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Volumn 117, Issue 44, 2013, Pages 13775-13785

How conformational flexibility stabilizes the hyperthermophilic elongation factor G-domain

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL FLEXIBILITY; CONFORMATIONAL SUBSTATES; EXTENSIVE SIMULATIONS; INTERNAL FLUCTUATION; MECHANICAL EXCITATIONS; TECHNOLOGICAL APPLICATIONS; THERMOPHILIC ORGANISMS; THERMOPHILIC PROTEINS;

EID: 84887752230     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp407078z     Document Type: Article
Times cited : (34)

References (85)
  • 1
    • 0026800672 scopus 로고
    • Analysis of the Heat Capacity Dependence of Protein Folding
    • Yang, A.-S.; Sharp, K. A.; Honig, B. Analysis of the Heat Capacity Dependence of Protein Folding J. Mol. Biol. 1992, 227, 889-900
    • (1992) J. Mol. Biol. , vol.227 , pp. 889-900
    • Yang, A.-S.1    Sharp, K.A.2    Honig, B.3
  • 2
    • 0000159569 scopus 로고    scopus 로고
    • Protein Structure and the Energetics of Protein Stability
    • Robertson, A. D.; Murphy, K. P. Protein Structure and the Energetics of Protein Stability Chem. Rev. 1997, 97, 1251-1268
    • (1997) Chem. Rev. , vol.97 , pp. 1251-1268
    • Robertson, A.D.1    Murphy, K.P.2
  • 4
    • 34948815009 scopus 로고    scopus 로고
    • A Diverse Family of Thermostable Cytochrome P450s Created by Recombination of Stabilizing Fragments
    • Li, Y.; Drummond, D. A.; Sawayama, A. M.; Snow, C. D.; Bloom, J. D.; Arnold, F. H. A Diverse Family of Thermostable Cytochrome P450s Created by Recombination of Stabilizing Fragments Nat. Biotechnol. 2007, 25, 1051-1056
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1051-1056
    • Li, Y.1    Drummond, D.A.2    Sawayama, A.M.3    Snow, C.D.4    Bloom, J.D.5    Arnold, F.H.6
  • 5
    • 33845288649 scopus 로고    scopus 로고
    • Iterative Saturation Mutagenesis on the Basis of B Factors as a Strategy for Increasing Protein Thermostability
    • Reetz, M. T.; Carballeira, J. D.; Vogel, A. Iterative Saturation Mutagenesis on the Basis of B Factors as a Strategy for Increasing Protein Thermostability Angew. Chem. 2006, 45, 7745-7751
    • (2006) Angew. Chem. , vol.45 , pp. 7745-7751
    • Reetz, M.T.1    Carballeira, J.D.2    Vogel, A.3
  • 6
    • 0035910266 scopus 로고    scopus 로고
    • Achieving Stability and Conformational Specificity in Designed Proteins via Binary Patterning
    • Marshall, S. A.; Mayo, S. L. Achieving Stability and Conformational Specificity in Designed Proteins via Binary Patterning J. Mol. Biol. 2001, 305, 619-631
    • (2001) J. Mol. Biol. , vol.305 , pp. 619-631
    • Marshall, S.A.1    Mayo, S.L.2
  • 7
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability
    • Vieille, C.; Zeikus, G. J. Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability Microbiol. Mol. Biol. Rev. 2001, 65, 1-43
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 8
    • 0032438190 scopus 로고    scopus 로고
    • The Stability of Proteins in Extreme Environments
    • Jaenicke, R.; Böhm, G. The Stability of Proteins in Extreme Environments Curr. Opin. Struct. Biol. 1998, 8, 738-748
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 738-748
    • Jaenicke, R.1    Böhm, G.2
  • 9
    • 84856833536 scopus 로고    scopus 로고
    • Thermophilic Proteins: Insight and Perspective from in Silico Experiments
