) Using dynamics-based comparisons to predict nucleic acid binding sites in proteins: an application to OB-fold domains. Bioinformatics 25: 1876-1883.
    • (2009) Bioinformatics , vol.25 , pp. 1876-1883
    • Zen, A.1    de Chiara, C.2    Pastore, A.3    Micheletti, C.4
  • 21
    • 43049104657 scopus 로고    scopus 로고
    • Correspondences between low-energy modes in enzymes: Dynamics-based alignment of enzymatic functional families
    • Zen A, Carnevale V, Lesk AM, Micheletti C (2008) Correspondences between low-energy modes in enzymes: Dynamics-based alignment of enzymatic functional families. Protein Sci 17: 918-929.
    • (2008) Protein Sci , vol.17 , pp. 918-929
    • Zen, A.1    Carnevale, V.2    Lesk, A.M.3    Micheletti, C.4
  • 23
    • 0035132230 scopus 로고    scopus 로고
    • Anisotropy of fluctuation dynamics of proteins with an elastic network model
    • Atilgan AR, Durell SR, Jernigan RL, Demirel MC, Keskin O, et al. (2001) Anisotropy of fluctuation dynamics of proteins with an elastic network model. Biophys J 80: 505-515.
    • (2001) Biophys J , vol.80 , pp. 505-515
    • Atilgan, A.R.1    Durell, S.R.2    Jernigan, R.L.3    Demirel, M.C.4    Keskin, O.5
  • 24
    • 0035044995 scopus 로고    scopus 로고
    • Conformational change of proteins arising from normal mode calculations
    • Tama F, Sanejouand YH (2001) Conformational change of proteins arising from normal mode calculations. Protein Eng 14: 1-6.
    • (2001) Protein Eng , vol.14 , pp. 1-6
    • Tama, F.1    Sanejouand, Y.H.2
  • 25
    • 33750407288 scopus 로고    scopus 로고
    • Anisotropic network model: Systematic evaluation and a new web interface
    • Eyal E, Yang LW, Bahar I (2006) Anisotropic network model: systematic evaluation and a new web interface. Bioinformatics 22: 2619-2627.
    • (2006) Bioinformatics , vol.22 , pp. 2619-2627
    • Eyal, E.1    Yang, L.W.2    Bahar, I.3
  • 26
    • 0036721233 scopus 로고    scopus 로고
    • Normal mode analysis of macromolecular motions in a database framework: Developing mode concentration as a useful classifying statistic
    • Krebs WG, Alexandrov V, Wilson CA, Echols N, Yu HY, et al. (2002) Normal mode analysis of macromolecular motions in a database framework: Developing mode concentration as a useful classifying statistic. Proteins-Structure Function and Genetics 48: 682-695.
    • (2002) Proteins-Structure Function and Genetics , vol.48 , pp. 682-695
    • Krebs, W.G.1    Alexandrov, V.2    Wilson, C.A.3    Echols, N.4    Yu, H.Y.5
  • 27
    • 0141792364 scopus 로고    scopus 로고
    • Allosteric changes in protein structure computed by a simple mechanical model: Hemoglobin T - R2 transition
    • Xu CY, Tobi D, Bahar I (2003) Allosteric changes in protein structure computed by a simple mechanical model: Hemoglobin T,-. R2 transition. J Mol Biol 333: 153-168.
    • (2003) J Mol Biol , vol.333 , pp. 153-168
    • Xu, C.Y.1    Tobi, D.2    Bahar, I.3
  • 28
    • 0030599027 scopus 로고    scopus 로고
    • Analysis of the low-frequency normal modes of the R state of aspartate transcarbamylase and a comparison with the T state modes
    • Thomas A, Field MJ, Perahia D (1996) Analysis of the low-frequency normal modes of the R state of aspartate transcarbamylase and a comparison with the T state modes. J Mol Biol 261: 490-506.
    • (1996) J Mol Biol , vol.261 , pp. 490-506
    • Thomas, A.1    Field, M.J.2    Perahia, D.3
  • 29
    • 0029937635 scopus 로고    scopus 로고
    • Motions in hemoglobin studied by normal mode analysis and energy minimization: Evidence for the existence of tertiary T-like, quaternary R-like intermediate structures
    • Mouawad L, Perahia D (1996) Motions in hemoglobin studied by normal mode analysis and energy minimization: Evidence for the existence of tertiary T-like, quaternary R-like intermediate structures. J Mol Biol 258: 393-410.
