메뉴 건너뛰기




Volumn 327, Issue 2, 2003, Pages 549-560

Importance of substrate and cofactor polarization in the active site of dihydrofolate reductase

Author keywords

Dihydrofolate reductase; Enzyme catalysis; Polarization effect; Substrate enzyme binding

Indexed keywords

DIHYDROFOLATE REDUCTASE; GLUTAMIC ACID; PTERIN;

EID: 0037459224     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00123-2     Document Type: Article
Times cited : (83)

References (67)
  • 2
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Eschericia coli
    • Fierke C.A., Johnson K.A., Benkovic S.J. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Eschericia coli. Biochemistry. 26:1987;4085-4092.
    • (1987) Biochemistry , vol.26 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 3
    • 0023748631 scopus 로고
    • Mechanism of the reaction catalyzed by dihydrofolate reductase from Esterichia coli: PH and deuterium isotope effects with NADPH as the variable substrate
    • Morrison J.F., Stone S.R. Mechanism of the reaction catalyzed by dihydrofolate reductase from Esterichia coli: pH and deuterium isotope effects with NADPH as the variable substrate. Biochemistry. 27:1988;5499-5506.
    • (1988) Biochemistry , vol.27 , pp. 5499-5506
    • Morrison, J.F.1    Stone, S.R.2
  • 4
    • 37049083821 scopus 로고
    • Prediction of selective bioreductive antitumor, antifolate activity using a modified ab initio method for calculating enzyme-inhibitor interaction energies
    • Reynolds C.A., Richards W.G., Goodford P.J. Prediction of selective bioreductive antitumor, antifolate activity using a modified ab initio method for calculating enzyme-inhibitor interaction energies. J. Chem. Soc., Perkin Trans. 2:1988;551-556.
    • (1988) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 551-556
    • Reynolds, C.A.1    Richards, W.G.2    Goodford, P.J.3
  • 6
    • 0024498518 scopus 로고
    • Dihydrofolate reductase: Multiple conformations and alternative modes of substrate binding
    • Birdsall B., Feeney J., Tendler S.J.B., Hammond S.J., Roberts G.C.K. Dihydrofolate reductase: multiple conformations and alternative modes of substrate binding. Biochemistry. 28:1989;2297-2305.
    • (1989) Biochemistry , vol.28 , pp. 2297-2305
    • Birdsall, B.1    Feeney, J.2    Tendler, S.J.B.3    Hammond, S.J.4    Roberts, G.C.K.5
  • 7
    • 0023759007 scopus 로고
    • The hypothetical active site lattice. An approach to modelling active sites from data on inhibitor molecules
    • Doweyko A.M. The hypothetical active site lattice. An approach to modelling active sites from data on inhibitor molecules. J. Med. Chem. 31:1988;1396-1406.
    • (1988) J. Med. Chem. , vol.31 , pp. 1396-1406
    • Doweyko, A.M.1
  • 8
    • 0012346957 scopus 로고
    • Inhibitor and substrate binding in dihydrofolate reductase. A theoretical approach
    • (Modell. Mol. Struct. Prop.)
    • Solmajer T., Hodoscek M. Inhibitor and substrate binding in dihydrofolate reductase. A theoretical approach. Stud. Phys. Theor. Chem. 71:1990;567-574. (Modell. Mol. Struct. Prop.).
    • (1990) Stud. Phys. Theor. Chem. , vol.71 , pp. 567-574
    • Solmajer, T.1    Hodoscek, M.2
  • 9
    • 0033226561 scopus 로고    scopus 로고
    • Towards understanding the mechanics of molecular recognition by computer simulations of ligand-protein interactions
    • Verkhivker G.M., Rejto P.A., Bouzida D., Arthurs S., Colson A.B., Freer S.T., et al. Towards understanding the mechanics of molecular recognition by computer simulations of ligand-protein interactions. J. Mol. Recognit. 12:1999;371-389.
