메뉴 건너뛰기




Volumn 2, Issue C, 1996, Pages 315-372

Protein Electrostatics

Author keywords

electrostatic interactions; enzymatic activity; molecular dynamics; pH; Poisson Boltzmann equation; protein engineering; protein folding; protein stability; simulation methods; solvation; structure function relationship

Indexed keywords


EID: 0000240916     PISSN: 13872656     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1387-2656(08)70016-4     Document Type: Article
Times cited : (33)

References (160)
  • 2
    • 4243463817 scopus 로고
    • Electrostatics in biomolecular structure and dynamics
    • Davis M.E., and McCammon J.A. Electrostatics in biomolecular structure and dynamics. Chem Rev 90 (1990) 509-521
    • (1990) Chem Rev , vol.90 , pp. 509-521
    • Davis, M.E.1    McCammon, J.A.2
  • 3
    • 0028266377 scopus 로고
    • Hydrodynamic motions of large molecules
    • Northrup S.H. Hydrodynamic motions of large molecules. Curr Opin Struct Biol 4 (1994) 269-274
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 269-274
    • Northrup, S.H.1
  • 6
    • 0027935845 scopus 로고
    • A negative electrostatic determinant mediates the association between the Escherichia coli trp repressor and its operator DNA
    • Guenot J., Fletterick R.J., and Kollman P.A. A negative electrostatic determinant mediates the association between the Escherichia coli trp repressor and its operator DNA. Protein Sci 3 (1994) 1276-1285
    • (1994) Protein Sci , vol.3 , pp. 1276-1285
    • Guenot, J.1    Fletterick, R.J.2    Kollman, P.A.3
  • 9
    • 0027946039 scopus 로고
    • Electrostatic effects in the control of glycogen phosphorylase by phosphorylation
    • Johnson L.N., and Barford D. Electrostatic effects in the control of glycogen phosphorylase by phosphorylation. Protein Sci 3 (1994) 1726-1730
    • (1994) Protein Sci , vol.3 , pp. 1726-1730
    • Johnson, L.N.1    Barford, D.2
  • 10
    • 0025944990 scopus 로고
    • Electrostatic control of midpoint potentials in the cytochrome subunit of the Rhodopseudomonas viridis reaction center
    • Gunner M.R., and Honig B. Electrostatic control of midpoint potentials in the cytochrome subunit of the Rhodopseudomonas viridis reaction center. Proc Natl Acad Sci USA 88 (1991) 9151-9155
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9151-9155
    • Gunner, M.R.1    Honig, B.2
  • 11
    • 0028618183 scopus 로고
    • Crystal structure of the eucaryotic DNA polymerase processivity factor PCNA
    • Krishna T.S.R., Kong X.-P., Gary S., Burgers P., and Kuriyan J. Crystal structure of the eucaryotic DNA polymerase processivity factor PCNA. Cell 79 (1994) 1233-1243
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.R.1    Kong, X.-P.2    Gary, S.3    Burgers, P.4    Kuriyan, J.5
  • 13
    • 0027231258 scopus 로고
    • On the pH dependence of protein stability
    • Yang A.-S., and Honig B. On the pH dependence of protein stability. J Mol Biol 231 (1993) 459-474
    • (1993) J Mol Biol , vol.231 , pp. 459-474
    • Yang, A.-S.1    Honig, B.2
  • 16
    • 0003475941 scopus 로고
    • van Gunsteren W.F., and Weiner P.K. (Eds), Escom, Leiden
    • In: van Gunsteren W.F., and Weiner P.K. (Eds). Computer Simulation of Biomolecular Systems (1989), Escom, Leiden
    • (1989) Computer Simulation of Biomolecular Systems
  • 17
    • 34250928962 scopus 로고
    • Volumen und Hydratationswarme der ionen
    • Bom M. Volumen und Hydratationswarme der ionen. Z Phys 1 (1920) 45-48
    • (1920) Z Phys , vol.1 , pp. 45-48
    • Bom, M.1
  • 19
    • 0343791148 scopus 로고
    • Electric moments of molecular liquids
    • Onsager L. Electric moments of molecular liquids. J Am Chem Soc 58 (1936) 1486-1493
    • (1936) J Am Chem Soc , vol.58 , pp. 1486-1493
    • Onsager, L.1
  • 20
    • 20644431615 scopus 로고
    • Theory of solutions of molecules containing widely separated charges with special application to zwitterions
    • Kirkwood J.G. Theory of solutions of molecules containing widely separated charges with special application to zwitterions. J Chem Phys 2 7 (1934) 351-361
    • (1934) J Chem Phys , vol.2 , Issue.7 , pp. 351-361
    • Kirkwood, J.G.1
  • 23
    • 33847005283 scopus 로고
    • Correlations in the motion of atoms in liquid argon
    • Rahaman A. Correlations in the motion of atoms in liquid argon. Phys Rev 136A (1964) 405-411
    • (1964) Phys Rev , vol.136 A , pp. 405-411
    • Rahaman, A.1
  • 25
    • 0003990679 scopus 로고
    • Ciccotti G., Frenkel D., and McDonald I.R. (Eds), North-Holland, Amsterdam
