메뉴 건너뛰기




Volumn 41, Issue , 2006, Pages 315-362

Effect of enzyme dynamics on catalytic activity

Author keywords

[No Author keywords available]

Indexed keywords


EID: 33749469496     PISSN: 00653160     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3160(06)41006-6     Document Type: Review
Times cited : (8)

References (65)
  • 1
    • 0000421878 scopus 로고
    • The nature of forces between large molecules of biological interest
    • Pauling L. The nature of forces between large molecules of biological interest. Nature 161 (1948) 707-709
    • (1948) Nature , vol.161 , pp. 707-709
    • Pauling, L.1
  • 2
    • 0016624901 scopus 로고
    • Binding energy, specificity, and enzymic catalysis: the Circe effect
    • Jencks W. Binding energy, specificity, and enzymic catalysis: the Circe effect. Adv. Enzym. 43 (1975) 219-310
    • (1975) Adv. Enzym. , vol.43 , pp. 219-310
    • Jencks, W.1
  • 3
    • 9744244983 scopus 로고    scopus 로고
    • Enzymatic transition states: thermodynamics, dynamics and analogue design
    • Schramm V. Enzymatic transition states: thermodynamics, dynamics and analogue design. Arch. Biochem. Biophys. 433 (2005) 13-26
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 13-26
    • Schramm, V.1
  • 4
    • 36749119688 scopus 로고
    • CO binding to heme proteins: a model for barrier height distributions and slow conformational changes
    • Agmon N., and Hopfield J. CO binding to heme proteins: a model for barrier height distributions and slow conformational changes. J. Chem. Phys. 79 (1983) 2042-2053
    • (1983) J. Chem. Phys. , vol.79 , pp. 2042-2053
    • Agmon, N.1    Hopfield, J.2
  • 6
    • 33748589503 scopus 로고    scopus 로고
    • Isotope effects and quantum tunneling in enzyme-catalyzed hydrogen transfer. Part I. The experimental basis
    • Romesberg F., and Schowen R. Isotope effects and quantum tunneling in enzyme-catalyzed hydrogen transfer. Part I. The experimental basis. Adv. Phys. Org. Chem. 39 (2004) 27-77
    • (2004) Adv. Phys. Org. Chem. , vol.39 , pp. 27-77
    • Romesberg, F.1    Schowen, R.2
  • 7
    • 33749492843 scopus 로고    scopus 로고
    • Probes for hydrogen tunneling and coupled motion in enzymatic systems
    • Schowen R., Klinman J., and Hynes J. (Eds), Wiley, Weinheim
    • Kohen A. Probes for hydrogen tunneling and coupled motion in enzymatic systems. In: Schowen R., Klinman J., and Hynes J. (Eds). Handbook of Hydrogen, Vol. 2: Biological Aspects of Hydrogen Transfer (2005), Wiley, Weinheim
    • (2005) Handbook of Hydrogen, Vol. 2: Biological Aspects of Hydrogen Transfer
    • Kohen, A.1
  • 9
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus R.A., and Sutin N. Electron transfers in chemistry and biology. Biochim. Biophys. Acta. 811 (1985) 265-322
    • (1985) Biochim. Biophys. Acta. , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 10
    • 36449000988 scopus 로고
    • Quantum rates for a double well coupled to a dissipative bath: accurate path integral results and comparison with approximate theories
    • Topaler M., and Makri N. Quantum rates for a double well coupled to a dissipative bath: accurate path integral results and comparison with approximate theories. J. Chem. Phys. 101 (1994) 7500-7519
    • (1994) J. Chem. Phys. , vol.101 , pp. 7500-7519
    • Topaler, M.1    Makri, N.2
  • 11
    • 0001378703 scopus 로고    scopus 로고
    • Quantum activated rates: an evolution operator approach
    • Schwartz S.D. Quantum activated rates: an evolution operator approach. J. Chem. Phys. 105 (1996) 6871-6879
    • (1996) J. Chem. Phys. , vol.105 , pp. 6871-6879
    • Schwartz, S.D.1
  • 12
    • 0347193736 scopus 로고
    • Reaction-rate theory: fifty years after Kramers
