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Volumn 8, Issue 2, 1998, Pages 245-249

Theory of biomolecular recognition

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BINDING; KINETICS; MOLECULAR RECOGNITION; PRIORITY JOURNAL; REVIEW; THEORY; THERMODYNAMICS;

EID: 0032054612     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80046-8     Document Type: Article
Times cited : (142)

References (59)
  • 1
    • 0000686383 scopus 로고    scopus 로고
    • Molecular recognition
    • S.H. Gellman.
    • Gellman SH. Molecular recognition. Chem Rev. 97:1997;1231-1734.
    • (1997) Chem Rev , vol.97 , pp. 1231-1734
  • 4
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes: Simple physics, complicated biology
    • Murray D, Ben-Tal N, Honig B, McLaughlin S. Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology. Structure. 5:1997;985-989.
    • (1997) Structure , vol.5 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 5
    • 0030048070 scopus 로고    scopus 로고
    • Protein-protein interactions in the rigor actomyosin complex
    • Milligan RA. Protein-protein interactions in the rigor actomyosin complex. Proc Natl Acad Sci USA. 93:1996;21-26.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 21-26
    • Milligan, R.A.1
  • 6
    • 0029109468 scopus 로고
    • Protein-protein interactions: A review of protein dimer structures
    • Jones S, Thornton JM. Protein-protein interactions: a review of protein dimer structures. Prog Biophys Mol Biol. 63:1995;31-65.
    • (1995) Prog Biophys Mol Biol , vol.63 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 7
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S, Thornton JM. Principles of protein-protein interactions. Proc Natl Acad Sci USA. 93:1996;13-20.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 8
    • 0030050701 scopus 로고    scopus 로고
    • Binding in growth hormone receptor complex
    • Wells JA. Binding in growth hormone receptor complex. Proc Natl Acad Sci USA. 93:1996;1-6.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1-6
    • Wells, J.A.1
  • 9
    • 0029900085 scopus 로고    scopus 로고
    • Negative electrostatic surface potential of protein sites specific for anionic ligands
    • Ledvina PS, Yao N, Choudhary A, Quiocho FA. Negative electrostatic surface potential of protein sites specific for anionic ligands. Proc Natl Acad Sci USA. 93:1996;6786-6791.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6786-6791
    • Ledvina, P.S.1    Yao, N.2    Choudhary, A.3    Quiocho, F.A.4
  • 10
    • 0031571127 scopus 로고    scopus 로고
    • Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin
    • Carr PA, Erickson HP, Palmer AG. Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin. Structure. 5:1997;949-959.
    • (1997) Structure , vol.5 , pp. 949-959
    • Carr, P.A.1    Erickson, H.P.2    Palmer, A.G.3
  • 11
    • 0031238604 scopus 로고    scopus 로고
    • DNA recognition and bending
    • Allemann RK, Egli M. DNA recognition and bending. Chem Biol. 4:1997;643-650.
    • (1997) Chem Biol , vol.4 , pp. 643-650
    • Allemann, R.K.1    Egli, M.2
  • 12
    • 0030803385 scopus 로고    scopus 로고
    • Electrostatic mechanism for DNA bending by bZIP proteins
    • Paolella DN, Liu Y, Fabian MA, Schepartz A. Electrostatic mechanism for DNA bending by bZIP proteins. Biochemistry. 36:1997;10033-10038.
    • (1997) Biochemistry , vol.36 , pp. 10033-10038
    • Paolella, D.N.1    Liu, Y.2    Fabian, M.A.3    Schepartz, A.4
  • 13
    • 0031588020 scopus 로고    scopus 로고
    • Quasi-equivalent viruses: A paradigm for protein assemblies
    • Johnson JE, Speir JA. Quasi-equivalent viruses: a paradigm for protein assemblies. J Mol Biol. 269:1997;665-675.