    • (1996) J Mol Biol , vol.258 , pp. 393-410
    • Mouawad, L.1    Perahia, D.2
  • 30
    • 34248159870 scopus 로고    scopus 로고
    • Thorough validation of protein normal mode analysis: A comparative study with essential dynamics
    • Rueda M, Chacon P, Orozco M (2007) Thorough validation of protein normal mode analysis: A comparative study with essential dynamics. Structure 15: 565-575.
    • (2007) Structure , vol.15 , pp. 565-575
    • Rueda, M.1    Chacon, P.2    Orozco, M.3
  • 31
    • 70449923870 scopus 로고    scopus 로고
    • A comparative analysis of the equilibrium dynamics of a designed protein inferred from NMR, X-ray, and computations
    • Liu L, Koharudin LMI, Gronenborn AM, Bahar I (2009) A comparative analysis of the equilibrium dynamics of a designed protein inferred from NMR, X-ray, and computations. Proteins-Structure Function and Bioinformatics 77: 927-939.
    • (2009) Proteins-Structure Function and Bioinformatics , vol.77 , pp. 927-939
    • Liu, L.1    Koharudin, L.M.I.2    Gronenborn, A.M.3    Bahar, I.4
  • 32
    • 0036118398 scopus 로고    scopus 로고
    • Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis
    • Ramon-Maiques S, Marina A, Gil-Ortiz F, Fita I, Rubio V (2002) Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis. Structure 10: 329-342.
    • (2002) Structure , vol.10 , pp. 329-342
    • Ramon-Maiques, S.1    Marina, A.2    Gil-Ortiz, F.3    Fita, I.4    Rubio, V.5
  • 33
    • 0037485781 scopus 로고    scopus 로고
    • The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase, determined from the structures of crystalline complexes, including a complex with an AlF4- transition state mimic
    • Gil-Ortiz F, Ramon-Maiques S, Fita I, Rubio V (2003) The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase, determined from the structures of crystalline complexes, including a complex with an AlF4- transition state mimic. J Mol Biol 331: 231-244.
    • (2003) J Mol Biol , vol.331 , pp. 231-244
    • Gil-Ortiz, F.1    Ramon-Maiques, S.2    Fita, I.3    Rubio, V.4
  • 34
    • 31344471928 scopus 로고    scopus 로고
    • Structural bases of feed-back control of arginine biosynthesis, revealed by the structures of two hexameric N-acetylglutamate kinases, from Thermotoga maritima and Pseudomonas aeruginosa
    • Ramon-Maiques S, Fernandez-Murga ML, Gil-Ortiz F, Vagin A, Fita I, et al. (2006) Structural bases of feed-back control of arginine biosynthesis, revealed by the structures of two hexameric N-acetylglutamate kinases, from Thermotoga maritima and Pseudomonas aeruginosa. J Mol Biol 356: 695-713.
    • (2006) J Mol Biol , vol.356 , pp. 695-713
    • Ramon-Maiques, S.1    Fernandez-Murga, M.L.2    Gil-Ortiz, F.3    Vagin, A.4    Fita, I.5
  • 35
    • 41949141258 scopus 로고    scopus 로고
    • Basis of arginine sensitivity of microbial N-acetyl-L-glutamate kinases: Mutagenesis and protein engineering study with the Pseudomonas aeruginosa and Escherichia coli enzymes
    • Fernandez-Murga ML, Rubio V (2008) Basis of arginine sensitivity of microbial N-acetyl-L-glutamate kinases: Mutagenesis and protein engineering study with the Pseudomonas aeruginosa and Escherichia coli enzymes. J Bacteriol 190: 3018-3025.
    • (2008) J Bacteriol , vol.190 , pp. 3018-3025
    • Fernandez-Murga, M.L.1    Rubio, V.2
  • 36
    • 0242411465 scopus 로고    scopus 로고
    • Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and aspartokinase III probes the catalytic and substrate-binding mechanisms of these amino acid kinase family enzymes and allows three-dimensional modelling of aspartokinase
    • Marco-Marin C, Ramon-Maiques S, Tavarez S, Rubio V (2003) Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and aspartokinase III probes the catalytic and substrate-binding mechanisms of these amino acid kinase family enzymes and allows three-dimensional modelling of aspartokinase. J Mol Biol 334: 459-476.