    • (1999) J. Mol. Recognit. , vol.12 , pp. 371-389
    • Verkhivker, G.M.1    Rejto, P.A.2    Bouzida, D.3    Arthurs, S.4    Colson, A.B.5    Freer, S.T.6
  • 10
    • 0026570384 scopus 로고
    • Ab initio studies of aromatic-aromatic and aromatic-polar interactions in the binding of substrate and inhibitor to dihydrofolate reductase
    • Sapse A.M., Schweitzer B.S., Dicker A.P., Bertino J.R., Frecer V. Ab initio studies of aromatic-aromatic and aromatic-polar interactions in the binding of substrate and inhibitor to dihydrofolate reductase. Int. J. Pept. Protein Res. 39:1992;18-23.
    • (1992) Int. J. Pept. Protein Res. , vol.39 , pp. 18-23
    • Sapse, A.M.1    Schweitzer, B.S.2    Dicker, A.P.3    Bertino, J.R.4    Frecer, V.5
  • 11
    • 0012312172 scopus 로고
    • Prediction of relative binding constants of cofactors and designed ligands to dihydrofolate reductase by computer simulation
    • Cummins P.L., Gready J.E. Prediction of relative binding constants of cofactors and designed ligands to dihydrofolate reductase by computer simulation. Pteridines. 3:1992;137-139.
    • (1992) Pteridines , vol.3 , pp. 137-139
    • Cummins, P.L.1    Gready, J.E.2
  • 12
    • 0027474782 scopus 로고
    • Novel mechanism-based substrates of dihydrofolate reductase and the thermodynamics of ligand binding: A comparison of theory and experiment for 8-methylpterin and 6,8-dimethylpterin
    • Cummins P.L., Gready J.E. Novel mechanism-based substrates of dihydrofolate reductase and the thermodynamics of ligand binding: a comparison of theory and experiment for 8-methylpterin and 6,8-dimethylpterin. Proteins: Struct. Funct. Genet. 15:1993;426-435.
    • (1993) Proteins: Struct. Funct. Genet. , vol.15 , pp. 426-435
    • Cummins, P.L.1    Gready, J.E.2
  • 13
    • 0027443717 scopus 로고
    • Voronoi modeling: The binding of triazines and pyrimidines to L. casei dihydrofolate reductase
    • Bradley M.P., Crippen G.M. Voronoi modeling: the binding of triazines and pyrimidines to L. casei dihydrofolate reductase. J. Med. Chem. 36:1993;3171-3177.
    • (1993) J. Med. Chem. , vol.36 , pp. 3171-3177
    • Bradley, M.P.1    Crippen, G.M.2
  • 14
    • 0027673314 scopus 로고
    • Computer-aided drug design: A free-energy perturbation study on the binding of methyl-substituted pterins and N5-deazapterins to dihydrofolate reductase
    • Cummins P.L., Gready J.E. Computer-aided drug design: a free-energy perturbation study on the binding of methyl-substituted pterins and N5-deazapterins to dihydrofolate reductase. J. Comput.-Aided Mol. Des. 7:1993;535-555.
    • (1993) J. Comput.-Aided Mol. Des. , vol.7 , pp. 535-555
    • Cummins, P.L.1    Gready, J.E.2
  • 15
    • 0027613969 scopus 로고
    • An approximate but efficient method to calculate free energy trends by computer simulation: Application to dihydrofolate reductase-inhibitor complexes
    • Gerber P.R., Mark A.E., van Gunsteren W.F. An approximate but efficient method to calculate free energy trends by computer simulation: application to dihydrofolate reductase-inhibitor complexes. J. Comput.-Aided Mol. Des. 7:1993;305-323.
    • (1993) J. Comput.-Aided Mol. Des. , vol.7 , pp. 305-323
    • Gerber, P.R.1    Mark, A.E.2    Van Gunsteren, W.F.3
  • 16
    • 0001173794 scopus 로고
    • The influence of starting coordinates in free energy simulations of ligand binding to dihydrofolate reductase
    • Cummins P.L., Gready J.E. The influence of starting coordinates in free energy simulations of ligand binding to dihydrofolate reductase. Mol. Simul. 15:1995;155-175.
