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Volumn 46, Issue 51, 2007, Pages 15076-15088

On the relationship between thermal stability and catalytic power of enzymes

Author keywords

[No Author keywords available]

Indexed keywords

BIOACTIVITY; CATALYST ACTIVITY; ELECTROSTATICS; PROTEIN FOLDING; THERMODYNAMIC STABILITY;

EID: 37349007321     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701732a     Document Type: Article
Times cited : (85)

References (58)
  • 3
    • 0029102089 scopus 로고
    • Dynamics of the Dihydrofolate-Reductase Folate Complex: Catalytic Sites and Regions Known to Undergo Conformational Change Exhibit Diverse Dynamical Features
    • Epstein, D. M., Benkovic, S. J., and Wright, P. E. (1995) Dynamics of the Dihydrofolate-Reductase Folate Complex: Catalytic Sites and Regions Known to Undergo Conformational Change Exhibit Diverse Dynamical Features, Biochemistry 34, 11037-11048.
    • (1995) Biochemistry , vol.34 , pp. 11037-11048
    • Epstein, D.M.1    Benkovic, S.J.2    Wright, P.E.3
  • 4
    • 3042660150 scopus 로고    scopus 로고
    • Structure, dynamics, and catalytic function of dihydrofolate reductase
    • Schnell, J. R., Dyson, H. J., and Wright, P. E. (2004) Structure, dynamics, and catalytic function of dihydrofolate reductase, Annu. Rev. Biophys. Biomol. Struct. 33, 119-140.
    • (2004) Annu. Rev. Biophys. Biomol. Struct , vol.33 , pp. 119-140
    • Schnell, J.R.1    Dyson, H.J.2    Wright, P.E.3
  • 5
    • 1842839777 scopus 로고    scopus 로고
    • Quantum-classical simulation methods for hydrogen transfer in enzymes: A case study of dihydrofolate reductase
    • Hammes-Schiffer, S. (2004) Quantum-classical simulation methods for hydrogen transfer in enzymes: A case study of dihydrofolate reductase, Curr. Opin. Struct. Biol. 14, 192-201.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 192-201
    • Hammes-Schiffer, S.1
  • 6
    • 33646935697 scopus 로고    scopus 로고
    • Dynamical contributions to enzyme catalysis: Critical tests of a popular hypothesis
    • Olsson, M. H. M., Parson, W. W., and Warshel, A. (2006) Dynamical contributions to enzyme catalysis: Critical tests of a popular hypothesis, Chem. Rev. 106, 1737-1756.
    • (2006) Chem. Rev , vol.106 , pp. 1737-1756
    • Olsson, M.H.M.1    Parson, W.W.2    Warshel, A.3
  • 7
    • 32244432145 scopus 로고    scopus 로고
    • Effects of a distal mutation on active site chemistry
    • Wang, L., Tharp, S., Selzer, T., Benkovic, S. J., and Kohen, A. (2006) Effects of a distal mutation on active site chemistry, Biochemistry 45, 1383-1392.
    • (2006) Biochemistry , vol.45 , pp. 1383-1392
    • Wang, L.1    Tharp, S.2    Selzer, T.3    Benkovic, S.J.4    Kohen, A.5
  • 8
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • Zavodszky, P., Kardos, J., Svingor, A., and Petsko, G. A. (1998) Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins, Proc. Natl. Acad. Sci. U.S.A. 95, 7406-7411.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 7406-7411
    • Zavodszky, P.1    Kardos, J.2    Svingor, A.3    Petsko, G.A.4
  • 9
    • 0033519504 scopus 로고    scopus 로고
    • Quantum enzymology: Tunnel vision
    • Ringe, D., and Petsko, G. A. (1999) Quantum enzymology: Tunnel vision, Nature 399, 417-418.
    • (1999) Nature , vol.399 , pp. 417-418
    • Ringe, D.1    Petsko, G.A.2
  • 10
    • 0033519723 scopus 로고    scopus 로고
    • Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase
    • Kohen, A., Cannio, R., Bartolucci, S., and Klinman, J. P. (1999) Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase, Nature 399, 496-499.