    • Hänggi P., Talkner P., and Borkovec M. Reaction-rate theory: fifty years after Kramers. Rev. Mod. Phys. 62 (1990) 251-341
    • (1990) Rev. Mod. Phys. , vol.62 , pp. 251-341
    • Hänggi, P.1    Talkner, P.2    Borkovec, M.3
  • 13
    • 0000458906 scopus 로고
    • Calculation of dynamic friction on intramolecular degrees of freedom
    • Straub J.E., Borkovec M., and Berne B.J. Calculation of dynamic friction on intramolecular degrees of freedom. J. Phys. Chem. 91 (1987) 4995-4998
    • (1987) J. Phys. Chem. , vol.91 , pp. 4995-4998
    • Straub, J.E.1    Borkovec, M.2    Berne, B.J.3
  • 14
    • 18844402460 scopus 로고
    • Nonlinear generalized Langevin equations
    • Zwanzig R. Nonlinear generalized Langevin equations. J. Stat. Phys. 9 (1973) 215-220
    • (1973) J. Stat. Phys. , vol.9 , pp. 215-220
    • Zwanzig, R.1
  • 15
    • 85056406805 scopus 로고    scopus 로고
    • Variational transition state theory and multidimensional tunneling for simple and complex reactions in the gas phase, solids, liquids, and enzymes
    • Kohen A., and Limbach H. (Eds), Marcel Dekker, New York
    • Truhlar D. Variational transition state theory and multidimensional tunneling for simple and complex reactions in the gas phase, solids, liquids, and enzymes. In: Kohen A., and Limbach H. (Eds). Isotope Effects in Chemistry and Biology (2005), Marcel Dekker, New York
    • (2005) Isotope Effects in Chemistry and Biology
    • Truhlar, D.1
  • 16
    • 0001784518 scopus 로고
    • Proton transfer reactions
    • Cooper A., Houben J., and Chien L. (Eds), Plenum, New York p. 293
    • Borgis D., and Hynes J.T. Proton transfer reactions. In: Cooper A., Houben J., and Chien L. (Eds). The Enzyme Catalysis Process (1989), Plenum, New York p. 293
    • (1989) The Enzyme Catalysis Process
    • Borgis, D.1    Hynes, J.T.2
  • 17
    • 5544259571 scopus 로고
    • Molecular dynamics simulation for a model nonadiabatic proton transfer reactions in solution
    • Borgis D., and Hynes J.T. Molecular dynamics simulation for a model nonadiabatic proton transfer reactions in solution. J. Chem. Phys. 94 (1991) 3619-3628
    • (1991) J. Chem. Phys. , vol.94 , pp. 3619-3628
    • Borgis, D.1    Hynes, J.T.2
  • 18
    • 11344269742 scopus 로고    scopus 로고
    • Kinetic isotope effects for nonadiabatic proton transfer reactions in a polar environment: 1 Interpretation of tunneling kinetic isotopic effects
    • Kiefer P., and Hynes J. Kinetic isotope effects for nonadiabatic proton transfer reactions in a polar environment: 1 Interpretation of tunneling kinetic isotopic effects. J. Phys. Chem. A. 108 (2004) 11793-11808
    • (2004) J. Phys. Chem. A. , vol.108 , pp. 11793-11808
    • Kiefer, P.1    Hynes, J.2
  • 19
    • 0002577737 scopus 로고
    • The theory of cryochemical reaction rates in the Leggett formalism
    • Benderskii V., Goldanskii V., and Makarov D. The theory of cryochemical reaction rates in the Leggett formalism. Chem. Phys. Lett. 171 (1990) 91-96
    • (1990) Chem. Phys. Lett. , vol.171 , pp. 91-96
    • Benderskii, V.1    Goldanskii, V.2    Makarov, D.3
  • 20
    • 11744322797 scopus 로고
    • Low-temperature chemical reactions. Effect of symmetrically coupled vibrations in collinear exchange reactions
    • Benderskii V., Goldanskii V., and Makarov D. Low-temperature chemical reactions. Effect of symmetrically coupled vibrations in collinear exchange reactions. Chem. Phys. 154 (1991) 407-424
    • (1991) Chem. Phys. , vol.154 , pp. 407-424
    • Benderskii, V.1    Goldanskii, V.2    Makarov, D.3
  • 22
    • 0347866726 scopus 로고    scopus 로고
    • Activated chemistry in the presence of a strongly symmetrically coupled vibration
    • Antoniou D., and Schwartz S.D. Activated chemistry in the presence of a strongly symmetrically coupled vibration. J. Chem. Phys. 108 (1998) 3620-3625