    • (1995) Mol. Simul. , vol.15 , pp. 155-175
    • Cummins, P.L.1    Gready, J.E.2
  • 17
    • 0031023843 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the docking of substituted N5-deazapterins to dihydrofolate reductase
    • Gorse A.-D., Gready J.E. Molecular dynamics simulations of the docking of substituted N5-deazapterins to dihydrofolate reductase. Protein Eng. 10:1997;23-30.
    • (1997) Protein Eng. , vol.10 , pp. 23-30
    • Gorse, A.-D.1    Gready, J.E.2
  • 18
    • 0032014129 scopus 로고    scopus 로고
    • Computation of affinity and selectivity: Binding of 2,4-diaminopteridine and 2,4-diaminoquinazoline inhibitors to dihydrofolate reductases
    • Marelius J., Graffner-Nordberg M., Hansson T., Hallberg A., Aqvist J. Computation of affinity and selectivity: binding of 2,4-diaminopteridine and 2,4-diaminoquinazoline inhibitors to dihydrofolate reductases. J. Comput.-Aided Mol. Des. 12:1998;119-131.
    • (1998) J. Comput.-Aided Mol. Des. , vol.12 , pp. 119-131
    • Marelius, J.1    Graffner-Nordberg, M.2    Hansson, T.3    Hallberg, A.4    Aqvist, J.5
  • 19
    • 0032111506 scopus 로고    scopus 로고
    • Identification and energetic ranking of possible docking sites for pterin on dihydrofolate reductase
    • Bliznyuk A.A., Gready J.E. Identification and energetic ranking of possible docking sites for pterin on dihydrofolate reductase. J. Comput.-Aided Mol. Des. 12:1998;325-333.
    • (1998) J. Comput.-Aided Mol. Des. , vol.12 , pp. 325-333
    • Bliznyuk, A.A.1    Gready, J.E.2
  • 20
    • 0034687230 scopus 로고    scopus 로고
    • Computational predictions of binding affinities to dihydrofolate reductase: Synthesis and biological evaluation of methotrexate analogues
    • Graffner-Nordberg M., Marelius J., Ohlsson S., Persson S., Swedberg G., Andersson P., et al. Computational predictions of binding affinities to dihydrofolate reductase: synthesis and biological evaluation of methotrexate analogues. J. Med. Chem. 43:2000;3852-3861.
    • (2000) J. Med. Chem. , vol.43 , pp. 3852-3861
    • Graffner-Nordberg, M.1    Marelius, J.2    Ohlsson, S.3    Persson, S.4    Swedberg, G.5    Andersson, P.6
  • 21
    • 0035146602 scopus 로고    scopus 로고
    • A search for sources of drug resistance by the 4D-QSAR analysis of a set of antimalarial dihydrofolate reductase inhibitors
    • Santos-Filho O.A., Hopfinger A.J. A search for sources of drug resistance by the 4D-QSAR analysis of a set of antimalarial dihydrofolate reductase inhibitors. J. Comput.-Aided Mol. Des. 15:2001;1-12.
    • (2001) J. Comput.-Aided Mol. Des. , vol.15 , pp. 1-12
    • Santos-Filho, O.A.1    Hopfinger, A.J.2
  • 22
    • 0035732844 scopus 로고    scopus 로고
    • One site fits both: A model for the ternary complex of folate+NADPH in R67 dihydrofolate reductase, a D2 symmetric enzyme
    • Howell E.E., Shukla U., Hicks S.N., Smiley R.D., Kuhn L.A., Zavodszky M.I. One site fits both: a model for the ternary complex of folate+NADPH in R67 dihydrofolate reductase, a D2 symmetric enzyme. J. Comput.-Aided Mol. Des. 15:2001;1035-1052.