    • In: Ciccotti G., Frenkel D., and McDonald I.R. (Eds). Simulation of Liquids and Solids (1987), North-Holland, Amsterdam
    • (1987) Simulation of Liquids and Solids
  • 26
    • 0028093487 scopus 로고
    • A view of thermodynamics of hydration emerging from continuum studies
    • Rashin A.A., and Bukatin M.A. A view of thermodynamics of hydration emerging from continuum studies. Biophys Chem 51 (1994) 167-192
    • (1994) Biophys Chem , vol.51 , pp. 167-192
    • Rashin, A.A.1    Bukatin, M.A.2
  • 27
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig B., and Nicholls A. Classical electrostatics in biology and chemistry. Science 268 (1995) 1144-1149
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 28
    • 0021476470 scopus 로고
    • Calculations of electrostatic interactions in biological systems and in solutions
    • Warshel A., and Russell S.T. Calculations of electrostatic interactions in biological systems and in solutions. Q Rev Biophys 17 (1984) 283-422
    • (1984) Q Rev Biophys , vol.17 , pp. 283-422
    • Warshel, A.1    Russell, S.T.2
  • 29
    • 0021935830 scopus 로고
    • Electrostatic effects in proteins
    • Matthew J.B. Electrostatic effects in proteins. Ann Rev Biophys Biophys Chem 14 (1985) 387-417
    • (1985) Ann Rev Biophys Biophys Chem , vol.14 , pp. 387-417
    • Matthew, J.B.1
  • 30
    • 0022988144 scopus 로고
    • The modelling of electrostatic interactions in the function of globular proteins
    • Rogers N.K. The modelling of electrostatic interactions in the function of globular proteins. Prog Biophys Molec Biol 48 (1986) 37-66
    • (1986) Prog Biophys Molec Biol , vol.48 , pp. 37-66
    • Rogers, N.K.1
  • 31
    • 0024519351 scopus 로고
    • Treatment of electrostatic effects in macromolecular modeling
    • Harvey S.C. Treatment of electrostatic effects in macromolecular modeling. Proteins 5 (1989) 78-92
    • (1989) Proteins , vol.5 , pp. 78-92
    • Harvey, S.C.1
  • 32
    • 2142813682 scopus 로고
    • Computer simulations of molecular dynamics: Methodology, applications, and perspectives in chemistry
    • van Gunsteren W.F., and Berendsen H.J.C. Computer simulations of molecular dynamics: Methodology, applications, and perspectives in chemistry. Angew Chem Int Ed Eng 29 (1990) 992-1023
    • (1990) Angew Chem Int Ed Eng , vol.29 , pp. 992-1023
    • van Gunsteren, W.F.1    Berendsen, H.J.C.2
  • 33
    • 0025283002 scopus 로고
    • Electrostatic interactions in macromolecules: Theory and applications
    • Sharp K.A., and Honig B. Electrostatic interactions in macromolecules: Theory and applications. Ann Rev Biophys Biophys Chem 19 (1990) 301-332
    • (1990) Ann Rev Biophys Biophys Chem , vol.19 , pp. 301-332
    • Sharp, K.A.1    Honig, B.2
  • 34
    • 0000339209 scopus 로고
    • Electrostatic Effects in Biological Molecules
    • Bashford D. Electrostatic Effects in Biological Molecules. Curr Opin Struct Biol 1 2 (1991) 175-184
    • (1991) Curr Opin Struct Biol , vol.1 , Issue.2 , pp. 175-184
    • Bashford, D.1
  • 36
    • 0028215767 scopus 로고
    • Electrostatic interactions in macromolecules
    • Sharp K.A. Electrostatic interactions in macromolecules. Curr Opin Struct Biol 4 (1994) 234-239
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 234-239
    • Sharp, K.A.1
  • 37
    • 0029066848 scopus 로고
    • Theory of electrostatic interactions in macromolecules
    • Gilson M.K. Theory of electrostatic interactions in macromolecules. Curr Opin Struct Biol 5 (1995) 216-223
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 216-223
    • Gilson, M.K.1
  • 38
    • 26744440015 scopus 로고
    • Structural and energetic effects of truncating long ranged interactions in ionic and polar fluids
    • Brooks ID C.L., Pettitt B.M., and Karplus M. Structural and energetic effects of truncating long ranged interactions in ionic and polar fluids. J Chem Phys 83 (1985) 5897-5908
    • (1985) J Chem Phys , vol.83 , pp. 5897-5908
    • Brooks ID, C.L.1    Pettitt, B.M.2    Karplus, M.3
  • 39
    • 0001257361 scopus 로고
    • On the evaluation of electrostatic interactions in molecular modeling
    • Greengard L., and Rokhlin V. On the evaluation of electrostatic interactions in molecular modeling. Chemica Scripta 29A (1989) 139-144
    • (1989) Chemica Scripta , vol.29 A , pp. 139-144
    • Greengard, L.1    Rokhlin, V.2
  • 40
    • 0011668309 scopus 로고
    • On modeling hydrophobic interactions
    • Berne B.J., and Wallqvist A. On modeling hydrophobic interactions. Chemica Scripta 29A (1989) 85-91