    • Sterpone, F.; Melchionna, S. Thermophilic Proteins: Insight and Perspective from in Silico Experiments Chem. Soc. Rev. 2012, 41, 1665-1676
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 1665-1676
    • Sterpone, F.1    Melchionna, S.2
  • 10
    • 33745726737 scopus 로고    scopus 로고
    • Lessons in Stability from Thermophilic Proteins
    • Razvi, A.; Scholtz, J. M. Lessons in Stability from Thermophilic Proteins Protein Sci. 2006, 15, 1569-1578
    • (2006) Protein Sci. , vol.15 , pp. 1569-1578
    • Razvi, A.1    Scholtz, J.M.2
  • 11
    • 0025182490 scopus 로고
    • Extremely Thermostable D-glyceraldehyde-3-phosphate Dehydrogenase from the Eubacterium Thermotoga Maritima
    • Wrba, A.; Schweiger, A.; Schultes, V.; Jaenicke, R.; Zavodszky, P. Extremely Thermostable D-glyceraldehyde-3-phosphate Dehydrogenase from the Eubacterium Thermotoga Maritima Biochemistry 1990, 29, 7584-7592
    • (1990) Biochemistry , vol.29 , pp. 7584-7592
    • Wrba, A.1    Schweiger, A.2    Schultes, V.3    Jaenicke, R.4    Zavodszky, P.5
  • 12
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of Conformational Flexibility is a Key Event in the Thermal Adaptation of Proteins
    • Závodszky, P.; Kardos, J.; Svingor, A.; Petsko, G. A. Adjustment of Conformational Flexibility is a Key Event in the Thermal Adaptation of Proteins Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 7406-7411
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 7406-7411
    • Závodszky, P.1    Kardos, J.2    Svingor, A.3    Petsko, G.A.4
  • 13
    • 0034724392 scopus 로고    scopus 로고
    • Millisecond Time Scale Conformational Flexibility in a Hyperthermophile Protein at Ambient Temperature
    • Hernandez, G.; Jenney, F. E.; Adams, M. W. W.; LeMaster, D. M. Millisecond Time Scale Conformational Flexibility in a Hyperthermophile Protein at Ambient Temperature Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 3166-3170
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 3166-3170
    • Hernandez, G.1    Jenney, F.E.2    Adams, M.W.W.3    Lemaster, D.M.4
  • 14
    • 0034724271 scopus 로고    scopus 로고
    • Do Ultrastable Proteins from Hyperthermophiles Have High or Low Conformational Rigidity?
    • Jaenicke, R. Do Ultrastable Proteins from Hyperthermophiles Have High or Low Conformational Rigidity? Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 2962-2964
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 2962-2964
    • Jaenicke, R.1
  • 15
    • 0033865067 scopus 로고    scopus 로고
    • Structural Equilibrium Fluctuations in Mesophilic and Thermophilic a-Amylase
    • Fitter, J.; Heberle, J. Structural Equilibrium Fluctuations in Mesophilic and Thermophilic a-Amylase Biophys. J. 2000, 79, 1629-1636
    • (2000) Biophys. J. , vol.79 , pp. 1629-1636
    • Fitter, J.1    Heberle, J.2
  • 16
    • 2542487312 scopus 로고    scopus 로고
    • Multiple Time Scale Backbone Dynamics of Homologous Thermophilic and Mesophilic Ribonuclease HI Enzymes
    • Butterwick, J. A.; Loria, J. P.; Astrof, N. S.; Kroenke, C. D.; Cole, R.; Rance, M.; A., G. P., III Multiple Time Scale Backbone Dynamics of Homologous Thermophilic and Mesophilic Ribonuclease HI Enzymes J. Mol. Biol. 2004, 339, 855-871
    • (2004) J. Mol. Biol. , vol.339 , pp. 855-871
    • Butterwick, J.A.1    Loria, J.P.2    Astrof, N.S.3    Kroenke, C.D.4    Cole, R.5    Rance III, M.A.G.P.6