    • (1999) Nature , vol.399 , pp. 496-499
    • Kohen, A.1    Cannio, R.2    Bartolucci, S.3    Klinman, J.P.4
  • 11
    • 0034327617 scopus 로고    scopus 로고
    • Protein flexibility correlates with degree of hydrogen tunneling in thermophilic and mesophilic alcohol dehydrogenases
    • Kohen, A., and Klinman, J. P. (2000) Protein flexibility correlates with degree of hydrogen tunneling in thermophilic and mesophilic alcohol dehydrogenases, J. Am. Chem. Soc. 122, 10738-10739.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 10738-10739
    • Kohen, A.1    Klinman, J.P.2
  • 12
    • 0035707451 scopus 로고    scopus 로고
    • Dynamics of biochemical and biophysical reactions: Insight from computer simulations
    • Warshel, A., and Parson, W. W. (2001) Dynamics of biochemical and biophysical reactions: Insight from computer simulations, Q. Rev. Biophys. 34, 563-679.
    • (2001) Q. Rev. Biophys , vol.34 , pp. 563-679
    • Warshel, A.1    Parson, W.W.2
  • 13
    • 0041761262 scopus 로고    scopus 로고
    • Hydride transfer during catalysis by dihydrofolate reductase from Thermotoga maritima
    • Maglia, G., Javed, M. H., and Allemann, R. K. (2003) Hydride transfer during catalysis by dihydrofolate reductase from Thermotoga maritima, Biochem. J. 374, 529-535.
    • (2003) Biochem. J , vol.374 , pp. 529-535
    • Maglia, G.1    Javed, M.H.2    Allemann, R.K.3
  • 14
    • 0025182490 scopus 로고
    • Extremely Thermostable D-Glyceraldehyde-3-Phosphate Dehydrogenase from the Eubacterium Thermotoga maritima
    • Wrba, A., Schweiger, A., Schultes, V., Jaenicke, R., and Zavodszky, P. (1990) Extremely Thermostable D-Glyceraldehyde-3-Phosphate Dehydrogenase from the Eubacterium Thermotoga maritima, Biochemistry 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
  • 16
    • 0000230329 scopus 로고
    • Energetics of Enzyme Catalysis
    • Warshel, A. (1978) Energetics of Enzyme Catalysis, Proc. Natl. Acad. Sci. U.S.A. 75, 5250-5254.
    • (1978) Proc. Natl. Acad. Sci. U.S.A , vol.75 , pp. 5250-5254
    • Warshel, A.1
  • 18
    • 0016610491 scopus 로고
    • Computer-Simulation of Protein Folding
    • Levitt, M., and Warshel, A. (1975) Computer-Simulation of Protein Folding, Nature 253, 694-698.
    • (1975) Nature , vol.253 , pp. 694-698
    • Levitt, M.1    Warshel, A.2
  • 19
    • 0023449962 scopus 로고
    • Spin-Glasses and the Statistical-Mechanics of Protein Folding
    • Bryngelson, J. D., and Wolynes, P. G. (1987) Spin-Glasses and the Statistical-Mechanics of Protein Folding, Proc. Natl. Acad. Sci. U.S.A. 84, 7524-7528.
    • (1987) Proc. Natl. Acad. Sci. U.S.A , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 20
    • 0026519315 scopus 로고
    • A Lattice Model for Protein-Structure Prediction at Low Resolution
    • Hinds, D. A., and Levitt, M. (1992) A Lattice Model for Protein-Structure Prediction at Low Resolution, Proc. Natl. Acad. Sci. U.S.A. 89, 2536-2540.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 2536-2540
    • Hinds, D.A.1    Levitt, M.2
  • 21
    • 0029670994 scopus 로고    scopus 로고
    • Conserved residues and the mechanism of protein folding
    • Shakhnovich, E., Abkevich, V., and Ptitsyn, O. (1996) Conserved residues and the mechanism of protein folding, Nature 379, 96-98.