    • (2001) J. Comput.-Aided Mol. Des. , vol.15 , pp. 1035-1052
    • Howell, E.E.1    Shukla, U.2    Hicks, S.N.3    Smiley, R.D.4    Kuhn, L.A.5    Zavodszky, M.I.6
  • 24
    • 0030944408 scopus 로고    scopus 로고
    • Electrostatic characterization of enzyme complexes: Evaluation of the mechanism of catalysis of dihydrofolate reductase
    • Cannon W.R., Garrison B.J., Benkovic S.J. Electrostatic characterization of enzyme complexes: evaluation of the mechanism of catalysis of dihydrofolate reductase. J. Am. Chem. Soc. 119:1997;2386-2395.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2386-2395
    • Cannon, W.R.1    Garrison, B.J.2    Benkovic, S.J.3
  • 25
    • 0032511406 scopus 로고    scopus 로고
    • Structure of dihydrofolate when bound to dihydrofolate reductase
    • Deng H., Callender R. Structure of dihydrofolate when bound to dihydrofolate reductase. J. Am. Chem. Soc. 120:1998;7730-7737.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7730-7737
    • Deng, H.1    Callender, R.2
  • 26
    • 0001685622 scopus 로고    scopus 로고
    • Combined quantum and molecular mechanics (qm/mm) study of the ionization state of 8-methylpterin substrate bound to dihydrofolate reductase
    • Cummins P.L., Gready J.E. Combined quantum and molecular mechanics (qm/mm) study of the ionization state of 8-methylpterin substrate bound to dihydrofolate reductase. J. Phys. Chem. B. 104:2000;4503-4510.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 4503-4510
    • Cummins, P.L.1    Gready, J.E.2
  • 27
    • 0034351147 scopus 로고    scopus 로고
    • QM/MM and SCRF studies of the ionization state of 8-methylpterin substrate bound to dihydrofolate reductase: Existence of a low-barrier hydrogen bond
    • Cummins P.L., Gready J.E. QM/MM and SCRF studies of the ionization state of 8-methylpterin substrate bound to dihydrofolate reductase: existence of a low-barrier hydrogen bond. J. Mol. Graph. Modell. 18:2000;42-49.
    • (2000) J. Mol. Graph. Modell. , vol.18 , pp. 42-49
    • Cummins, P.L.1    Gready, J.E.2
  • 28
    • 84961978282 scopus 로고    scopus 로고
    • Energetically most likely substrate and active-site protonation sites and pathways in the catalytic mechanism of dihydrofolate reductase
    • Cummins P.L., Gready J.E. Energetically most likely substrate and active-site protonation sites and pathways in the catalytic mechanism of dihydrofolate reductase. J. Am. Chem. Soc. 123:2001;3418-3428.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3418-3428
    • Cummins, P.L.1    Gready, J.E.2
  • 29
    • 0001704148 scopus 로고    scopus 로고
    • Molecular dynamics and free energy perturbation study of hydride-ion transfer step in dihydrofolate reductase using combined quantum and molecular mechanical model
    • Cummins P.L., Gready J.E. Molecular dynamics and free energy perturbation study of hydride-ion transfer step in dihydrofolate reductase using combined quantum and molecular mechanical model. J. Comput. Chem. 19:1998;977-988.
    • (1998) J. Comput. Chem. , vol.19 , pp. 977-988
    • Cummins, P.L.1    Gready, J.E.2
  • 30
    • 0041853282 scopus 로고    scopus 로고
    • Investigating enzyme reaction mechanisms with quantum mechanical-molecular mechanical plus molecular dynamics calculations
    • (Combined Quantum Mechanical and Molecular Mechanical Methods)
    • Cummins P.L., Gready J.E. Investigating enzyme reaction mechanisms with quantum mechanical-molecular mechanical plus molecular dynamics calculations. ACS Sympos. Ser. 712:1998;250-263. (Combined Quantum Mechanical and Molecular Mechanical Methods).