    • (1989) Chemica Scripta , vol.29 A , pp. 85-91
    • Berne, B.J.1    Wallqvist, A.2
  • 41
    • 0026315121 scopus 로고
    • Electrostatic screening in molecular dynamics simulations
    • Solmajer T., and Mehler E.L. Electrostatic screening in molecular dynamics simulations. Protein Engng 4 8 (1991) 911-917
    • (1991) Protein Engng , vol.4 , Issue.8 , pp. 911-917
    • Solmajer, T.1    Mehler, E.L.2
  • 43
    • 0000910556 scopus 로고
    • Molecular dynamics of macromolecules in water
    • Levitt M. Molecular dynamics of macromolecules in water. Chemica Scripta 29A (1989) 197-203
    • (1989) Chemica Scripta , vol.29 A , pp. 197-203
    • Levitt, M.1
  • 44
    • 0026343488 scopus 로고
    • Conformational flexibility of aqueous monomeric and dimeric insulin: A molecular dynamics study
    • Mark A.E., Berendsen H.J.C., and van Gunsteren W.F. Conformational flexibility of aqueous monomeric and dimeric insulin: A molecular dynamics study. Biochemistry 30 (1991) 10866-10872
    • (1991) Biochemistry , vol.30 , pp. 10866-10872
    • Mark, A.E.1    Berendsen, H.J.C.2    van Gunsteren, W.F.3
  • 45
    • 0024578173 scopus 로고
    • Free energy via molecular simulation: Application to chemical and biomolecular systems
    • Beveridge D.L., and DiCapua F.M. Free energy via molecular simulation: Application to chemical and biomolecular systems. Ann Rev Biophys Biophys Chem 18 (1989) 431-492
    • (1989) Ann Rev Biophys Biophys Chem , vol.18 , pp. 431-492
    • Beveridge, D.L.1    DiCapua, F.M.2
  • 46
    • 0022816745 scopus 로고
    • The dielectric constant of a folded protein
    • Gilson M.K., and Honig B.H. The dielectric constant of a folded protein. Biopolymers 25 (1986) 2097-2119
    • (1986) Biopolymers , vol.25 , pp. 2097-2119
    • Gilson, M.K.1    Honig, B.H.2
  • 47
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B., and Richards F.M. The interpretation of protein structures: Estimation of static accessibility. J Mol Biol 55 (1971) 379-400
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 51
    • 33751552991 scopus 로고
    • Calculating total electrostatic energies with the nonlinear Poisson-Boltzmann equation
    • Sharp K.A., and Honig B. Calculating total electrostatic energies with the nonlinear Poisson-Boltzmann equation. J Phys Chem 94 (1990) 7648-7692
    • (1990) J Phys Chem , vol.94 , pp. 7648-7692
    • Sharp, K.A.1    Honig, B.2
  • 52
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free energies using macroscopic solvent methods
    • Sitkoff D., Sharp K.A., and Honig B. Accurate calculation of hydration free energies using macroscopic solvent methods. J Phys Chem 98 (1994) 1978-1988
    • (1994) J Phys Chem , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 53
    • 0028334097 scopus 로고
    • Decomposition of the free energy of a system in terms of specific interactions
    • Mark A.E., and van Gunsteren W.F. Decomposition of the free energy of a system in terms of specific interactions. J Mol Biol 240 (1994) 167-176
    • (1994) J Mol Biol , vol.240 , pp. 167-176
    • Mark, A.E.1    van Gunsteren, W.F.2
  • 56
    • 0015520587 scopus 로고
    • The interpretation of protein titration curves
    • Tanford C., and Roxby R. The interpretation of protein titration curves. Application to lysozyme. Biochemistry 11 11 (1972) 2192-2198
    • (1972) Application to lysozyme. Biochemistry , vol.11 , Issue.11 , pp. 2192-2198
    • Tanford, C.1    Roxby, R.2
  • 58
    • 0000501485 scopus 로고
    • A model for electrostatic effects in proteins
    • States D.J., and Karplus M. A model for electrostatic effects in proteins. J Mol Biol 197 (1987) 122-130
    • (1987) J Mol Biol , vol.197 , pp. 122-130
    • States, D.J.1    Karplus, M.2
  • 59
    • 0020475509 scopus 로고
    • Calculation of the electric potential in the active site cleft due to alphahelix dipoles
    • Warwicker J., and Watson H.C. Calculation of the electric potential in the active site cleft due to alphahelix dipoles. J Mol Biol 157 (1982) 671-679
    • (1982) J Mol Biol , vol.157 , pp. 671-679
    • Warwicker, J.1    Watson, H.C.2
  • 60
    • 0023054659 scopus 로고
    • Continuum dieletric modelling of the protein-solvent system, and calculation of the long-range electrostatic field of the enzyme phosphoglycerate mutase
    • Warwicker J. Continuum dieletric modelling of the protein-solvent system, and calculation of the long-range electrostatic field of the enzyme phosphoglycerate mutase. J Theor Biol 121 (1986) 199-210