    • (1997) J Mol Biol , vol.269 , pp. 665-675
    • Johnson, J.E.1    Speir, J.A.2
  • 16
    • 0030972149 scopus 로고    scopus 로고
    • Differences in water release with DNA binding by ultrabithorax and deformed homeodomains
    • Li L, Matthews KS. Differences in water release with DNA binding by ultrabithorax and deformed homeodomains. Biochemistry. 36:1997;7003-7011.
    • (1997) Biochemistry , vol.36 , pp. 7003-7011
    • Li, L.1    Matthews, K.S.2
  • 17
    • 0031591393 scopus 로고    scopus 로고
    • Electrostatics and hydration at the homeodomain - DNA interface: Chemical probes of an interfacial water cavity
    • Labeots LA, Weiss MA. Electrostatics and hydration at the homeodomain - DNA interface: chemical probes of an interfacial water cavity. J Mol Biol. 269:1997;113-128.
    • (1997) J Mol Biol , vol.269 , pp. 113-128
    • Labeots, L.A.1    Weiss, M.A.2
  • 18
    • 0030770571 scopus 로고    scopus 로고
    • Involvement of water molecules in the association of monoclonal antibody HyHEL-5 with bobwhite quail lysozyme
    • Xavier KA, Shick KA, Smith-Gill SJ, Willson RC. Involvement of water molecules in the association of monoclonal antibody HyHEL-5 with bobwhite quail lysozyme. Biophys J. 73:1997;2116-2125.
    • (1997) Biophys J , vol.73 , pp. 2116-2125
    • Xavier, K.A.1    Shick, K.A.2    Smith-Gill, S.J.3    Willson, R.C.4
  • 19
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • Davies DR, Cohen GH. Interactions of protein antigens with antibodies. Proc Natl Acad Sci USA. 93:1996;7-12.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 20
    • 0030828982 scopus 로고    scopus 로고
    • Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase: Distinctions between active center ligands and fasciculin
    • Radic Z, Kirchhoff PD, Quinn DM, McCammon JA, Taylor P. Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase: distinctions between active center ligands and fasciculin. J Biol Chem. 272:1997;23265-23277.
    • (1997) J Biol Chem , vol.272 , pp. 23265-23277
    • Radic, Z.1    Kirchhoff, P.D.2    Quinn, D.M.3    McCammon, J.A.4    Taylor, P.5
  • 21
    • 0031588017 scopus 로고    scopus 로고
    • Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL
    • Perrett S, Zahn R, Stenberg G, Fersht AR. Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL. J Mol Biol. 269:1997;892-901.
    • (1997) J Mol Biol , vol.269 , pp. 892-901
    • Perrett, S.1    Zahn, R.2    Stenberg, G.3    Fersht, A.R.4
  • 22
    • 0031058541 scopus 로고    scopus 로고
    • The statistical-thermodynamic basis for computation of binding affinities: A critical review
    • of outstanding interest. This paper derives the standard free energy of binding in a way that allows for direct contact with the interaction models that are commonly used in biochemistry. It clears up a number of misconceptions about such calculations, provides explicit formulas that account for concomitant binding or release of solvent or other molecules, and describes various possible decompositions that may aid in the interpretation of the results.
    • Gilson MK, Given JA, Bush BL, McCammon JA. The statistical-thermodynamic basis for computation of binding affinities: a critical review. of outstanding interest Biophys J. 72:1997;1047-1069 This paper derives the standard free energy of binding in a way that allows for direct contact with the interaction models that are commonly used in biochemistry. It clears up a number of misconceptions about such calculations, provides explicit formulas that account for concomitant binding or release of solvent or other molecules, and describes various possible decompositions that may aid in the interpretation of the results.
    • (1997) Biophys J , vol.72 , pp. 1047-1069
    • Gilson, M.K.1    Given, J.A.2    Bush, B.L.3    McCammon, J.A.4
  • 23
    • 0030503687 scopus 로고    scopus 로고
    • Free energy by molecular simulation
    • K.B. Lipkowitz, Boyd D.B. New York: VCH Publishers Inc
    • Straatsma TP. Free energy by molecular simulation. Lipkowitz KB, Boyd DB. Reviews in Computational Chemistry. 9:1996;81-127 VCH Publishers Inc, New York.