  • 17
    • 28844498987 scopus 로고    scopus 로고
    • Neutron Scattering Reveals the Dynamic Basis of Protein Adaptation to Extreme Temperature
    • Tehei, M.; Madern, D.; Franzetti, B.; Zaccai, G. Neutron Scattering Reveals the Dynamic Basis of Protein Adaptation to Extreme Temperature J. Biol. Chem. 2005, 280, 40974-40979
    • (2005) J. Biol. Chem. , vol.280 , pp. 40974-40979
    • Tehei, M.1    Madern, D.2    Franzetti, B.3    Zaccai, G.4
  • 18
    • 45849083521 scopus 로고    scopus 로고
    • Protein Dynamics and Stability: The Distribution of Atomic Fluctuations in Thermophilic and Mesophilic Dihydrofolate Reductase Derived Using Elastic Incoherent Neutron Scattering
    • Meinhold, L.; Clement, D.; Tehei, M.; Daniel, R.; Finney, J. L.; Smith, J. C. Protein Dynamics and Stability: The Distribution of Atomic Fluctuations in Thermophilic and Mesophilic Dihydrofolate Reductase Derived Using Elastic Incoherent Neutron Scattering Biophys. J. 2008, 94, 4812-4818
    • (2008) Biophys. J. , vol.94 , pp. 4812-4818
    • Meinhold, L.1    Clement, D.2    Tehei, M.3    Daniel, R.4    Finney, J.L.5    Smith, J.C.6
  • 19
    • 0032573431 scopus 로고    scopus 로고
    • The Stability of Salt Bridges at High Temperatures: Implications for Hyperthermophilic Proteins
    • Elcock, A. H. The Stability of Salt Bridges at High Temperatures: Implications for Hyperthermophilic Proteins J. Mol. Biol. 1998, 284, 489-502
    • (1998) J. Mol. Biol. , vol.284 , pp. 489-502
    • Elcock, A.H.1
  • 20
    • 0033603392 scopus 로고    scopus 로고
    • Electrostatic Contributions to the Stability of Hyperthermophilic Proteins
    • Xiao, L.; Honig, B. Electrostatic Contributions to the Stability of Hyperthermophilic Proteins J. Mol. Biol. 1999, 289, 1435-1444
    • (1999) J. Mol. Biol. , vol.289 , pp. 1435-1444
    • Xiao, L.1    Honig, B.2
  • 21
    • 4444362321 scopus 로고    scopus 로고
    • An Electrostatic Basis for the Stability of Thermophilic Proteins
    • Dominy, B. N.; Minoux, H.; Brooks, C. L., 3rd An Electrostatic Basis for the Stability of Thermophilic Proteins Proteins 2004, 57, 128-141
    • (2004) Proteins , vol.57 , pp. 128-141
    • Dominy, B.N.1    Minoux, H.2    Brooks III, C.L.3
  • 22
    • 33749442531 scopus 로고    scopus 로고
    • Similarity and Difference in the Unfolding of Thermophilic and Mesophilic Cold Shock Proteins Studied by Molecular Dynamics Simulations
    • Huang, X.; Zhou, H.-X. Similarity and Difference in the Unfolding of Thermophilic and Mesophilic Cold Shock Proteins Studied by Molecular Dynamics Simulations Biophys. J. 2006, 91, 2451-2463
    • (2006) Biophys. J. , vol.91 , pp. 2451-2463
    • Huang, X.1    Zhou, H.-X.2
  • 25
    • 84871198117 scopus 로고    scopus 로고
    • Promiscuous Contacts and Heightened Dynamics Increase Thermostability in an Engineered Variant of the Engrailed Homeodomain
    • McCully, M.; Beck, D.; Daggett, V. Promiscuous Contacts and Heightened Dynamics Increase Thermostability in an Engineered Variant of the Engrailed Homeodomain Protein. Eng. Des. Sel. 2013, 26, 35-45
    • (2013) Protein. Eng. Des. Sel. , vol.26 , pp. 35-45
    • McCully, M.1    Beck, D.2    Daggett, V.3
  • 26
    • 34250845103 scopus 로고    scopus 로고
    • Metastable Water Clusters in the Nonpolar Cavities of the Thermostable Protein Tetrabrachion