    • (1986) J Theor Biol , vol.121 , pp. 199-210
    • Warwicker, J.1
  • 61
    • 0022964504 scopus 로고
    • Focusing of electrostatic fields in the active site of Cu-Zn superoxide Dismutase: effects of ionic strength and amino acid modification
    • Klapper I., Hagstrom R., Fine R., Sharp K., and Honig B. Focusing of electrostatic fields in the active site of Cu-Zn superoxide Dismutase: effects of ionic strength and amino acid modification. Proteins 1 (1986) 47-56
    • (1986) Proteins , vol.1 , pp. 47-56
    • Klapper, I.1    Hagstrom, R.2    Fine, R.3    Sharp, K.4    Honig, B.5
  • 62
    • 0024580271 scopus 로고
    • The electrostatic potential of DNA
    • Jayaram B., Sharp K., and Honig B. The electrostatic potential of DNA. Biopolymers 28 (1989) 975-993
    • (1989) Biopolymers , vol.28 , pp. 975-993
    • Jayaram, B.1    Sharp, K.2    Honig, B.3
  • 63
    • 0017608499 scopus 로고
    • Direct solution of the Poisson equation for biomolecules of arbitray shape, polarizability density and charge distribution
    • Orttung W.H. Direct solution of the Poisson equation for biomolecules of arbitray shape, polarizability density and charge distribution. Ann NY Acad Sci 303 (1977) 22-37
    • (1977) Ann NY Acad Sci , vol.303 , pp. 22-37
    • Orttung, W.H.1
  • 64
    • 0022429751 scopus 로고
    • A new method for computing the macromolecular electric potential
    • Zauhar R.J., and Morgan R.S. A new method for computing the macromolecular electric potential. J Mol Biol 186 (1985) 815-820
    • (1985) J Mol Biol , vol.186 , pp. 815-820
    • Zauhar, R.J.1    Morgan, R.S.2
  • 65
    • 84988110397 scopus 로고
    • The rigorous computation of the molecular electric potential
    • Zauhar R.J., and Morgan R.S. The rigorous computation of the molecular electric potential. J Comput Chem 9 2 (1988) 171-187
    • (1988) J Comput Chem , vol.9 , Issue.2 , pp. 171-187
    • Zauhar, R.J.1    Morgan, R.S.2
  • 66
    • 0027254625 scopus 로고
    • Boundary element solution of macromolecular electrostatics: Interaction energy between two proteins
    • Zhou H.-X. Boundary element solution of macromolecular electrostatics: Interaction energy between two proteins. Biophys J 65 (1993) 955-963
    • (1993) Biophys J , vol.65 , pp. 955-963
    • Zhou, H.-X.1
  • 67
    • 84986524546 scopus 로고
    • Calculating electrostatic forces from grid-calculated potentials
    • Davis M.E., and McCammon J.A. Calculating electrostatic forces from grid-calculated potentials. J Comput Chem 11 (1990) 401-409
    • (1990) J Comput Chem , vol.11 , pp. 401-409
    • Davis, M.E.1    McCammon, J.A.2
  • 68
    • 0344778061 scopus 로고
    • Semianalytic treatment of solvation for molecular mechanics and dynamics
    • Still W.C., Tempczyk A., Hawley R.C., and Hendrickson T. Semianalytic treatment of solvation for molecular mechanics and dynamics. J Am Chem Soc 112 (1990) 6127-6129
    • (1990) J Am Chem Soc , vol.112 , pp. 6127-6129
    • Still, W.C.1    Tempczyk, A.2    Hawley, R.C.3    Hendrickson, T.4
  • 69
    • 84986528074 scopus 로고
    • The incorporation of hydration forces determined by continuum electrostatics into molecular mechanics simulations
    • Zauhar R.J. The incorporation of hydration forces determined by continuum electrostatics into molecular mechanics simulations. J Comput Chem 12 (1991) 575-583
    • (1991) J Comput Chem , vol.12 , pp. 575-583
    • Zauhar, R.J.1
  • 70
    • 84986430566 scopus 로고
    • Incorporating solvent and ion screening into molecular dynamics using the finite-difference Poisson-Boltzmann method
    • Sharp K. Incorporating solvent and ion screening into molecular dynamics using the finite-difference Poisson-Boltzmann method. J Comput Chem 12 4 (1991) 454-468
    • (1991) J Comput Chem , vol.12 , Issue.4 , pp. 454-468
    • Sharp, K.1
  • 71
    • 0026110673 scopus 로고
    • The inclusion of electrostatic hydration energies in molecular mechanics calculations
    • Gilson M.K., and Honig B. The inclusion of electrostatic hydration energies in molecular mechanics calculations. J Comput Aided Mol Des 5 (1991) 5-20
    • (1991) J Comput Aided Mol Des , vol.5 , pp. 5-20
    • Gilson, M.K.1    Honig, B.2
  • 72
    • 0000921135 scopus 로고
    • Molecular dynamics simulations in heterogeneous dielectrica and Debye-Hückel media: Application to the protein bovine pancreatic trypsin inhibitor
    • Niedermeier C., and Schulten K. Molecular dynamics simulations in heterogeneous dielectrica and Debye-Hückel media: Application to the protein bovine pancreatic trypsin inhibitor. Mol Simulation 8 (1992) 361-387