    • (1996) Reviews in Computational Chemistry , vol.9 , pp. 81-127
    • Straatsma, T.P.1
  • 24
    • 2542564912 scopus 로고    scopus 로고
    • Advances and continuing challenges in achieving realistic and predictive simulations of the properties of organic and biological molecules
    • Kollman PA. Advances and continuing challenges in achieving realistic and predictive simulations of the properties of organic and biological molecules. Accounts Chem Res. 29:1996;461-469.
    • (1996) Accounts Chem Res , vol.29 , pp. 461-469
    • Kollman, P.A.1
  • 25
    • 0030134642 scopus 로고    scopus 로고
    • On estimating the relative free energy of different molecular states with respect to a single reference state
    • of special interest. The authors describe a promising method for speeding up the comparison of the free energies for binding related ligand - receptor pairs. The method makes use of soft-core interaction centers to increase the overlap of a reference simulation with the configurations of differently substituted molecules.
    • Liu H, Mark AE, van Gunsteren WF. On estimating the relative free energy of different molecular states with respect to a single reference state. of special interest J Phys Chem. 100:1996;9485-9494 The authors describe a promising method for speeding up the comparison of the free energies for binding related ligand - receptor pairs. The method makes use of soft-core interaction centers to increase the overlap of a reference simulation with the configurations of differently substituted molecules.
    • (1996) J Phys Chem , vol.100 , pp. 9485-9494
    • Liu, H.1    Mark, A.E.2    Van Gunsteren, W.F.3
  • 26
    • 0001692244 scopus 로고    scopus 로고
    • Lambda-dynamics: A new approach to free energy calculations
    • of special interest. By treating the coupling variable in free energy simulations as a dynamic variable, the authors are able to increase the efficiency of a variety of free energy calculations.
    • Kong X, Brooks CL. Lambda-dynamics: a new approach to free energy calculations. of special interest J Chem Phys. 105:1996;2414-2423 By treating the coupling variable in free energy simulations as a dynamic variable, the authors are able to increase the efficiency of a variety of free energy calculations.
    • (1996) J Chem Phys , vol.105 , pp. 2414-2423
    • Kong, X.1    Brooks, C.L.2
  • 27
    • 0000204832 scopus 로고    scopus 로고
    • The Jacobian factor in free energy simulations
    • of special interest. This paper provides valuable insight and useful formulas for correcting the results of free energy simulations that involve changes in the internal coordinates that are subject to constraints.
    • Boresch S, Karplus M. The Jacobian factor in free energy simulations. of special interest J Chem Phys. 105:1996;5145-5154 This paper provides valuable insight and useful formulas for correcting the results of free energy simulations that involve changes in the internal coordinates that are subject to constraints.
    • (1996) J Chem Phys , vol.105 , pp. 5145-5154
    • Boresch, S.1    Karplus, M.2
  • 28
    • 0001656183 scopus 로고    scopus 로고
    • Free energy simulations: Correcting for electrostatic cutoffs by use of the Poisson equation
    • Rosat H, McCammon JA. Free energy simulations: correcting for electrostatic cutoffs by use of the Poisson equation. J Chem Phys. 104:1996;7645-7651.
    • (1996) J Chem Phys , vol.104 , pp. 7645-7651
    • Rosat, H.1    McCammon, J.A.2
  • 29
    • 0031561292 scopus 로고    scopus 로고
    • Continuum treatment of long-range interactions in free energy calculations. Application to protein-ligand binding
    • Simonson T, Archontis G, Karplus M. Continuum treatment of long-range interactions in free energy calculations. Application to protein-ligand binding. J Phys Chem B. 101:1997;8349-8362.
    • (1997) J Phys Chem B , vol.101 , pp. 8349-8362
    • Simonson, T.1    Archontis, G.2    Karplus, M.3
  • 30
    • 0031012579 scopus 로고    scopus 로고
    • Enzyme-inhibitor association thermodynamics: Explicit and continuum solvent studies
    • of special interest. The authors introduce the use of grand ensemble sampling to add or remove water molecules from binding pockets in calculations of free energies of binding.