    • Yin, H.; Hummer, G.; Rasaiah, J. C. Metastable Water Clusters in the Nonpolar Cavities of the Thermostable Protein Tetrabrachion J. Am. Chem. Soc. 2007, 129, 7369-7377
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 7369-7377
    • Yin, H.1    Hummer, G.2    Rasaiah, J.C.3
  • 28
    • 82955206478 scopus 로고    scopus 로고
    • Crowding Induces Differences in the Diffusion of Thermophilic and Mesophilic Proteins: A New Look at Neutron Scattering Results
    • Marcos, E.; Mestres, P.; Crehuet, R. Crowding Induces Differences in the Diffusion of Thermophilic and Mesophilic Proteins: A New Look at Neutron Scattering Results Biophys. J. 2011, 101, 2782-2789
    • (2011) Biophys. J. , vol.101 , pp. 2782-2789
    • Marcos, E.1    Mestres, P.2    Crehuet, R.3
  • 29
    • 84858320073 scopus 로고    scopus 로고
    • Dynamic Fingerprints of Protein Thermostability Revealed by Long Molecular Dynamics
    • Marcos, E.; Jiménez, A.; Crehuet, R. Dynamic Fingerprints of Protein Thermostability Revealed by Long Molecular Dynamics J. Chem. Theory. Comput. 2012, 8, 1129-1142
    • (2012) J. Chem. Theory. Comput. , vol.8 , pp. 1129-1142
    • Marcos, E.1    Jiménez, A.2    Crehuet, R.3
  • 30
    • 84874409618 scopus 로고    scopus 로고
    • Do Homologous Thermophilic-Mesophilic Proteins Exhibit Similar Structures and Dynamics at Optimal Growth Temperatures? A Molecular Dynamics Simulation Study
    • Basu, S.; Sen, S. Do Homologous Thermophilic-Mesophilic Proteins Exhibit Similar Structures and Dynamics at Optimal Growth Temperatures? A Molecular Dynamics Simulation Study J. Chem. Inf. Model. 2013, 53, 423-434
    • (2013) J. Chem. Inf. Model. , vol.53 , pp. 423-434
    • Basu, S.1    Sen, S.2
  • 31
    • 84884561782 scopus 로고    scopus 로고
    • Molecular Dynamics Perspective on the Protein Thermal Stability: A Case Study Using SAICAR Synthetase
    • 10.1021/ci400306m
    • Manjunath, K.; Sekar, K. Molecular Dynamics Perspective on the Protein Thermal Stability: A Case Study Using SAICAR Synthetase J. Chem. Inf. Model. 2013, 10.1021/ci400306m
    • (2013) J. Chem. Inf. Model.
    • Manjunath, K.1    Sekar, K.2
  • 32
    • 37349007321 scopus 로고    scopus 로고
    • On the Relationship between Thermal Stability and Catalytic Power of Enzymes
    • Roca, M.; Liu, H.; Messer, B.; Warshel, A. On the Relationship between Thermal Stability and Catalytic Power of Enzymes Biochemistry 2007, 46, 15076-15088
    • (2007) Biochemistry , vol.46 , pp. 15076-15088
    • Roca, M.1    Liu, H.2    Messer, B.3    Warshel, A.4
  • 33
    • 0024312593 scopus 로고
    • Structure-Function Relationships of Elongation Factor Tu. Isolation and Activity of the Guanine-Nucleotide-Binding Gomain
    • Jensen, M.; Cool, R.; Mortensen, K.; Clark, B.; Parmeggiani, A. Structure-Function Relationships of Elongation Factor Tu. Isolation and Activity of the Guanine-Nucleotide-Binding Gomain Eur. J. Biochm. 1989, 182, 247-255
    • (1989) Eur. J. Biochm. , vol.182 , pp. 247-255
    • Jensen, M.1    Cool, R.2    Mortensen, K.3    Clark, B.4    Parmeggiani, A.5
  • 34
    • 2542516344 scopus 로고    scopus 로고
    • The Crystal Structure of Sulfolobus Solfataricus Elongation Factor 1a in Complex with Magnesium and GDP
    • Luigi, V.; Alessia, R.; Mariorosario, M.; Piergiuseppe, C.; Paolo, A.; Adriana, Z. The Crystal Structure of Sulfolobus Solfataricus Elongation Factor 1a in Complex with Magnesium and GDP Biochemistry 2004, 43, 6630-6636