    • (1992) Mol Simulation , vol.8 , pp. 361-387
    • Niedermeier, C.1    Schulten, K.2
  • 73
    • 0001585447 scopus 로고
    • Computation of electrostatic forces on solvated molecules using the Poisson-Boltzmann equation
    • Gilson M.K., Davis M.E., Luty B.A., and McCammon J.A. 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
  • 74
    • 0028040064 scopus 로고
    • Evaluation of the conformational free energies of loops in proteins
    • Smith K.C., and Honig B. Evaluation of the conformational free energies of loops in proteins. Proteins 18 (1994) 119-132
    • (1994) Proteins , vol.18 , pp. 119-132
    • Smith, K.C.1    Honig, B.2
  • 75
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
    • Abagyan R., and Totrov M. Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins. J Mol Biol 235 (1994) 983-1002
    • (1994) J Mol Biol , vol.235 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 76
    • 0001205818 scopus 로고
    • Electrostatic effects in water-accessible regions of proteins
    • Mehler E.L., and Eichele G. Electrostatic effects in water-accessible regions of proteins. Biochemistry 23 (1984) 3887-3991
    • (1984) Biochemistry , vol.23 , pp. 3887-3991
    • Mehler, E.L.1    Eichele, G.2
  • 77
    • 0025197061 scopus 로고
    • a's of Ionizable Groups in Proteins: Atomic Detail from a Continuum Electrostatic Model
    • a's of Ionizable Groups in Proteins: Atomic Detail from a Continuum Electrostatic Model. Biochemistry 29 (1990) 10219-10225
    • (1990) Biochemistry , vol.29 , pp. 10219-10225
    • Bashford, D.1    Karplus, M.2
  • 78
    • 0027008756 scopus 로고
    • a, displacements at the active sites of FMN-depedent alpha-hydroxy acidoxidizing enzymes
    • a, displacements at the active sites of FMN-depedent alpha-hydroxy acidoxidizing enzymes. Protein Sci 1 (1992) 540-548
    • (1992) Protein Sci , vol.1 , pp. 540-548
    • Lederer, F.1
  • 80
    • 33751499830 scopus 로고
    • Multiple-site titration curves of proteins: An analysis of exact and approximate methods for their calculation
    • Bashford D., and Karplus M. Multiple-site titration curves of proteins: An analysis of exact and approximate methods for their calculation. J Phys Chem 95 (1991) 9561-9956
    • (1991) J Phys Chem , vol.95 , pp. 9561-9956
    • Bashford, D.1    Karplus, M.2
  • 82
    • 0027477251 scopus 로고
    • Multiple-site titration and molecular modeling: Two rapid methods for computing energies and forces for ionizable groups in proteins
    • Gilson M.K. Multiple-site titration and molecular modeling: Two rapid methods for computing energies and forces for ionizable groups in proteins. Proteins 15 (1993) 266-282
    • (1993) Proteins , vol.15 , pp. 266-282
    • Gilson, M.K.1
  • 83
    • 0026612756 scopus 로고
    • a, values of ionizable groups in bacteriorhodopsin
    • a, values of ionizable groups in bacteriorhodopsin. J Mol Biol 224 (1992) 473-486
    • (1992) J Mol Biol , vol.224 , pp. 473-486
    • Bashford, D.1    Gerwert, K.2
  • 84
    • 0024788820 scopus 로고
    • The nature of protein dipole moments, experimental and calculated permanent dipole of α-chymotrypsin
    • Antosiewicz J., and Porschke D. The nature of protein dipole moments, experimental and calculated permanent dipole of α-chymotrypsin. Biochemistry 28 (1989) 10072-10078
    • (1989) Biochemistry , vol.28 , pp. 10072-10078
    • Antosiewicz, J.1    Porschke, D.2
  • 85
    • 0026095641 scopus 로고
    • Protonation of interacting residues in a protein by a Monte Carlo method: application to lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides
    • Beroza P., Fredkin D.R., Okamura M.Y., and Feher G. Protonation of interacting residues in a protein by a Monte Carlo method: application to lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides. Proc Natl Acad Sci USA 88 (1991) 5804-5808
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5804-5808
    • Beroza, P.1    Fredkin, D.R.2    Okamura, M.Y.3    Feher, G.4
  • 91
    • 0024306320 scopus 로고
    • Molecular dynamics effects on protein electrostatics
    • Wendoloski J.J., and Matthew J.B. Molecular dynamics effects on protein electrostatics. Proteins 5 (1989) 313-321
    • (1989) Proteins , vol.5 , pp. 313-321
    • Wendoloski, J.J.1    Matthew, J.B.2
  • 92
    • 0026319199 scopus 로고
    • Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., and Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11 (1991) 281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 94