    • (1998) J. Chem. Phys. , vol.108 , pp. 3620-3625
    • Antoniou, D.1    Schwartz, S.D.2
  • 23
    • 7044254777 scopus 로고    scopus 로고
    • Transition path sampling study of classical rate-promoting vibrations
    • Antoniou D., Abolfath M.R., and Schwartz S.D. Transition path sampling study of classical rate-promoting vibrations. J. Chem. Phys. 121 (2004) 6442-6447
    • (2004) J. Chem. Phys. , vol.121 , pp. 6442-6447
    • Antoniou, D.1    Abolfath, M.R.2    Schwartz, S.D.3
  • 24
    • 0001150222 scopus 로고
    • Importance of nonseparability in quantum mechanical transition state theory
    • Miller W.H. Importance of nonseparability in quantum mechanical transition state theory. Acc. Chem. Res. 9 (1976) 306-312
    • (1976) Acc. Chem. Res. , vol.9 , pp. 306-312
    • Miller, W.H.1
  • 25
    • 33748274620 scopus 로고
    • Nonequilibrium solvation dynamics in solution reactions
    • van der Zwan G., and Hynes J.T. Nonequilibrium solvation dynamics in solution reactions. J. Chem. Phys. 78 (1983) 4174-4185
    • (1983) J. Chem. Phys. , vol.78 , pp. 4174-4185
    • van der Zwan, G.1    Hynes, J.T.2
  • 27
    • 0035249366 scopus 로고    scopus 로고
    • A computational method to discover the existence of promoting vibrations for chemical reactions in condensed phases
    • Caratzoulas S., and Schwartz S.D. A computational method to discover the existence of promoting vibrations for chemical reactions in condensed phases. J. Chem. Phys. 114 (2001) 2910-2918
    • (2001) J. Chem. Phys. , vol.114 , pp. 2910-2918
    • Caratzoulas, S.1    Schwartz, S.D.2
  • 28
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of protein
    • Zavodszky P., Kardos J., Svingor A., and Petsko G. Adjustment of conformational flexibility is a key event in the thermal adaptation of protein. Proc. Natl. Acad. Sci. USA 95 (1998) 7406-7411
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7406-7411
    • Zavodszky, P.1    Kardos, J.2    Svingor, A.3    Petsko, G.4
  • 29
    • 0033519723 scopus 로고    scopus 로고
    • Enzyme dynamics and hydrogen tunneling in a thermophilic alcohol dehydrogenase
    • Kohen A., Cannio R., Bartolucci S., and Klinman J. Enzyme dynamics and hydrogen tunneling in a thermophilic alcohol dehydrogenase. Nature 399 (1999) 496-499
    • (1999) Nature , vol.399 , pp. 496-499
    • Kohen, A.1    Cannio, R.2    Bartolucci, S.3    Klinman, J.4
  • 30
    • 0035859446 scopus 로고    scopus 로고
    • Internal enzyme motions as a source of catalytic activity: rate promoting vibrations and hydrogen tunneling
    • Antoniou D., and Schwartz S.D. Internal enzyme motions as a source of catalytic activity: rate promoting vibrations and hydrogen tunneling. J. Phys. Chem. B 105 (2001) 5553-5558
    • (2001) J. Phys. Chem. B , vol.105 , pp. 5553-5558
    • Antoniou, D.1    Schwartz, S.D.2
  • 31
    • 0037012441 scopus 로고    scopus 로고
    • Identification of a protein promoting vibration in the reaction catalyzed by horse liver alcohol dehydrogenase
    • Caratzoulas S., Mincer J.S., and Schwartz S.D. Identification of a protein promoting vibration in the reaction catalyzed by horse liver alcohol dehydrogenase. J. Am. Chem. Soc. 124 (2002) 3270-3276
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3270-3276
    • Caratzoulas, S.1    Mincer, J.S.2    Schwartz, S.D.3
  • 32
    • 0032817216 scopus 로고    scopus 로고
    • 2OH on the distance between reactants when catalyzed by horse liver alcohol dehydrogenase and 203 single point mutants
    • 2OH on the distance between reactants when catalyzed by horse liver alcohol dehydrogenase and 203 single point mutants. Bioorg. Chem. 27 (1999) 289-296
    • (1999) Bioorg. Chem. , vol.27 , pp. 289-296
    • Luo, J.1    Kahn, K.2    Bruice, T.C.3
  • 33
    • 0037104752 scopus 로고    scopus 로고