    • (1996) Nature , vol.379 , pp. 96-98
    • Shakhnovich, E.1    Abkevich, V.2    Ptitsyn, O.3
  • 22
    • 0025370815 scopus 로고
    • Dominant Forces in Protein Folding
    • Dill, K. A. (1990) Dominant Forces in Protein Folding, Biochemistry 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 23
    • 0030018099 scopus 로고    scopus 로고
    • Folding simulations and computer redesign of protein A three-helix bundle motifs
    • Olszewski, K. A., Kolinski, A., and Skolnick, J. (1996) Folding simulations and computer redesign of protein A three-helix bundle motifs, Proteins: Struct., Funct., Genet. 25, 286-299.
    • (1996) Proteins: Struct., Funct., Genet , vol.25 , pp. 286-299
    • Olszewski, K.A.1    Kolinski, A.2    Skolnick, J.3
  • 24
    • 22844456329 scopus 로고    scopus 로고
    • Using simplified protein representation as a reference potential for all-atom calculations of folding free energy
    • Fan, Z. Z., Hwang, J. K., and Warshel, A. (1999) Using simplified protein representation as a reference potential for all-atom calculations of folding free energy, Theor. Chem. Acc. 103, 77-80.
    • (1999) Theor. Chem. Acc , vol.103 , pp. 77-80
    • Fan, Z.Z.1    Hwang, J.K.2    Warshel, A.3
  • 25
    • 0000728542 scopus 로고
    • Microscopic and Semimicroscopic Calculations of Electrostatic Energies in Proteins by the Polaris and Enzymix Programs
    • Lee, F. S., Chu, Z. T., and Warshel, A. (1993) Microscopic and Semimicroscopic Calculations of Electrostatic Energies in Proteins by the Polaris and Enzymix Programs, J. Comput. Chem. 14, 161-185.
    • (1993) J. Comput. Chem , vol.14 , pp. 161-185
    • Lee, F.S.1    Chu, Z.T.2    Warshel, A.3
  • 26
    • 37349125262 scopus 로고    scopus 로고
    • Chu, Z. T., Villa, J., Strajbl, M., Schutz, C. N., Shurki, A., and Warshel, A. (2006) MOLARIS, version α9.06, University of Southern California, Los Angeles.
    • Chu, Z. T., Villa, J., Strajbl, M., Schutz, C. N., Shurki, A., and Warshel, A. (2006) MOLARIS, version α9.06, University of Southern California, Los Angeles.
  • 27
    • 37349057884 scopus 로고    scopus 로고
    • manuscript in preparation
    • Messer, B., Roca, M., and Warshel, A. (2007) (manuscript in preparation).
    • (2007)
    • Messer, B.1    Roca, M.2    Warshel, A.3
  • 29
    • 34247596467 scopus 로고    scopus 로고
    • Electrostatic contributions to protein stability and folding energy
    • Roca, M., Messer, B., and Warshel, A. (2007) Electrostatic contributions to protein stability and folding energy, FEBS Lett. 581, 2065-2071.
    • (2007) FEBS Lett , vol.581 , pp. 2065-2071
    • Roca, M.1    Messer, B.2    Warshel, A.3
  • 30
    • 0021480222 scopus 로고
    • Macroscopic Models for Studies of Electrostatic Interactions in Proteins: Limitations and Applicability
    • Warshel, A., Russell, S. T., and Churg, A. K. (1984) Macroscopic Models for Studies of Electrostatic Interactions in Proteins: Limitations and Applicability, Proc. Natl. Acad. Sci. U.S.A. 81, 4785-4789.
    • (1984) Proc. Natl. Acad. Sci. U.S.A , vol.81 , pp. 4785-4789
    • Warshel, A.1    Russell, S.T.2    Churg, A.K.3
  • 31
    • 0021476470 scopus 로고
    • Calculations of Electrostatic Interactions in Biological Systems and in Solutions
    • Warshel, A., and Russell, S. T. (1984) Calculations of Electrostatic Interactions in Biological Systems and in Solutions, Q. Rev. Biophys. 17, 283-422.