    • 0024706282 scopus 로고
    • Electrostatic fields in the active sites of lysozymes
    • Dao-Pin S., Liao D.-I., and Remington S.J. Electrostatic fields in the active sites of lysozymes. Proc Natl Acad Sci USA 86 (1989) 5361-5365
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5361-5365
    • Dao-Pin, S.1    Liao, D.-I.2    Remington, S.J.3
  • 97
    • 84988087911 scopus 로고
    • Calculating the electrostatic potential of proteins in solution: Method and error assessment
    • Gilson M.K., Sharp K.A., and Honig B. Calculating the electrostatic potential of proteins in solution: Method and error assessment. J Comput Chem 9 (1987) 327-335
    • (1987) J Comput Chem , vol.9 , pp. 327-335
    • Gilson, M.K.1    Sharp, K.A.2    Honig, B.3
  • 98
    • 84986486656 scopus 로고
    • A rapide finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls A., and Honig B. A rapide finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation. J Comput Chem 12 4 (1991) 435-445
    • (1991) J Comput Chem , vol.12 , Issue.4 , pp. 435-445
    • Nicholls, A.1    Honig, B.2
  • 99
    • 0023899747 scopus 로고
    • Energetics of charge-charge interactions in proteins
    • Gilson M.K., and Honig B. Energetics of charge-charge interactions in proteins. Proteins 3 (1988) 32-52
    • (1988) Proteins , vol.3 , pp. 32-52
    • Gilson, M.K.1    Honig, B.2
  • 101
    • 0023660015 scopus 로고
    • Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineering
    • Russell A.J., Thomas P.G., and Fersht A.R. Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineering. J Mol Biol 193 (1987) 803-813
    • (1987) J Mol Biol , vol.193 , pp. 803-813
    • Russell, A.J.1    Thomas, P.G.2    Fersht, A.R.3
  • 102
    • 0023280069 scopus 로고
    • Calculation of electrostatic potentials in an enzyme active site
    • Gilson M.K., and Honig B.H. Calculation of electrostatic potentials in an enzyme active site. Nature 330 (1987) 84-86
    • (1987) Nature , vol.330 , pp. 84-86
    • Gilson, M.K.1    Honig, B.H.2
  • 103
  • 105
    • 0015247070 scopus 로고
    • Hydrogen ion titration curve of lysozyme in 6 M guanidine hydrochloride
    • Roxby R., and Tanford C. Hydrogen ion titration curve of lysozyme in 6 M guanidine hydrochloride. Biochemistry 10 18 (1971) 3348-3352
    • (1971) Biochemistry , vol.10 , Issue.18 , pp. 3348-3352
    • Roxby, R.1    Tanford, C.2
  • 106
    • 33947465095 scopus 로고
    • The location of electrostatic charges in Kirkwood's model of organic ions
    • Tanford C. The location of electrostatic charges in Kirkwood's model of organic ions. J Am Chem Soc 79 (1957) 5348-5352
    • (1957) J Am Chem Soc , vol.79 , pp. 5348-5352
    • Tanford, C.1
  • 107
    • 0014938137 scopus 로고
    • Proton binding and dipole moment of hemoglobin Refined calculations
    • Orttung W.H. Proton binding and dipole moment of hemoglobin Refined calculations. Biochemistry 9 12 (1970) 2394-2402
    • (1970) Biochemistry , vol.9 , Issue.12 , pp. 2394-2402
    • Orttung, W.H.1
  • 111
    • 0018278646 scopus 로고
    • Proton nuclear magnetic ressonance study of histidine ionizations in myoglobin of various species
    • Botelho L.H., and Gurd F.R.N. Proton nuclear magnetic ressonance study of histidine ionizations in myoglobin of various species. Specific assignement of individual resonances. Biochemistry 17 24 (1978) 5188-5196
    • (1978) Specific assignement of individual resonances. Biochemistry , vol.17 , Issue.24 , pp. 5188-5196
    • Botelho, L.H.1    Gurd, F.R.N.2
  • 113
    • 0018749496 scopus 로고
    • Electrostatic effects in hemoglobin: Hydrogen ion equilibria in human deoxy-and oxyhemoglobin A
    • Matthew J.B., Hanania G.I.H., and Gurd F.R.N. Electrostatic effects in hemoglobin: Hydrogen ion equilibria in human deoxy-and oxyhemoglobin A. Biochemistry 18 10 (1979) 1919-1928
    • (1979) Biochemistry , vol.18 , Issue.10 , pp. 1919-1928
    • Matthew, J.B.1    Hanania, G.I.H.2    Gurd, F.R.N.3
  • 114
    • 0018356978 scopus 로고
    • Electrostatic effects in hemoglobin: Bohr effect and ionic strength dependence of individual groups
    • Matthew J.B., Hanania G.I., and Gurd F.R.N. Electrostatic effects in hemoglobin: Bohr effect and ionic strength dependence of individual groups. Biochemistry 18 10 (1979) 1928-1936
    • (1979) Biochemistry , vol.18 , Issue.10 , pp. 1928-1936
    • Matthew, J.B.1    Hanania, G.I.2    Gurd, F.R.N.3
  • 115
    • 0023646694 scopus 로고
    • How much do we know about the bohr effect of hemoglobin?