    • Promoting modes and demoting modes in enzyme-catalyzed proton transfer reactions: a study of models and realistic systems
    • Cui Q., and Karplus M. Promoting modes and demoting modes in enzyme-catalyzed proton transfer reactions: a study of models and realistic systems. J. Phys. Chem. B 106 (2002) 7927-7947
    • (2002) J. Phys. Chem. B , vol.106 , pp. 7927-7947
    • Cui, Q.1    Karplus, M.2
  • 34
    • 1042282260 scopus 로고    scopus 로고
    • Donor-acceptor distance and protein promoting vibration coupling to hydride transfer: a possible mechanism for kinetic control in isozymes of human lactate dehydrogenase
    • Basner J.E., and Schwartz S.D. Donor-acceptor distance and protein promoting vibration coupling to hydride transfer: a possible mechanism for kinetic control in isozymes of human lactate dehydrogenase. J. Phys. Chem. B 108 (2004) 444-451
    • (2004) J. Phys. Chem. B , vol.108 , pp. 444-451
    • Basner, J.E.1    Schwartz, S.D.2
  • 35
    • 10044273966 scopus 로고    scopus 로고
    • Promoting vibrations in human PNP: a molecular dynamics and hybrid quantum mechanical/molecular mechanical study
    • Núñez S., Antoniou D., Schramm V.L., and Schwartz S.D. Promoting vibrations in human PNP: a molecular dynamics and hybrid quantum mechanical/molecular mechanical study. J. Am. Chem. Soc. 126 (2004) 15720-15729
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15720-15729
    • Núñez, S.1    Antoniou, D.2    Schramm, V.L.3    Schwartz, S.D.4
  • 36
    • 1042299983 scopus 로고    scopus 로고
    • Transition state analysis for human and plasmodium falciparum purine nucleoside phosphorylases
    • Lewandowicz A., and Schramm V.L. Transition state analysis for human and plasmodium falciparum purine nucleoside phosphorylases. Biochemistry 43 (2004) 1458-1468
    • (2004) Biochemistry , vol.43 , pp. 1458-1468
    • Lewandowicz, A.1    Schramm, V.L.2
  • 37
    • 0041472499 scopus 로고    scopus 로고
    • Enzymatic transition state poise and transition state analogues
    • Schramm V.L. Enzymatic transition state poise and transition state analogues. Acc. Chem. Res. 36 (2003) 588-596
    • (2003) Acc. Chem. Res. , vol.36 , pp. 588-596
    • Schramm, V.L.1
  • 39
    • 12144251753 scopus 로고    scopus 로고
    • Coupling protein dynamics to reaction center electron density in enzymes: an electronic protein promoting vibration in human purine nucleoside phosphorylase
    • Mincer J.S., Núñez S., and Schwartz S.D. Coupling protein dynamics to reaction center electron density in enzymes: an electronic protein promoting vibration in human purine nucleoside phosphorylase. J. Theor. Comp. Chem. 3 (2004) 501-509
    • (2004) J. Theor. Comp. Chem. , vol.3 , pp. 501-509
    • Mincer, J.S.1    Núñez, S.2    Schwartz, S.D.3
  • 40
    • 0000729781 scopus 로고    scopus 로고
    • Transition path sampling and the calculation of rate constants
    • Dellago C., Bolhuis P., Csajka F., and Chandler D. Transition path sampling and the calculation of rate constants. J. Chem. Phys. 108 (1998) 1964-1977
    • (1998) J. Chem. Phys. , vol.108 , pp. 1964-1977
    • Dellago, C.1    Bolhuis, P.2    Csajka, F.3    Chandler, D.4
  • 42
    • 26444486352 scopus 로고    scopus 로고
    • How enzyme dynamics helps catalyze a reaction, in atomic detail: a transition path sampling study, J
    • Basner J.E., and Schwartz S.D. How enzyme dynamics helps catalyze a reaction, in atomic detail: a transition path sampling study, J. Am. Chem. Soc. 127 (2005) 13822-13831
    • (2005) Am. Chem. Soc. , vol.127 , pp. 13822-13831
    • Basner, J.E.1    Schwartz, S.D.2
  • 43
    • 1942437505 scopus 로고    scopus 로고
    • Orchestration of cooperative events in DNA synthesis and repair mechanism unraveled by transition path sampling of DNA polymerase β's closing