    • Resat H, Marrone TJ, McCammon JA. Enzyme-inhibitor association thermodynamics: explicit and continuum solvent studies. of special interest Biophys J. 72:1997;522-532 The authors introduce the use of grand ensemble sampling to add or remove water molecules from binding pockets in calculations of free energies of binding.
    • (1997) Biophys J , vol.72 , pp. 522-532
    • Resat, H.1    Marrone, T.J.2    McCammon, J.A.3
  • 31
    • 0030918284 scopus 로고    scopus 로고
    • Biomolecular dynamics at long timesteps: Bridging the timescale gap between simulation and experimentation
    • of special interest. This is a very useful review of the molecular dynamics method for sampling configurations, including the use of larger time steps to increase sampling efficiency.
    • Schlick T, Barth E, Mandziuk M. Biomolecular dynamics at long timesteps: bridging the timescale gap between simulation and experimentation. of special interest Annu Rev Biophys Biomol Struct. 26:1997;181-222 This is a very useful review of the molecular dynamics method for sampling configurations, including the use of larger time steps to increase sampling efficiency.
    • (1997) Annu Rev Biophys Biomol Struct , vol.26 , pp. 181-222
    • Schlick, T.1    Barth, E.2    Mandziuk, M.3
  • 32
    • 0031275544 scopus 로고    scopus 로고
    • Monte Carlo simulations for proteins: Binding affinities for trypsin - Benzamidine complexes via free-energy perturbations
    • Essex J, Tirado-Rives J, Severance DL, Jorgensen W. Monte Carlo simulations for proteins: binding affinities for trypsin - benzamidine complexes via free-energy perturbations. J Phys Chem B. 101:1998;9663-9669.
    • (1998) J Phys Chem B , vol.101 , pp. 9663-9669
    • Essex, J.1    Tirado-Rives, J.2    Severance, D.L.3    Jorgensen, W.4
  • 33
    • 0000682989 scopus 로고    scopus 로고
    • Finite difference Poisson-Boltzmann electrostatic calculations: Increased accuracy achieved by harmonic dielectric smoothing and charge antialiasing
    • Bruccoleri RE, Novotny J, Davis ME, Sharp KA. Finite difference Poisson-Boltzmann electrostatic calculations: increased accuracy achieved by harmonic dielectric smoothing and charge antialiasing. J Comput Chem. 18:1997;268-276.
    • (1997) J Comput Chem , vol.18 , pp. 268-276
    • Bruccoleri, R.E.1    Novotny, J.2    Davis, M.E.3    Sharp, K.A.4
  • 34
    • 0001445346 scopus 로고    scopus 로고
    • A fast adaptive multigrid boundary element method for macromolecular electrostatic computations in a solvent
    • Vorobjev YN, Scheraga HA. A fast adaptive multigrid boundary element method for macromolecular electrostatic computations in a solvent. J Comput Chem. 18:1997;569-583.
    • (1997) J Comput Chem , vol.18 , pp. 569-583
    • Vorobjev, Y.N.1    Scheraga, H.A.2
  • 35
    • 0001439211 scopus 로고    scopus 로고
    • Numerical solution of the Poisson-Boltzmann equation using tetrahedral finite-element meshes
    • Cortis CM, Friesner RA. Numerical solution of the Poisson-Boltzmann equation using tetrahedral finite-element meshes. J Comput Chem. 18:1997;1591-1608.
    • (1997) J Comput Chem , vol.18 , pp. 1591-1608
    • Cortis, C.M.1    Friesner, R.A.2
  • 36
    • 0001585447 scopus 로고
    • Computation of electrostatic forces on solvated molecules using the Poisson-Boltzmann equation
    • Gilson MK, Davis ME, Luty BA, McCammon JA. Computation of electrostatic forces on solvated molecules using the Poisson-Boltzmann equation. J Phys Chem. 97:1993;3591-3600.