    • (1998) ACS Sympos. Ser. , vol.712 , pp. 250-263
    • Cummins, P.L.1    Gready, J.E.2
  • 31
    • 0032693616 scopus 로고    scopus 로고
    • Enzyme polarization of substrates of dihydrofolate reductase by different theoretical methods
    • Greatbanks S.P., Gready J.E., Limaye A.C., Rendall A.P. Enzyme polarization of substrates of dihydrofolate reductase by different theoretical methods. Proteins: Struct. Funct. Genet. 37:1999;157-165.
    • (1999) Proteins: Struct. Funct. Genet. , vol.37 , pp. 157-165
    • Greatbanks, S.P.1    Gready, J.E.2    Limaye, A.C.3    Rendall, A.P.4
  • 32
    • 0001563728 scopus 로고    scopus 로고
    • Comparison of enzyme polarization of ligands and charge-transfer effects for dihydrofolate reductase using point-charge embedded ab initio quantum mechanical and linear-scaling semiempirical quantum mechanical methods
    • Greatbanks S.P., Gready J.E., Limaye A.C., Rendell A.P. Comparison of enzyme polarization of ligands and charge-transfer effects for dihydrofolate reductase using point-charge embedded ab initio quantum mechanical and linear-scaling semiempirical quantum mechanical methods. J. Comput. Chem. 21:2000;788-811.
    • (2000) J. Comput. Chem. , vol.21 , pp. 788-811
    • Greatbanks, S.P.1    Gready, J.E.2    Limaye, A.C.3    Rendell, A.P.4
  • 33
    • 0029875239 scopus 로고    scopus 로고
    • On transition structures for hydride transfer step: A theoretical study of the reaction catalyzed by dihydrofolate reductase enzyme
    • Andres J., Moliner V., Safont V.S., Domingo L.R., Picher M.T., Krechl J. On transition structures for hydride transfer step: a theoretical study of the reaction catalyzed by dihydrofolate reductase enzyme. Bioorg. Chem. 24:1996;10-18.
    • (1996) Bioorg. Chem. , vol.24 , pp. 10-18
    • Andres, J.1    Moliner, V.2    Safont, V.S.3    Domingo, L.R.4    Picher, M.T.5    Krechl, J.6
  • 34
    • 0000083020 scopus 로고    scopus 로고
    • Transition structures for hydride transfer reactions in vacuo and their role in enzyme catalysis
    • Andres J., Moliner V., Safont V.S., Aullo J.M., Diaz W., Tapia O. Transition structures for hydride transfer reactions in vacuo and their role in enzyme catalysis. THEOCHEM. 371:1996;299-312.
    • (1996) THEOCHEM , vol.371 , pp. 299-312
    • Andres, J.1    Moliner, V.2    Safont, V.S.3    Aullo, J.M.4    Diaz, W.5    Tapia, O.6
  • 35
    • 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., Moliner V. 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. 121:1999;12140-12147.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 12140-12147
    • Castillo, R.1    Andres, J.2    Moliner, V.3
  • 36
    • 0037188007 scopus 로고    scopus 로고
    • Nuclear quantum effects and enzyme dynamics in dihydrofolate reductase catalysis
    • Agarwal P.K., Billeter S.R., Hammes-Schiffer S. Nuclear quantum effects and enzyme dynamics in dihydrofolate reductase catalysis. J. Phys. Chem. B. 106:2002;3283-3293.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 3283-3293
    • Agarwal, P.K.1    Billeter, S.R.2    Hammes-Schiffer, S.3
  • 38
    • 0033955055 scopus 로고    scopus 로고
    • Protein dynamics in enzymatic catalysis: Exploration of dihydrofolate reductase
    • Radkiewicz J.L., Brooks C.L. III. 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.L.1    Brooks C.L. III2
  • 40
    • 0026095360 scopus 로고
    • Theoretical studies on the dihydrofolate reductase mechanism: Electronic polarization of bound substrates
    • Bajorath J., Kraut J., Li Z., Kitson D.H., Hagler A.T. Theoretical studies on the dihydrofolate reductase mechanism: electronic polarization of bound substrates. Proc. Natl Acad. Sci. USA. 88:1991;6423-6426.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 6423-6426
    • Bajorath, J.1    Kraut, J.2    Li, Z.3    Kitson, D.H.4    Hagler, A.T.5
  • 43
    • 0035892157 scopus 로고    scopus 로고
    • Canonical variational theory for enzyme kinetics with the protein mean force and multidimensional quantum mechanical tunneling dynamics. Theory and application to liver alcohol dehydrogenase
    • Alhambra C., Corchado J.C., Sánchez M.L., Garcia-Viloca M., Gao J., Truhlar D.G. Canonical variational theory for enzyme kinetics with the protein mean force and multidimensional quantum mechanical tunneling dynamics. Theory and application to liver alcohol dehydrogenase. J. Phys. Chem. B. 105:2001;11326-11340.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 11326-11340
    • Alhambra, C.1    Corchado, J.C.2    Sánchez, M.L.3    Garcia-Viloca, M.4    Gao, J.5    Truhlar, D.G.6
  • 44
    • 0031443372 scopus 로고    scopus 로고
    • Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from a kinetic analysis of a site-directed mutant
    • Cameron C.E., Benkovic S.J. Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from a kinetic analysis of a site-directed mutant. Biochemistry. 36:1997;15792-15800.