    • Radhakrishnan R., and Schlick T. Orchestration of cooperative events in DNA synthesis and repair mechanism unraveled by transition path sampling of DNA polymerase β's closing. Proc. Natl. Acad. Sci. USA 101 (2004) 5970-5975
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5970-5975
    • Radhakrishnan, R.1    Schlick, T.2
  • 46
    • 31544456090 scopus 로고    scopus 로고
    • Insight into catalytically relevant correlated motions in human purine nucleoside phosphorylase, J
    • Núñez S., Wing C., Antoniou D., Schramm V.L., and Schwartz S.D. Insight into catalytically relevant correlated motions in human purine nucleoside phosphorylase, J. Phys. Chem. A 110 (2006) 463-472
    • (2006) Phys. Chem. A , vol.110 , pp. 463-472
    • Núñez, S.1    Wing, C.2    Antoniou, D.3    Schramm, V.L.4    Schwartz, S.D.5
  • 49
    • 0035928796 scopus 로고    scopus 로고
    • Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism
    • Osborne M., Schnell J., Benkovic S., Dyson H., and Wright P. Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism. Biochemistry 40 (2001) 9846-9859
    • (2001) Biochemistry , vol.40 , pp. 9846-9859
    • Osborne, M.1    Schnell, J.2    Benkovic, S.3    Dyson, H.4    Wright, P.5
  • 50
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of E. coli dihydrofolate reductase: crystallographic evidence
    • Sawaya M., and Kraut J. Loop and subdomain movements in the mechanism of E. coli dihydrofolate reductase: crystallographic evidence. Biochemistry 36 (1997) 586-603
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.1    Kraut, J.2
  • 51
    • 0037159205 scopus 로고    scopus 로고
    • Coupling interactions of distal residues enhance dihydrofolate reductase catalysis: mutational effects on hydride ransfer rates
    • Rajagopalan P., Lutz S., and Benkovic S. Coupling interactions of distal residues enhance dihydrofolate reductase catalysis: mutational effects on hydride ransfer rates. Biochemistry 41 (2002) 12618-12628
    • (2002) Biochemistry , vol.41 , pp. 12618-12628
    • Rajagopalan, P.1    Lutz, S.2    Benkovic, S.3
  • 52
    • 0033955055 scopus 로고    scopus 로고
    • Protein dynamics in enzymatic catalysis: exploration of dihydrofolate reductase
    • Radkiewicz J., and Brooks C.L. Protein dynamics in enzymatic catalysis: exploration of dihydrofolate reductase. J. Am. Chem. Soc. 122 (2000) 225-231
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 225-231
    • Radkiewicz, J.1    Brooks, C.L.2
  • 53
    • 0344391945 scopus 로고    scopus 로고
    • Reaction-path energetics and kinetics of the hydride transfer reaction catalyzed by dihydrofolate reductase
    • Garcia-Viloca M., Truhlar D., and Gao J. Reaction-path energetics and kinetics of the hydride transfer reaction catalyzed by dihydrofolate reductase. Biochemistry 42 (2003) 13558-13575
    • (2003) Biochemistry , vol.42 , pp. 13558-13575
    • Garcia-Viloca, M.1    Truhlar, D.2    Gao, J.3
  • 54
    • 1842839777 scopus 로고    scopus 로고
    • Quantum-classical simulation methods for hydrogen transfer in enzymes: a case study of dihydrofolate reductase
    • Hammes-Schiffer S. Quantum-classical simulation methods for hydrogen transfer in enzymes: a case study of dihydrofolate reductase. Curr. Opin. Struct. Biol. 14 (2004) 192-201
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 192-201
    • Hammes-Schiffer, S.1
  • 55
    • 6344294816 scopus 로고    scopus 로고
    • The coupling of structural fluctuations to hydride transfer in dihydrofolate reductase
    • Thorpe I., and Brooks C. The coupling of structural fluctuations to hydride transfer in dihydrofolate reductase. Proteins: Struct. Funct. Bioinf. 57 (2004) 444-457
    • (2004) Proteins: Struct. Funct. Bioinf. , vol.57 , pp. 444-457
    • Thorpe, I.1    Brooks, C.2