    • (1984) Q. Rev. Biophys , vol.17 , pp. 283-422
    • Warshel, A.1    Russell, S.T.2
  • 32
    • 0034652206 scopus 로고    scopus 로고
    • Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism
    • Fersht, A. R. (2000) Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism, Proc. Natl. Acad. Sci. U.S.A. 97, 1525-1529.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 1525-1529
    • Fersht, A.R.1
  • 33
    • 20444389830 scopus 로고    scopus 로고
    • Structural Genomics of Thermotoga maritima proteins shows that contact order is a major determinant of protein thermostability
    • Robinson-Rechavi, M., and Godzik, A. (2005) Structural Genomics of Thermotoga maritima proteins shows that contact order is a major determinant of protein thermostability, Structure 13, 857-860.
    • (2005) Structure , vol.13 , pp. 857-860
    • Robinson-Rechavi, M.1    Godzik, A.2
  • 34
    • 0037058992 scopus 로고    scopus 로고
    • Probing the folding free energy landscape of the src-SH3 protein domain
    • Shea, J. E., Onuchic, J. N., and Brooks, C. L. (2002) Probing the folding free energy landscape of the src-SH3 protein domain, Proc. Natl. Acad. Sci. U.S.A. 99, 16064-16068.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 16064-16068
    • Shea, J.E.1    Onuchic, J.N.2    Brooks, C.L.3
  • 35
    • 0007836334 scopus 로고
    • Dynamics of Reactions in Polar-Solvents: Semi-Classical Trajectory Studies of Electron-Transfer and Proton-Transfer Reactions
    • Warshel, A. (1982) Dynamics of Reactions in Polar-Solvents: Semi-Classical Trajectory Studies of Electron-Transfer and Proton-Transfer Reactions, J. Phys. Chem. 86, 2218-2224.
    • (1982) J. Phys. Chem , vol.86 , pp. 2218-2224
    • Warshel, A.1
  • 36
    • 33845282688 scopus 로고
    • Microscopic Examination of Free-Energy Relationships for Electron-Transfer in Polar-Solvents
    • Hwang, J. K., and Warshel, A. (1987) Microscopic Examination of Free-Energy Relationships for Electron-Transfer in Polar-Solvents, J. Am. Chem. Soc. 109, 715-720.
    • (1987) J. Am. Chem. Soc , vol.109 , pp. 715-720
    • Hwang, J.K.1    Warshel, A.2
  • 37
    • 4243810035 scopus 로고
    • Simulation of Enzyme-Reactions Using Valence-Bond Force-Fields and Other Hybrid Quantum-Classical Approaches
    • Aqvist, J., and Warshel, A. (1993) Simulation of Enzyme-Reactions Using Valence-Bond Force-Fields and Other Hybrid Quantum-Classical Approaches, Chem. Rev. 93, 2523-2544.
    • (1993) Chem. Rev , vol.93 , pp. 2523-2544
    • Aqvist, J.1    Warshel, A.2
  • 38
    • 27544492154 scopus 로고    scopus 로고
    • Through the channel and around the channel: Validating and comparing microscopic approaches for the evaluation of free energy profiles for ion penetration through ion channels
    • Kato, M., and Warshel, A. (2005) Through the channel and around the channel: Validating and comparing microscopic approaches for the evaluation of free energy profiles for ion penetration through ion channels, J. Phys. Chem. B 109, 19516-19522.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 19516-19522
    • Kato, M.1    Warshel, A.2
  • 39
    • 84962477148 scopus 로고    scopus 로고
    • Structure/function correlations of proteins using MM, QM/MM, and related approaches: Methods, concepts, pitfalls, and current progress
    • Shurki, A., and Warshel, A. (2003) Structure/function correlations of proteins using MM, QM/MM, and related approaches: Methods, concepts, pitfalls, and current progress, Adv. Protein Chem. 66, 249-313.
    • (2003) Adv. Protein Chem , vol.66 , pp. 249-313
    • Shurki, A.1    Warshel, A.2
  • 40
    • 0344391945 scopus 로고    scopus 로고
    • Reaction-path energetics and kinetics of the hydride transfer reaction catalyzed by dihydrofolate reductase
    • Garcia-Viloca, M., Truhlar, D. G., and Gao, J. L. (2003) Reaction-path energetics and kinetics of the hydride transfer reaction catalyzed by dihydrofolate reductase, Biochemistry 42, 13558-13575.