    • (2004) Biochemistry , vol.43 , pp. 6630-6636
    • Luigi, V.1    Alessia, R.2    Mariorosario, M.3    Piergiuseppe, C.4    Paolo, A.5    Adriana, Z.6
  • 35
    • 0033593370 scopus 로고    scopus 로고
    • Crystal Structure of Intact Elongation Factor EF-Tu from Escherichia coli in GDP Conformation at 2.05 Å Resolution
    • Song, H.; Parsons, M. R.; Rowsell, S.; Leonard, G.; Phillips, S. E. Crystal Structure of Intact Elongation Factor EF-Tu from Escherichia coli in GDP Conformation at 2.05 Å Resolution J. Mol. Biol. 1999, 285, 1245-1256
    • (1999) J. Mol. Biol. , vol.285 , pp. 1245-1256
    • Song, H.1    Parsons, M.R.2    Rowsell, S.3    Leonard, G.4    Phillips, S.E.5
  • 36
    • 3142714765 scopus 로고    scopus 로고
    • Extending the Treatment of Backbone Energetics in Protein Force Fields: Limitations of Gas-phase Quantum Mechanics in Reproducing Protein Conformational Distributions in Molecular Dynamics Simulations
    • MacKerell, A. D.; Feig, M.; Brooks(III), C. L. Extending the Treatment of Backbone Energetics in Protein Force Fields: Limitations of Gas-phase Quantum Mechanics in Reproducing Protein Conformational Distributions in Molecular Dynamics Simulations J. Comput. Chem. 2004, 25, 1400-1415
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • Mackerell, A.D.1    Feig, M.2    Brooks III, C.L.3
  • 37
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of Multiple Amber Force Fields and Development of Improved Protein Backbone Parameters
    • Hornak, V.; Abel, R.; Okur, A.; Strockbine, B.; Roitberg, A.; Simmerling, C. Comparison of Multiple Amber Force Fields and Development of Improved Protein Backbone Parameters Proteins 2006, 15, 712-725
    • (2006) Proteins , vol.15 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 39
    • 84889585833 scopus 로고    scopus 로고
    • Using Collective Variables to Drive Molecular Dynamics Simulations
    • in press
    • Fiorin, G.; Klein, M. L.; Hénin, J. Using Collective Variables to Drive Molecular Dynamics Simulations. Mol. Phys. 2013, in press
    • (2013) Mol. Phys.
    • Fiorin, G.1    Klein, M.L.2    Hénin, J.3
  • 40
    • 84869064697 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of a Characteristic DPC Micelle in Water
    • Abel, S.; Dupradeau, F.-Y.; Marchi, M. Molecular Dynamics Simulations of a Characteristic DPC Micelle in Water J. Chem. Theory. Comput. 2012, 8, 4610-4623
    • (2012) J. Chem. Theory. Comput. , vol.8 , pp. 4610-4623
    • Abel, S.1    Dupradeau, F.-Y.2    Marchi, M.3
  • 41
    • 74349095210 scopus 로고    scopus 로고
    • VORO++: A Three-Dimensional Voronoi Cell Library in C++
    • Rycroft, C. VORO++: A Three-Dimensional Voronoi Cell Library in C++ Chaos 2009, 19, 041111
    • (2009) Chaos , vol.19 , pp. 041111
    • Rycroft, C.1
  • 43
    • 0020102027 scopus 로고
    • Least Squares Quantization in PCM
    • Lloyd, S. P. Least Squares Quantization in PCM IEEE Trans. Inf. Theory 1982, 28, 129-137
    • (1982) IEEE Trans. Inf. Theory , vol.28 , pp. 129-137
    • Lloyd, S.P.1
  • 46
    • 33645695182 scopus 로고    scopus 로고
    • Department of Physics and Beckman Institute, University of Illinois: Urbana, IL.
    • Schulten, K.; Kosztin, I. Lectures in Theoretical Biophysics; Department of Physics and Beckman Institute, University of Illinois: Urbana, IL, 2000.