    • (1993) J Phys Chem , vol.97 , pp. 3591-3600
    • Gilson, M.K.1    Davis, M.E.2    Luty, B.A.3    McCammon, J.A.4
  • 37
    • 0029895487 scopus 로고    scopus 로고
    • The low dielectric interior of proteins is sufficient to cause major structural changes in DNA on association
    • of special interest. The binding of many biomolecular pairs involves sizable deformations of one or both molecules. This paper demonstrates that molecular dynamics simulations with continuum solvent models can rapidly generate such deformations. This is likely to prove useful in future simulations of the docking of flexible biomolecules.
    • Elcock AH, McCammon JA. The low dielectric interior of proteins is sufficient to cause major structural changes in DNA on association. of special interest J Am Chem Soc. 118:1996;3787-3788 The binding of many biomolecular pairs involves sizable deformations of one or both molecules. This paper demonstrates that molecular dynamics simulations with continuum solvent models can rapidly generate such deformations. This is likely to prove useful in future simulations of the docking of flexible biomolecules.
    • (1996) J Am Chem Soc , vol.118 , pp. 3787-3788
    • Elcock, A.H.1    McCammon, J.A.2
  • 38
    • 0031560531 scopus 로고    scopus 로고
    • Incorporating hydration force determined by boundary element method into stochastic dynamics
    • Wang CX, Wan SZ, Xiang ZX, Shi YY. Incorporating hydration force determined by boundary element method into stochastic dynamics. J Phys Chem B. 101:1997;230-235.
    • (1997) J Phys Chem B , vol.101 , pp. 230-235
    • Wang, C.X.1    Wan, S.Z.2    Xiang, Z.X.3    Shi, Y.Y.4
  • 39
    • 0031010107 scopus 로고    scopus 로고
    • The kinetics of protein-protein recognition
    • of special interest. The author provides an insightful discussion of how electrostatic interactions can modify the rate of protein - protein binding.
    • Janin J. The kinetics of protein-protein recognition. of special interest Proteins. 28:1997;153-161 The author provides an insightful discussion of how electrostatic interactions can modify the rate of protein - protein binding.
    • (1997) Proteins , vol.28 , pp. 153-161
    • Janin, J.1
  • 40
    • 0030891436 scopus 로고    scopus 로고
    • Simulation of the diffusional association of barnase and barstar
    • of outstanding interest. This paper makes use of several innovations to provide an important new Brownian dynamics approach for calculating rates of protein - protein binding. Effective charges are used to approximate the effect of the low dielectric volumes of the proteins on their electrostatic interaction, and a valuable analysis of the criteria for successful binding is presented.
    • Gabdoulline RR, Wade RC. Simulation of the diffusional association of barnase and barstar. of outstanding interest Biophys J. 72:1997;1917-1929 This paper makes use of several innovations to provide an important new Brownian dynamics approach for calculating rates of protein - protein binding. Effective charges are used to approximate the effect of the low dielectric volumes of the proteins on their electrostatic interaction, and a valuable analysis of the criteria for successful binding is presented.
    • (1997) Biophys J , vol.72 , pp. 1917-1929
    • Gabdoulline, R.R.1    Wade, R.C.2
  • 41
    • 0030070532 scopus 로고    scopus 로고
    • Weighted-ensemble Brownian dynamics simulations for protein association reactions
    • of outstanding interest. The authors describe a novel way of generating the trajectory statistics needed for rate constant calculations by Brownian dynamics simulation. The method involves eliminating certain members of the ensemble of diffusing reactant pairs, and duplicating others, so as to insure adequate sampling of low probability configurations.
    • Huber GA, Kim S. Weighted-ensemble Brownian dynamics simulations for protein association reactions. of outstanding interest Biophys J. 70:1996;97-110 The authors describe a novel way of generating the trajectory statistics needed for rate constant calculations by Brownian dynamics simulation. The method involves eliminating certain members of the ensemble of diffusing reactant pairs, and duplicating others, so as to insure adequate sampling of low probability configurations.