    • (2003) J Mol Biol , vol.334 , pp. 459-476
    • Marco-Marin, C.1    Ramon-Maiques, S.2    Tavarez, S.3    Rubio, V.4
  • 37
    • 20444409186 scopus 로고    scopus 로고
    • Coupling between catalytic site and collective dynamics: A requirement for mechanochemical activity of enzymes
    • Yang LW, Bahar I (2005) Coupling between catalytic site and collective dynamics: A requirement for mechanochemical activity of enzymes. Structure 13: 893-904.
    • (2005) Structure , vol.13 , pp. 893-904
    • Yang, L.W.1    Bahar, I.2
  • 38
    • 37349007321 scopus 로고    scopus 로고
    • On the relationship between thermal stability and catalytic power of enzymes
    • Roca M, Liu H, Messer B, Warshel A (2007) On the relationship between thermal stability and catalytic power of enzymes. Biochemistry 46: 15076-15088.
    • (2007) Biochemistry , vol.46 , pp. 15076-15088
    • Roca, M.1    Liu, H.2    Messer, B.3    Warshel, A.4
  • 39
    • 0016613586 scopus 로고
    • N-Acetylglutamate 5-phosphotransferase of Pseudomonas Aeruginosa - Catalytic and regulatory properties
    • Haas D, Leisinger T (1975) N-Acetylglutamate 5-phosphotransferase of Pseudomonas Aeruginosa - Catalytic and regulatory properties. Eur J Biochem 52: 377-383.
    • (1975) Eur J Biochem , vol.52 , pp. 377-383
    • Haas, D.1    Leisinger, T.2
  • 40
    • 34848882812 scopus 로고    scopus 로고
    • Signal propagation in proteins and relation to equilibrium fluctuations
    • Chennubhotla C, Bahar I (2007) Signal propagation in proteins and relation to equilibrium fluctuations. PLoS Comput Biol 3: 1716-1726.
    • (2007) PLoS Comput Biol , vol.3 , pp. 1716-1726
    • Chennubhotla, C.1    Bahar, I.2
  • 43
    • 23244442698 scopus 로고    scopus 로고
    • Probing the local dynamics of nucleotide-binding pocket coupled to the global dynamics: Myosin versus kinesin
    • Zheng WJ, Brooks BR (2005) Probing the local dynamics of nucleotide-binding pocket coupled to the global dynamics: Myosin versus kinesin. Biophys J 89: 167-178.
    • (2005) Biophys J , vol.89 , pp. 167-178
    • Zheng, W.J.1    Brooks, B.R.2
  • 44
    • 0034595434 scopus 로고    scopus 로고
    • The 1.5 angstrom resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases
    • Ramon-Maiques S, Marina A, Uriarte M, Fita I, Rubio V (2000) The 1.5 angstrom resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases. J Mol Biol 299: 463-476.
    • (2000) J Mol Biol , vol.299 , pp. 463-476
    • Ramon-Maiques, S.1    Marina, A.2    Uriarte, M.3    Fita, I.4    Rubio, V.5
  • 45
    • 23944435947 scopus 로고    scopus 로고
    • The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis
    • Marco-Marin C, Gil-Ortiz F, Rubio V (2005) The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis. J Mol Biol 352: 438-454.
    • (2005) J Mol Biol , vol.352 , pp. 438-454
    • Marco-Marin, C.1    Gil-Ortiz, F.2    Rubio, V.3
  • 46
    • 33745024278 scopus 로고    scopus 로고
    • Symmetry, form, and shape: Guiding principles for robustness in macromolecular machines
    • Tama F, Brooks CL (2006) Symmetry, form, and shape: Guiding principles for robustness in macromolecular machines. Annu Rev Biophys Biomol Struct 35: 115-133.
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 115-133
    • Tama, F.1    Brooks, C.L.2
  • 47
    • 33644517853 scopus 로고    scopus 로고
    • Functional modes of proteins are among the most robust
    • Nicolay S, Sanejouand YH (2006) Functional modes of proteins are among the most robust. Phys Rev Lett 96.
    • (2006) Phys Rev Lett , pp. 96
    • Nicolay, S.1    Sanejouand, Y.H.2
  • 49
    • 0036840202 scopus 로고    scopus 로고
    • A coarse-grained normal mode approach for macromolecules: An efficient implementation and application to Ca2+-ATPase
    • Li GH, Cui Q (2002) A coarse-grained normal mode approach for macromolecules: An efficient implementation and application to Ca2+-ATPase. Biophys J 83: 2457-2474.