    • (2000) Lectures in Theoretical Biophysics
    • Schulten, K.1    Kosztin, I.2
  • 47
    • 23244438863 scopus 로고    scopus 로고
    • Position-dependent diffusion Coefficients and Free Energies from Bayesian Analysis of Equilibrium and Replica Molecular Dynamics Simulations
    • Hummer, G. Position-dependent diffusion Coefficients and Free Energies from Bayesian Analysis of Equilibrium and Replica Molecular Dynamics Simulations New J. Phys. 2005, 7, 34
    • (2005) New J. Phys. , vol.7 , pp. 34
    • Hummer, G.1
  • 49
    • 33947716119 scopus 로고    scopus 로고
    • A Semiempirical Free Energy Force Field with Charge-Based Desolvation
    • Huey, R.; Morris, G. M.; Olson, A. J.; Goodsell, D. S. A Semiempirical Free Energy Force Field with Charge-Based Desolvation J. Comput. Chem. 2007, 28, 1145-1152
    • (2007) J. Comput. Chem. , vol.28 , pp. 1145-1152
    • Huey, R.1    Morris, G.M.2    Olson, A.J.3    Goodsell, D.S.4
  • 51
    • 85083147269 scopus 로고    scopus 로고
    • R Development Core Team, R: A Language and Environment for Statistical Computing. R Foundation for Statistical Computing: Vienna, Austria, 2008; ISBN 3-900051-07-0
    • R Development Core Team, R: A Language and Environment for Statistical Computing. R Foundation for Statistical Computing: Vienna, Austria, 2008; ISBN 3-900051-07-0.
  • 52
    • 0032568599 scopus 로고    scopus 로고
    • Funnels and Frustration in Off-Lattice Minimalist Protein Landscapes
    • Nymeyer, H.; Onuchic, A. G.; Folding, J. Funnels and Frustration in Off-Lattice Minimalist Protein Landscapes Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 5921-5928
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 5921-5928
    • Nymeyer, H.1    Onuchic, A.G.2    Folding, J.3
  • 53
    • 75749153687 scopus 로고    scopus 로고
    • Coordinate-Dependent Diffusion in Protein Folding
    • Best, R.; Hummer, G. Coordinate-Dependent Diffusion in Protein Folding Proc. Natl. Acad. Sci. U.S.A. 2010, 1088-1093
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , pp. 1088-1093
    • Best, R.1    Hummer, G.2
  • 54
    • 0030587932 scopus 로고    scopus 로고
    • An α to β Conformational Switch in EF-Tu
    • Abel, K.; Yoder, M. D.; Hilgenfeld, R.; Jurnak, F. An α to β Conformational Switch in EF-Tu Structure 1996, 4, 1153-1159
    • (1996) Structure , vol.4 , pp. 1153-1159
    • Abel, K.1    Yoder, M.D.2    Hilgenfeld, R.3    Jurnak, F.4
  • 57
    • 2142820913 scopus 로고    scopus 로고
    • Atomic Mean-Square Displacements in Proteins by Molecular Dynamics: A Case for Analysis of Variance
    • Maragliano, L.; Cottone, G.; Cordone, L.; Ciccotti, G. Atomic Mean-Square Displacements in Proteins by Molecular Dynamics: A Case for Analysis of Variance Biophys. J. 2004, 88, 2765-2772
    • (2004) Biophys. J. , vol.88 , pp. 2765-2772
    • Maragliano, L.1    Cottone, G.2    Cordone, L.3    Ciccotti, G.4
  • 60
    • 84927514013 scopus 로고
    • Nouvelles Applications des Paramètres Continus à la Théorie des Formes Quadratiques
    • Voronoi, G. F. Nouvelles Applications des Paramètres Continus à la Théorie des Formes Quadratiques. J. Reine Angew. Math. 1908, 134.