    • (1997) Biochemistry , vol.36 , pp. 15792-15800
    • Cameron, C.E.1    Benkovic, S.J.2
  • 45
    • 0027125907 scopus 로고
    • A prior evaluation of aqueous polarization effects through Monte Carlo QM-MM simulations
    • Gao J., Xia X. A prior evaluation of aqueous polarization effects through Monte Carlo QM-MM simulations. Science. 258:1992;631-635.
    • (1992) Science , vol.258 , pp. 631-635
    • Gao, J.1    Xia, X.2
  • 46
    • 84961976173 scopus 로고
    • Polarization of the nucleic acid bases in aqueous solution
    • erratum: 1993, 202, 567
    • Cramer C.J., Truhlar D.G. Polarization of the nucleic acid bases in aqueous solution. Chem. Phys. Lett. 198:1992;74-80. erratum: 1993, 202, 567.
    • (1992) Chem. Phys. Lett. , vol.198 , pp. 74-80
    • Cramer, C.J.1    Truhlar, D.G.2
  • 48
    • 0017100947 scopus 로고
    • Theoretical studies of enzymatic reactions: Dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
    • Warshel A., Levitt M. Theoretical studies of enzymatic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme. J. Mol. Biol. 103:1976;227-249.
    • (1976) J. Mol. Biol. , vol.103 , pp. 227-249
    • Warshel, A.1    Levitt, M.2
  • 49
    • 84988053595 scopus 로고
    • 3Cl+Cl-exchange reaction and gas phase protonation of polyethers
    • 3Cl+Cl-exchange reaction and gas phase protonation of polyethers. J. Comp. Chem. 7:1986;718-730.
    • (1986) J. Comp. Chem. , vol.7 , pp. 718-730
    • Singh, U.C.1    Kollman, P.A.2
  • 50
    • 33845283509 scopus 로고
    • Free energy perturbation theory method for chemical reactions in the condensed phase: A dynamic approach based on a combined quantum and molecular mechanics potential
    • Bash P.A., Field M.J., Karplus M. Free energy perturbation theory method for chemical reactions in the condensed phase: a dynamic approach based on a combined quantum and molecular mechanics potential. J. Am. Chem. Soc. 109:1987;8092-8094.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 8092-8094
    • Bash, P.A.1    Field, M.J.2    Karplus, M.3
  • 51
    • 84962367344 scopus 로고
    • Methods and applications of combined quantum mechanical and molecular mechanical potentials
    • Gao J. Methods and applications of combined quantum mechanical and molecular mechanical potentials. Rev. Comput. Chem. 7:1995;119-185.
    • (1995) Rev. Comput. Chem. , vol.7 , pp. 119-185
    • Gao, J.1
  • 52
    • 0000411659 scopus 로고    scopus 로고
    • A generalized hybrid orbital (GHO) method for the treatment of boundary atoms in combined QM/MM calculations
    • Gao J., Amara P., Alhambra C., Field M.J. A generalized hybrid orbital (GHO) method for the treatment of boundary atoms in combined QM/MM calculations. J. Phys. Chem. A. 102:1998;4714-4721.