  • 56
    • 4244134441 scopus 로고
    • Topography and dynamics of multidimensional interatomic potential surfaces
    • Berry R.S., and Kunz R. Topography and dynamics of multidimensional interatomic potential surfaces. Phys. Rev. Lett. 20 (1995) 3951-3954
    • (1995) Phys. Rev. Lett. , vol.20 , pp. 3951-3954
    • Berry, R.S.1    Kunz, R.2
  • 57
    • 0000370391 scopus 로고    scopus 로고
    • The topology of multidimensional potential energy surfaces: theory and application to peptide structure and kinetics
    • Becker O., and Karplus M. The topology of multidimensional potential energy surfaces: theory and application to peptide structure and kinetics. J. Chem. Phys. 106 (1997) 1495-1517
    • (1997) J. Chem. Phys. , vol.106 , pp. 1495-1517
    • Becker, O.1    Karplus, M.2
  • 58
    • 0031055306 scopus 로고    scopus 로고
    • Geometrical versus topological clustering: insight into conformation mapping
    • Becker O. Geometrical versus topological clustering: insight into conformation mapping. Proteins: Struct. Funct. Genet. 27 (1997) 213-226
    • (1997) Proteins: Struct. Funct. Genet. , vol.27 , pp. 213-226
    • Becker, O.1
  • 59
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H., Sligar S., and Wolynes P. The energy landscapes and motions of proteins. Science 254 (1991) 1598-1603
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.2    Wolynes, P.3
  • 60
    • 12944327750 scopus 로고    scopus 로고
    • Energy landscapes and solved protein-folding problems
    • Wolynes P. Energy landscapes and solved protein-folding problems. Phil. Trans. Roy. Soc. Lond. A 363 (2005) 453-464
    • (2005) Phil. Trans. Roy. Soc. Lond. A , vol.363 , pp. 453-464
    • Wolynes, P.1
  • 61
    • 0344951101 scopus 로고    scopus 로고
    • Interbasin motion approach to dynamics of conformationally constrained peptides
    • Despa F., Fernandez A., Berry R.S., Levy Y., and Jortner J. Interbasin motion approach to dynamics of conformationally constrained peptides. J. Chem. Phys. 118 (2003) 5673-5682
    • (2003) J. Chem. Phys. , vol.118 , pp. 5673-5682
    • Despa, F.1    Fernandez, A.2    Berry, R.S.3    Levy, Y.4    Jortner, J.5
  • 62
    • 36448998595 scopus 로고
    • Theoretical foundations of kinetic Monte Carlo simulations
    • Fichthorn K., and Weinberg W. Theoretical foundations of kinetic Monte Carlo simulations. J. Chem. Phys. 95 (1991) 1090-1096
    • (1991) J. Chem. Phys. , vol.95 , pp. 1090-1096
    • Fichthorn, K.1    Weinberg, W.2
  • 63
    • 0011690680 scopus 로고    scopus 로고
    • Methods for finding saddle points and minimum energy paths
    • Schwartz S.D. (Ed), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Henkelman G., Johannesson G., and Jonsson H. Methods for finding saddle points and minimum energy paths. In: Schwartz S.D. (Ed). Theoretical Methods in Condensed Phase Chemistry (2000), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • (2000) Theoretical Methods in Condensed Phase Chemistry
    • Henkelman, G.1    Johannesson, G.2    Jonsson, H.3
  • 64
    • 0344236155 scopus 로고    scopus 로고
    • The free energy landscape and dynamics of met-enkephalin
    • Evans D., and Wales D. The free energy landscape and dynamics of met-enkephalin. J. Chem. Phys. 119 (2003) 9947-9955
    • (2003) J. Chem. Phys. , vol.119 , pp. 9947-9955
    • Evans, D.1    Wales, D.2
  • 65
    • 17544365232 scopus 로고    scopus 로고
    • Finite-temperature string method for the study of rare events
    • Weinan E., Ren W., and Vanden-Eijnden E. Finite-temperature string method for the study of rare events. J. Phys. Chem. B 109 (2005) 6688-6693
    • (2005) J. Phys. Chem. B , vol.109 , pp. 6688-6693
    • Weinan, E.1    Ren, W.2    Vanden-Eijnden, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.