    • (2003) Biochemistry , vol.42 , pp. 13558-13575
    • Garcia-Viloca, M.1    Truhlar, D.G.2    Gao, J.L.3
  • 41
    • 25144458498 scopus 로고    scopus 로고
    • Conformational substates modulate hydride transfer in dihydrofolate reductase
    • Thorpe, I. F., and Brooks, C. L. (2005) Conformational substates modulate hydride transfer in dihydrofolate reductase, J. Am. Chem. Soc. 127, 12997-13006.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 12997-13006
    • Thorpe, I.F.1    Brooks, C.L.2
  • 42
    • 0033616094 scopus 로고    scopus 로고
    • Catalytic mechanism of dihydrofolate reductase enzyme. A combined quantum-mechanical/molecular- mechanical characterization of transition state structure for the hydride transfer step
    • Castillo, R., Andres, J., and Moliner, V. (1999) Catalytic mechanism of dihydrofolate reductase enzyme. A combined quantum-mechanical/molecular- mechanical characterization of transition state structure for the hydride transfer step, J. Am. Chem. Soc. 121, 12140-12147.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 12140-12147
    • Castillo, R.1    Andres, J.2    Moliner, V.3
  • 43
    • 0242391099 scopus 로고    scopus 로고
    • Cummins, P. L., and Gready, J. E. (2003) Computational methods for the study of enzymic reaction mechanisms. II. An overlapping mechanically embedded method for hybrid semi-empirical-QM/MM calculations, THEOCHEM 632, 247-257.
    • Cummins, P. L., and Gready, J. E. (2003) Computational methods for the study of enzymic reaction mechanisms. II. An overlapping mechanically embedded method for hybrid semi-empirical-QM/MM calculations, THEOCHEM 632, 247-257.
  • 44
    • 34249104188 scopus 로고    scopus 로고
    • The Catalytic Effect of Dihydrofolate Reductase and Its Mutants Is Determined by Reorganization Energies
    • Liu, H., and Warshel, A. (2007) The Catalytic Effect of Dihydrofolate Reductase and Its Mutants Is Determined by Reorganization Energies, Biochemistry 46, 6011-6025.
    • (2007) Biochemistry , vol.46 , pp. 6011-6025
    • Liu, H.1    Warshel, A.2
  • 45
    • 0041600218 scopus 로고
    • Simulation of Free-Energy Relationships and Dynamics of Sn2 Reactions in Aqueous-Solution
    • Hwang, J. K., King, G., Creighton, S., and Warshel, A. (1988) Simulation of Free-Energy Relationships and Dynamics of Sn2 Reactions in Aqueous-Solution, J. Am. Chem. Soc. 110, 5297-5311.
    • (1988) J. Am. Chem. Soc , vol.110 , pp. 5297-5311
    • Hwang, J.K.1    King, G.2    Creighton, S.3    Warshel, A.4
  • 46
    • 36549094414 scopus 로고
    • A Surface Constrained All-Atom Solvent Model for Effective Simulations of Polar Solutions
    • King, G., and Warshel, A. (1989) A Surface Constrained All-Atom Solvent Model for Effective Simulations of Polar Solutions, J. Chem. Phys. 91, 3647-3661.
    • (1989) J. Chem. Phys , vol.91 , pp. 3647-3661
    • King, G.1    Warshel, A.2
  • 47
    • 0000115003 scopus 로고
    • A Local Reaction Field Method for Fast Evaluation of Long-Range Electrostatic Interactions in Molecular Simulations
    • Lee, F. S., and Warshel, A. (1992) A Local Reaction Field Method for Fast Evaluation of Long-Range Electrostatic Interactions in Molecular Simulations, J. Chem. Phys. 97, 3100-3107.