    • (1998) J. Phys. Chem. A , vol.102 , pp. 4714-4721
    • Gao, J.1    Amara, P.2    Alhambra, C.3    Field, M.J.4
  • 53
    • 0036025446 scopus 로고    scopus 로고
    • Quantum mechanical methods for enzyme kinetics
    • Gao J., Truhlar D.G. Quantum mechanical methods for enzyme kinetics. Annu. Rev. Phys. Chem. 53:2002;457-505.
    • (2002) Annu. Rev. Phys. Chem. , vol.53 , pp. 457-505
    • Gao, J.1    Truhlar, D.G.2
  • 54
    • 0842341771 scopus 로고
    • Development and use of quantum mechanical molecular models. 76. AM1: A new general purpose quantum mechanical molecular model
    • Dewar M.J.S., Zoebisch E.G., Healy E.F., Stewart J.J.P. Development and use of quantum mechanical molecular models. 76. AM1: a new general purpose quantum mechanical molecular model. J. Am. Chem. Soc. 107:1985;3902-3909.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 3902-3909
    • Dewar, M.J.S.1    Zoebisch, E.G.2    Healy, E.F.3    Stewart, J.J.P.4
  • 59
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • Sawaya M.R., Kraut J. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry. 36:1997;586-603.
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 61
    • 34547809547 scopus 로고
    • A unified formulation of the constant-temperature molecular dynamics methods
    • Nosé S. A unified formulation of the constant-temperature molecular dynamics methods. J. Chem. Phys. 81:1984;511-519.
    • (1984) J. Chem. Phys. , vol.81 , pp. 511-519
    • Nosé, S.1
  • 62
    • 0001538909 scopus 로고
    • Canonical dynamics equilibrium phase-space distributions
    • Hoover W.G. Canonical dynamics equilibrium phase-space distributions. Phys. Rev. A. 31:1985;1695-1697.
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 64
    • 0001678587 scopus 로고    scopus 로고
    • A theoretical investigation of the enol content of acetic acid and the acetate ion in aqueous solution
    • Gao J. A theoretical investigation of the enol content of acetic acid and the acetate ion in aqueous solution. Theochem. 370:1996;203-208.
    • (1996) Theochem , vol.370 , pp. 203-208
    • Gao, J.1
  • 65
    • 0037456452 scopus 로고    scopus 로고
    • A perturbation approach to combined QM/MM simulations of solute-solvent interactions in solution
    • in press
    • Cubero E., Luque F.J., Orozco M., Gao J. A perturbation approach to combined QM/MM simulations of solute-solvent interactions in solution. J. Phys. Chem. B. 2003;. in press.
    • (2003) J. Phys. Chem. B
    • Cubero, E.1    Luque, F.J.2    Orozco, M.3    Gao, J.4
  • 66
    • 11644266970 scopus 로고
    • Electronic population analysis on LCAO molecular wave functions. I
    • Mulliken R.S. Electronic population analysis on LCAO molecular wave functions. I. J. Chem. Phys. 23:1955;1833-1844.
    • (1955) J. Chem. Phys. , vol.23 , pp. 1833-1844
    • Mulliken, R.S.1
  • 67
    • 0028305058 scopus 로고
    • Determination by Raman, spectroscopy of the pka of N5 of dihydrofolate bound to dihydrofolate reductase: Mechanistic implications
    • Chen Y.-Q., Kraut J., Blakley R.L., Callender R. Determination by Raman, spectroscopy of the pka of N5 of dihydrofolate bound to dihydrofolate reductase: mechanistic implications. Biochemistry. 33:1994;7021-7026.
    • (1994) Biochemistry , vol.33 , pp. 7021-7026
    • Chen, Y.-Q.1    Kraut, J.2    Blakley, R.L.3    Callender, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.