    • (1908) J. Reine Angew. Math. , vol.134
    • Voronoi, G.F.1
  • 62
    • 0036931447 scopus 로고    scopus 로고
    • Toward the Physical Basis of Thermophilic Proteins: Linking of Enriched Polar Interactions and Reduced Heat Capacity of Unfolding
    • Zhou, H.-X. Toward the Physical Basis of Thermophilic Proteins: Linking of Enriched Polar Interactions and Reduced Heat Capacity of Unfolding Biophys. J. 2002, 83, 3126-3133
    • (2002) Biophys. J. , vol.83 , pp. 3126-3133
    • Zhou, H.-X.1
  • 64
    • 0345598919 scopus 로고    scopus 로고
    • Adhesive-Cohesive Model for Protein Compressibility: An Alternative Perspective on Stability
    • Dadarlat, V. M.; Post, C. B. Adhesive-Cohesive Model for Protein Compressibility: An Alternative Perspective on Stability Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 14778-14783
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 14778-14783
    • Dadarlat, V.M.1    Post, C.B.2
  • 65
    • 44949259971 scopus 로고    scopus 로고
    • Mechanistic Elements of Protein Cold Denaturation
    • Lopez, C. F.; Darst, R. K.; Rossky, P. J. Mechanistic Elements of Protein Cold Denaturation J. Phys. Chem. B 2008, 112, 5961-5967
    • (2008) J. Phys. Chem. B , vol.112 , pp. 5961-5967
    • Lopez, C.F.1    Darst, R.K.2    Rossky, P.J.3
  • 66
    • 0029619776 scopus 로고
    • A Novel Basis for Capsid Stabilization by Antiviral Compounds
    • Phelps, D. K.; Post, C. B. A Novel Basis for Capsid Stabilization by Antiviral Compounds J. Mol. Biol. 1995, 254, 544-551
    • (1995) J. Mol. Biol. , vol.254 , pp. 544-551
    • Phelps, D.K.1    Post, C.B.2
  • 67
    • 0037703765 scopus 로고    scopus 로고
    • Compressibility of Cavities and Biological Water from Voronoi Volumes in Hydrated Proteins
    • Marchi, M. Compressibility of Cavities and Biological Water from Voronoi Volumes in Hydrated Proteins J. Phys. Chem. B 2003, 107, 6598-6602
    • (2003) J. Phys. Chem. B , vol.107 , pp. 6598-6602
    • Marchi, M.1
  • 70
    • 84944486544 scopus 로고
    • Prediction and Entropy of Printed English
    • Shannon, C. E. Prediction and Entropy of Printed English Bell Syst. Tech. J. 1951, 50-64
    • (1951) Bell Syst. Tech. J. , pp. 50-64
    • Shannon, C.E.1
  • 72
    • 0017706821 scopus 로고
    • Reversible Thermal Unfolding of Thermostable Phosphoglycerate Kinase. Thermostability Associated with Mean Zero Enthalpy Change
    • Nojima, H.; Ikai, A.; Oshima, T.; Noda, H. Reversible Thermal Unfolding of Thermostable Phosphoglycerate Kinase. Thermostability Associated with Mean Zero Enthalpy Change J. Mol. Biol. 1977, 116, 429-442
    • (1977) J. Mol. Biol. , vol.116 , pp. 429-442
    • Nojima, H.1    Ikai, A.2    Oshima, T.3    Noda, H.4
  • 74
    • 0035835077 scopus 로고    scopus 로고
    • Comparison of Protein Backbone Entropy and β -Sheet Stability: NMR-Derived Dynamics of Protein G B1 Domain Mutants
    • Stone, M. J.; Gupta, S.; Snyder, N.; Regan, L. Comparison of Protein Backbone Entropy and β -Sheet Stability: NMR-Derived Dynamics of Protein G B1 Domain Mutants J. Am. Chem. Soc. 2001, 123, 185-186
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 185-186
    • Stone, M.J.1    Gupta, S.2    Snyder, N.3    Regan, L.4
  • 75
    • 0034868445 scopus 로고    scopus 로고
    • NMR Relaxation Studies of the Role of Conformational Entropy in Protein Stability and Ligand Binding
    • Stone, M. J. NMR Relaxation Studies of the Role of Conformational Entropy in Protein Stability and Ligand Binding Acc. Chem. Res. 2001, 34, 379-388
    • (2001) Acc. Chem. Res. , vol.34 , pp. 379-388
    • Stone, M.J.1
  • 76
    • 77951143923 scopus 로고    scopus 로고