    • (1992) J. Chem. Phys , vol.97 , pp. 3100-3107
    • Lee, F.S.1    Warshel, A.2
  • 48
    • 0034737320 scopus 로고    scopus 로고
    • The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability
    • Dams, T., Auerbach, G., Bader, G., Jacob, U., Ploom, T., Huber, R., and Jaenicke, R. (2000) The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability, J. Mol. Biol. 297, 659-672.
    • (2000) J. Mol. Biol , vol.297 , pp. 659-672
    • Dams, T.1    Auerbach, G.2    Bader, G.3    Jacob, U.4    Ploom, T.5    Huber, R.6    Jaenicke, R.7
  • 49
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • Sawaya, M. R., and Kraut, J. (1997) Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence, Biochemistry 36, 586-603.
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 50
    • 0033551438 scopus 로고    scopus 로고
    • Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima
    • Dams, T., and Jaenicke, R. (1999) Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima, Biochemistry 38, 9169-9178.
    • (1999) Biochemistry , vol.38 , pp. 9169-9178
    • Dams, T.1    Jaenicke, R.2
  • 51
    • 0034622508 scopus 로고    scopus 로고
    • Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: Thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles
    • Ionescu, R. M., Smith, V. F., O'Neill, J. C., and Matthews, C. R. (2000) Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: Thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles, Biochemistry 39, 9540-9550.
    • (2000) Biochemistry , vol.39 , pp. 9540-9550
    • Ionescu, R.M.1    Smith, V.F.2    O'Neill, J.C.3    Matthews, C.R.4
  • 52
    • 0031808658 scopus 로고    scopus 로고
    • Stretching exercises: Flexibility in dihydrofolate reductase catalysis
    • Miller, G. P., and Benkovic, S. J. (1998) Stretching exercises: Flexibility in dihydrofolate reductase catalysis, Chem. Biol. 5, R105-R113.
    • (1998) Chem. Biol , vol.5
    • Miller, G.P.1    Benkovic, S.J.2
  • 53
    • 0024445808 scopus 로고
    • Dispersed Polaron Simulations of Electron Transfer in Photosynthetic Reaction Centers
    • Warshel, A., Chu, Z. T., and Parson, W. W. (1989) Dispersed Polaron Simulations of Electron Transfer in Photosynthetic Reaction Centers, Science 246, 112-116.
    • (1989) Science , vol.246 , pp. 112-116
    • Warshel, A.1    Chu, Z.T.2    Parson, W.W.3
  • 54
    • 0001604008 scopus 로고
    • The Dynamics of the Primary Event in Rhodopsins Revisited
    • Warshel, A., Chu, Z. T., and Hwang, J. K. (1991) The Dynamics of the Primary Event in Rhodopsins Revisited, Chem. Phys. 158, 303-314.
    • (1991) Chem. Phys , vol.158 , pp. 303-314
    • Warshel, A.1    Chu, Z.T.2    Hwang, J.K.3
  • 56
    • 23844458318 scopus 로고    scopus 로고
    • Increased flexibility as a strategy for cold adaptation: A comparative molecular dynamics study of cold- and warm-active uracil DNA glycosylase
    • Olufsen, M., Smalas, A. O., Moe, E., and Brandsdal, B. O. (2005) Increased flexibility as a strategy for cold adaptation: A comparative molecular dynamics study of cold- and warm-active uracil DNA glycosylase, J. Biol. Chem. 280, 18042-18048.
    • (2005) J. Biol. Chem , vol.280 , pp. 18042-18048
    • Olufsen, M.1    Smalas, A.O.2    Moe, E.3    Brandsdal, B.O.4
  • 57
    • 33747756504 scopus 로고    scopus 로고
    • Flexibility and enzymatic cold-adaptation: A comparative molecular dynamics investigation of the elastase family
    • Papaleo, E., Riccardi, L., Villa, C., Fantucci, P., and De Gioia, L. (2006) Flexibility and enzymatic cold-adaptation: A comparative molecular dynamics investigation of the elastase family, Biochim. Biophys. Acta 1764, 1397-1406.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1397-1406
    • Papaleo, E.1    Riccardi, L.2    Villa, C.3    Fantucci, P.4    De Gioia, L.5


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