    • (1996) Biophys J , vol.70 , pp. 97-110
    • Huber, G.A.1    Kim, S.2
  • 42
    • 0031207063 scopus 로고    scopus 로고
    • Brownian dynamics simulation of diffusion-limited polymerization of rodlike molecules: Isotropic translational diffusion
    • Gupta JS, Khakhar DV. Brownian dynamics simulation of diffusion-limited polymerization of rodlike molecules: isotropic translational diffusion. J Chem Phys. 107:1997;3289-3296.
    • (1997) J Chem Phys , vol.107 , pp. 3289-3296
    • Gupta, J.S.1    Khakhar, D.V.2
  • 43
  • 44
    • 0030805890 scopus 로고    scopus 로고
    • Binding of the estrogen receptor to DNA. The role of waters
    • Kosztin D, Bishop TC, Schulten K. Binding of the estrogen receptor to DNA. The role of waters. Biophys J. 73:1997;557-570.
    • (1997) Biophys J , vol.73 , pp. 557-570
    • Kosztin, D.1    Bishop, T.C.2    Schulten, K.3
  • 45
    • 0030815020 scopus 로고    scopus 로고
    • Computational binding studies of orthogonal cyclosporin-cyclophilin pairs
    • Pierce AC, Jorgensen WL. Computational binding studies of orthogonal cyclosporin-cyclophilin pairs. Angew Chem Int Ed. 36:1997;1466-1469.
    • (1997) Angew Chem Int Ed , vol.36 , pp. 1466-1469
    • Pierce, A.C.1    Jorgensen, W.L.2
  • 46
    • 0031008575 scopus 로고    scopus 로고
    • On the calculation of binding free energies using continuum methods: Application to MHC class I protein - Peptide interactions
    • of special interest. This paper includes a particularly complete discussion of some of the issues involved in the practical applications of continuum solvation models in calculations of free energies of binding.
    • Froloff N, Windemuth A, Honig B. On the calculation of binding free energies using continuum methods: application to MHC class I protein - peptide interactions. of special interest Protein Sci. 6:1997;1293-1301 This paper includes a particularly complete discussion of some of the issues involved in the practical applications of continuum solvation models in calculations of free energies of binding.
    • (1997) Protein Sci , vol.6 , pp. 1293-1301
    • Froloff, N.1    Windemuth, A.2    Honig, B.3
  • 47
    • 0030803237 scopus 로고    scopus 로고
    • A theoretical investigation of tight-binding thermolysin inhibitors
    • Shen J. A theoretical investigation of tight-binding thermolysin inhibitors. J Med Chem. 40:1997;2953-2958.
    • (1997) J Med Chem , vol.40 , pp. 2953-2958
    • Shen, J.1
  • 48
    • 0030606788 scopus 로고    scopus 로고
    • Electrostatic interactions in hirudin-thrombin binding
    • Sharp KA. Electrostatic interactions in hirudin-thrombin binding. Biophys Chem. 61:1996;37-49.
    • (1996) Biophys Chem , vol.61 , pp. 37-49
    • Sharp, K.A.1
  • 49
    • 0345577694 scopus 로고
    • Binding of cations and protons in the active site of acetylcholinesterase
    • Pullman A. Dordrecht, The Netherlands: Kluwer Academic Publishers
    • Wlodek S, Antosiewicz J, McCammon JA, Gilson MK. Binding of cations and protons in the active site of acetylcholinesterase. Pullman A. Modelling of Biomolecular Structures and Mechanisms. 1995;25-37 Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Modelling of Biomolecular Structures and Mechanisms , pp. 25-37
    • Wlodek, S.1    Antosiewicz, J.2    McCammon, J.A.3    Gilson, M.K.4
  • 51
    • 0030944408 scopus 로고    scopus 로고
    • Electrostatic characterization of enzyme complexes: Evaluation of the mechanism of catalysis of dihydrofolate reductase
    • Cannon WR, Garrison BJ, Benkovic SJ. 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
  • 53
    • 0031561809 scopus 로고    scopus 로고
    • Protein binding versus protein folding: The role of hydrophilic bridges in protein associations
    • Xu D, Lin SL, Nussinov R. Protein binding versus protein folding: the role of hydrophilic bridges in protein associations. J Mol Biol. 265:1997;68-84.