    • (2002) Biophys J , vol.83 , pp. 2457-2474
    • Li, G.H.1    Cui, Q.2
  • 50
    • 3242875210 scopus 로고    scopus 로고
    • ElNemo: A normal mode web server for protein movement analysis and the generation of templates for molecular replacement
    • Suhre K, Sanejouand YH (2004) ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Res 32: W610-W614.
    • (2004) Nucleic Acids Res , vol.32
    • Suhre, K.1    Sanejouand, Y.H.2
  • 51
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    • Bahar I, Atilgan AR, Erman B (1997) Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential. Folding & Design 2: 173-181.
    • (1997) Folding & Design , vol.2 , pp. 173-181
    • Bahar, I.1    Atilgan, A.R.2    Erman, B.3
  • 52
    • 0035996990 scopus 로고    scopus 로고
    • Dynamics of proteins in crystals: Comparison of experiment with simple models
    • Kundu S, Melton JS, Sorensen DC, Phillips GN (2002) Dynamics of proteins in crystals: Comparison of experiment with simple models. Biophys J 83: 723-732.
    • (2002) Biophys J , vol.83 , pp. 723-732
    • Kundu, S.1    Melton, J.S.2    Sorensen, D.C.3    Phillips, G.N.4
  • 53
    • 0345973041 scopus 로고    scopus 로고
    • Gaussian dynamics of folded proteins
    • Haliloglu T, Bahar I, Erman B (1997) Gaussian dynamics of folded proteins. Phys Rev Lett 79: 3090-3093.
    • (1997) Phys Rev Lett , vol.79 , pp. 3090-3093
    • Haliloglu, T.1    Bahar, I.2    Erman, B.3
  • 54
    • 58849116413 scopus 로고    scopus 로고
    • Application of Elastic Network Models to Proteins in the Crystalline State
    • Riccardi D, Cui Q, Phillips GN (2009) Application of Elastic Network Models to Proteins in the Crystalline State. Biophys J 96: 464-475.
    • (2009) Biophys J , vol.96 , pp. 464-475
    • Riccardi, D.1    Cui, Q.2    Phillips, G.N.3
  • 55
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, van der Spoel D (2001) GROMACS 3.0: a package for molecular simulation and trajectory analysis. Journal of Molecular Modeling 7: 306-317.
    • (2001) Journal of Molecular Modeling , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 56
    • 47649125643 scopus 로고    scopus 로고
    • Allosteric regulation and catalysis emerge via a common route
    • Goodey NM, Benkovic SJ (2008) Allosteric regulation and catalysis emerge via a common route. Nat Chem Biol 4: 474-482.
    • (2008) Nat Chem Biol , vol.4 , pp. 474-482
    • Goodey, N.M.1    Benkovic, S.J.2
  • 58
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel GM, Lockless SW, Wall MA, Ranganathan R (2003) Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nat Struct Biol 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
  • 60
    • 33749055796 scopus 로고    scopus 로고
    • Markov propagation of allosteric effects in biomolecular systems: Application to GroEL-GroES
    • Chennubhotla C, Bahar I (2006) Markov propagation of allosteric effects in biomolecular systems: application to GroEL-GroES. Mol Syst Biol 2.
    • (2006) Mol Syst Biol , pp. 2
    • Chennubhotla, C.1    Bahar, I.2
  • 61
    • 33645102817 scopus 로고    scopus 로고
    • Interactions in native binding sites cause a large change in protein dynamics
    • Ming DM, Wall ME (2006) Interactions in native binding sites cause a large change in protein dynamics. J Mol Biol 358: 213-223.
    • (2006) J Mol Biol , vol.358 , pp. 213-223
    • Ming, D.M.1    Wall, M.E.2
  • 62
    • 0000359491 scopus 로고    scopus 로고
    • On the quadratic reaction path evaluated in a reduced potential energy surface model and the problem to locate transition states
    • Anglada JM, Besalu E, Bofill JM, Crehuet R (2001) On the quadratic reaction path evaluated in a reduced potential energy surface model and the problem to locate transition states. J Comput Chem 22: 387-406.
    • (2001) J Comput Chem , vol.22 , pp. 387-406
    • Anglada, J.M.1    Besalu, E.2    Bofill, J.M.3    Crehuet, R.4


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