    • Ho C., and Russu I.M. How much do we know about the bohr effect of hemoglobin?. Biochemistry 26 (1987) 6299-6305
    • (1987) Biochemistry , vol.26 , pp. 6299-6305
    • Ho, C.1    Russu, I.M.2
  • 117
    • 0023120307 scopus 로고
    • Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor
    • Wlodawer A., Deisenhofer J., and Huber H. Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor. J Mol Biol 193 (1987) 145-156
    • (1987) J Mol Biol , vol.193 , pp. 145-156
    • Wlodawer, A.1    Deisenhofer, J.2    Huber, H.3
  • 118
    • 0026795399 scopus 로고
    • Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures
    • Bemdt K.D., Güntert P., Orbons L.M., and Wüthrich K. Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures. J Mol Biol 227 (1992) 757-775
    • (1992) J Mol Biol , vol.227 , pp. 757-775
    • Bemdt, K.D.1    Güntert, P.2    Orbons, L.M.3    Wüthrich, K.4
  • 119
    • 0018782084 scopus 로고
    • Nuclear magnetic ressonance of labile proteins in the bovine trypsin pancreatic inhibitor
    • Wüthrich K., and Wagner G. Nuclear magnetic ressonance of labile proteins in the bovine trypsin pancreatic inhibitor. J Mol Biol 130 (1979) 1-18
    • (1979) J Mol Biol , vol.130 , pp. 1-18
    • Wüthrich, K.1    Wagner, G.2
  • 120
    • 0020481290 scopus 로고
    • Analysis of electrostatic interactions and their relationship to conformation and stability of bovine pancreatic trypsin inhibitor
    • Marsh K.L., Maskalik D., England R.D., Friend S.H., and Gurd F.R.N. Analysis of electrostatic interactions and their relationship to conformation and stability of bovine pancreatic trypsin inhibitor. Biochemistry 21 (1982) 5241-5251
    • (1982) Biochemistry , vol.21 , pp. 5241-5251
    • Marsh, K.L.1    Maskalik, D.2    England, R.D.3    Friend, S.H.4    Gurd, F.R.N.5
  • 121
    • 0024802754 scopus 로고
    • Electrostatic interactions in proteins: Calculations of the electrostatic term of free energy and the electrostatic potential field
    • Karshikov A.D., Engh R., Bode W., and Atanasov B.P. Electrostatic interactions in proteins: Calculations of the electrostatic term of free energy and the electrostatic potential field. Eur J Biophys 17 (1989) 287-297
    • (1989) Eur J Biophys , vol.17 , pp. 287-297
    • Karshikov, A.D.1    Engh, R.2    Bode, W.3    Atanasov, B.P.4
  • 123
    • 0021480222 scopus 로고
    • Macrospic models for studies of electrostatic interactions in proteins: Limitations and applicability
    • Warshel A., Russell S.T., and Churg A.K. Macrospic models for studies of electrostatic interactions in proteins: Limitations and applicability. Proc Natl Acad Sci USA 81 (1984) 4785-4789
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4785-4789
    • Warshel, A.1    Russell, S.T.2    Churg, A.K.3
  • 124
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill K.A. Dominant forces in protein folding. Biochemistry 29 31 (1990) 7133-7155
    • (1990) Biochemistry , vol.29 , Issue.31 , pp. 7133-7155
    • Dill, K.A.1
  • 125
    • 0021763134 scopus 로고
    • On the environment of ionizable groups in globular proteins
    • Rashin A.A., and Honig B. On the environment of ionizable groups in globular proteins. J Mol Biol 173 (1984) 515-521
    • (1984) J Mol Biol , vol.173 , pp. 515-521
    • Rashin, A.A.1    Honig, B.2
  • 126
    • 0021112481 scopus 로고
    • Ion-pairs in Proteins
    • Barlow D.J., and Thornton J.M. Ion-pairs in Proteins. J Mol Biol 168 (1983) 867-885
    • (1983) J Mol Biol , vol.168 , pp. 867-885
    • Barlow, D.J.1    Thornton, J.M.2
  • 127
    • 0020474627 scopus 로고
    • Effect on protein stability of reversing the charge of amino groups
    • Hollecker M., and Creighton T.E. Effect on protein stability of reversing the charge of amino groups. Biochem Biophys Acta 701 (1982) 395-404