    • Temperature Dependence of the Flexibility of Thermophilic and Mesophilic Flavoenzymes of the Nitroreductase Fold
    • Merkley, E. D.; Parson, W. W.; Daggett, V. Temperature Dependence of the Flexibility of Thermophilic and Mesophilic Flavoenzymes of the Nitroreductase Fold Protein Eng. Des. Sel. 2010, 23, 327-336
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 327-336
    • Merkley, E.D.1    Parson, W.W.2    Daggett, V.3
  • 79
    • 0037193194 scopus 로고    scopus 로고
    • Microcalorimetric Study of Elongation Factor Tu from Thermus Thermophilus in Nucleotide-free, GDP and GTP Forms and in the Presence of Elongation Factor Ts
    • Sedlák, E.; Sprinzl, M.; Grillenbeck, N.; Antalk, M. Microcalorimetric Study of Elongation Factor Tu from Thermus Thermophilus in Nucleotide-free, GDP and GTP Forms and in the Presence of Elongation Factor Ts Biochim. Biophys. Acta 2002, 1596, 357-365
    • (2002) Biochim. Biophys. Acta , vol.1596 , pp. 357-365
    • Sedlák, E.1    Sprinzl, M.2    Grillenbeck, N.3    Antalk, M.4
  • 81
    • 77149131242 scopus 로고    scopus 로고
    • Comparing Geometric and Kinetic Cluster Algorithms for Molecular Simulation Data
    • Keller, B.; Daura, X.; Gunsteren, W. V. Comparing Geometric and Kinetic Cluster Algorithms for Molecular Simulation Data J. Chem. Phys. 2010, 132, 074110
    • (2010) J. Chem. Phys. , vol.132 , pp. 074110
    • Keller, B.1    Daura, X.2    Gunsteren, W.V.3
  • 82
    • 0000710672 scopus 로고    scopus 로고
    • Diffusive Dynamics of the Reaction Coordinate for Protein Folding Funnels
    • Socci, N. D.; Onuchic, J. N.; Wolynes, P. G. Diffusive Dynamics of the Reaction Coordinate for Protein Folding Funnels J. Chem. Phys. 1996, 104, 5860
    • (1996) J. Chem. Phys. , vol.104 , pp. 5860
    • Socci, N.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 83
    • 84865987083 scopus 로고    scopus 로고
    • Energy Landscape Analysis of Native Folding of the Prion Protein Yields the Diffusion Constant, Transition Path Time and Rates
    • Yu, H.; Gupta, A. N.; Liu, X.; Neupane, K.; Brigley, A. M.; Sosova, I.; Woodside, M. T. Energy Landscape Analysis of Native Folding of the Prion Protein Yields the Diffusion Constant, Transition Path Time and Rates Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 14452
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 14452
    • Yu, H.1    Gupta, A.N.2    Liu, X.3    Neupane, K.4    Brigley, A.M.5    Sosova, I.6    Woodside, M.T.7
  • 84
    • 33747623305 scopus 로고    scopus 로고
    • End-to-End Distance Distributions and Intrachain Diffusion Constants in Unfolded Polypeptide Chains Indicate Intramolecular Hydrogen Bond Formation
    • Möglich, A.; Joder, K.; Thomas, T. K. End-to-End Distance Distributions and Intrachain Diffusion Constants in Unfolded Polypeptide Chains Indicate Intramolecular Hydrogen Bond Formation Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 12394-12399
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 12394-12399
    • Möglich, A.1    Joder, K.2    Thomas, T.K.3
  • 85
    • 79959935915 scopus 로고    scopus 로고
    • Converting Structural Information into an Allosteric-Energy-Based Picture for Elongation Factor Tu Activation by the Ribosome
    • Adamczyk, A. J.; Warshel, A. Converting Structural Information into an Allosteric-Energy-Based Picture for Elongation Factor Tu Activation by the Ribosome Proc. Natl. Acad. Sci. U.S.A. 2011, 108, 9827-9832
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 9827-9832
    • Adamczyk, A.J.1    Warshel, A.2


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