    • (1997) J Mol Biol , vol.265 , pp. 68-84
    • Xu, D.1    Lin, S.L.2    Nussinov, R.3
  • 55
    • 0029816432 scopus 로고    scopus 로고
    • Binding of ionic ligands to polyelectrolytes
    • Stigter D, Dill KA. Binding of ionic ligands to polyelectrolytes. Biophys J. 71:1996;2064-2074.
    • (1996) Biophys J , vol.71 , pp. 2064-2074
    • Stigter, D.1    Dill, K.A.2
  • 56
    • 0030200215 scopus 로고    scopus 로고
    • Acetylcholinesterase: Role of the enzyme's charge distribution in steering charged ligands toward the active site
    • Antosiewicz J, Wlodek ST, McCammon JA. Acetylcholinesterase: role of the enzyme's charge distribution in steering charged ligands toward the active site. Biopolymers. 39:1996;85-94.
    • (1996) Biopolymers , vol.39 , pp. 85-94
    • Antosiewicz, J.1    Wlodek, S.T.2    McCammon, J.A.3
  • 57
    • 0030729719 scopus 로고    scopus 로고
    • Design of fast enzymes by optimizing interaction potential in active site
    • of special interest. Very quick approximations of the rate constants of certain diffusion-controlled associations, based on the authors' analytical work, are shown to be useful in the engineering of faster enzymes.
    • Zhou H-X, Wong K-Y, Vijayakumar M. Design of fast enzymes by optimizing interaction potential in active site. of special interest Proc Natl Acad Sci USA. 94:1998;12372-12377 Very quick approximations of the rate constants of certain diffusion-controlled associations, based on the authors' analytical work, are shown to be useful in the engineering of faster enzymes.
    • (1998) Proc Natl Acad Sci USA , vol.94 , pp. 12372-12377
    • Zhou H-X1    Wong K-Y2    Vijayakumar, M.3
  • 58
    • 0030603887 scopus 로고    scopus 로고
    • Electrostatic channeling in the bifunctional enzyme dihydrofolate reductase-thymidylate synthase
    • of special interest. The authors show that Brownian dynamics simulations that make use of Poisson - Boltzmann electrostatic models provide a quantitative insight into the efficiency of multifunctional enzyme complexes. The electrostatic channeling of diffusing intermediates from one active site to another, as seen in this bifunctional enzyme, is likely to occur more widely.
    • Elcock AH, Potter MJ, Matthews DA, Knighton DR, McCammon JA. Electrostatic channeling in the bifunctional enzyme dihydrofolate reductase-thymidylate synthase. of special interest J Mol Biol. 262:1996;370-374 The authors show that Brownian dynamics simulations that make use of Poisson - Boltzmann electrostatic models provide a quantitative insight into the efficiency of multifunctional enzyme complexes. The electrostatic channeling of diffusing intermediates from one active site to another, as seen in this bifunctional enzyme, is likely to occur more widely.
    • (1996) J Mol Biol , vol.262 , pp. 370-374
    • Elcock, A.H.1    Potter, M.J.2    Matthews, D.A.3    Knighton, D.R.4    McCammon, J.A.5
  • 59
    • 0030998431 scopus 로고    scopus 로고
    • Construction of a homodimeric dihydrofolate reductase-thymidylate synthase bifunctional enzyme
    • Trujillo M, Duncan R, Santi DV. Construction of a homodimeric dihydrofolate reductase-thymidylate synthase bifunctional enzyme. Protein Eng. 10:1997;567-573.
    • (1997) Protein Eng , vol.10 , pp. 567-573
    • Trujillo, M.1    Duncan, R.2    Santi, D.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.