    • (1982) Biochem Biophys Acta , vol.701 , pp. 395-404
    • Hollecker, M.1    Creighton, T.E.2
  • 128
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • Waldburguer C.D., Schildbach J.F., and Sauer R.T. Are buried salt bridges important for protein stability and conformational specificity?. Nature Struct Biol 2 2 (1995) 122-128
    • (1995) Nature Struct Biol , vol.2 , Issue.2 , pp. 122-128
    • Waldburguer, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 129
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch Z.S., and Tidor B. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci 3 (1994) 211-226
    • (1994) Protein Sci , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 131
    • 0025234587 scopus 로고
    • pH-induced denaturation of proteins: A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme
    • Anderson D.E., Becktel W.J., and Dahlquist F.W. pH-induced denaturation of proteins: A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry 29 (1990) 2403-2408
    • (1990) Biochemistry , vol.29 , pp. 2403-2408
    • Anderson, D.E.1    Becktel, W.J.2    Dahlquist, F.W.3
  • 132
    • 0025037308 scopus 로고
    • Effects of engineered salt bridges on the stability of subtilisin BPN
    • Erwin C.R., Barnett B.L., Oliver J.D., and Sullivan J.F. Effects of engineered salt bridges on the stability of subtilisin BPN. Protein Engng 4 1 (1990) 87-97
    • (1990) Protein Engng , vol.4 , Issue.1 , pp. 87-97
    • Erwin, C.R.1    Barnett, B.L.2    Oliver, J.D.3    Sullivan, J.F.4
  • 134
    • 0019837215 scopus 로고
    • Nature of the charged distributions in proteins
    • Wada A., and Nakamura H. Nature of the charged distributions in proteins. Nature 293 (1981) 757-758
    • (1981) Nature , vol.293 , pp. 757-758
    • Wada, A.1    Nakamura, H.2
  • 135
    • 0023779259 scopus 로고
    • Calculation of the total electrostatic energy of a macromolecular system: Solvation energies, binding energies, and conformational analysis
    • Gilson M.K., and Honig B. Calculation of the total electrostatic energy of a macromolecular system: Solvation energies, binding energies, and conformational analysis. Proteins 4 (1988) 7-18
    • (1988) Proteins , vol.4 , pp. 7-18
    • Gilson, M.K.1    Honig, B.2
  • 136
    • 0028929583 scopus 로고
    • Free energy balance in protein folding
    • Honig B., and Yang A.-S. Free energy balance in protein folding. Adv Protein Chem 46 (1995) 27-58
    • (1995) Adv Protein Chem , vol.46 , pp. 27-58
    • Honig, B.1    Yang, A.-S.2
  • 137
    • 0014718113 scopus 로고
    • Protein denaturation Part C
    • Tanford C. Protein denaturation Part C. Adv Protein Chem 25 (1970) 1-95
    • (1970) Adv Protein Chem , vol.25 , pp. 1-95
    • Tanford, C.1
  • 138
    • 0017058392 scopus 로고
    • Evolution of enzyme function and the development of catalytic efficiency
    • Albery J.W., and Knowles J.R. Evolution of enzyme function and the development of catalytic efficiency. Biochemistry 15 (1976) 5631-5640
    • (1976) Biochemistry , vol.15 , pp. 5631-5640
    • Albery, J.W.1    Knowles, J.R.2
  • 140
    • 0023364022 scopus 로고
    • Computer simulations of the diffusion of a substrate to an active site of an enzyme
    • Sharp K., Fine R., and Honig B. Computer simulations of the diffusion of a substrate to an active site of an enzyme. Science 236 (1987) 1460-1463
    • (1987) Science , vol.236 , pp. 1460-1463
    • Sharp, K.1    Fine, R.2    Honig, B.3
  • 141
    • 0023837924 scopus 로고
    • Simulation of the diffusion controlled reaction between superoxide and superoxide dismutase
    • Allison S.A., Bacquet R.J., and McCammon J.A. Simulation of the diffusion controlled reaction between superoxide and superoxide dismutase. II. Detailed models. Biopolymers 27 (1988) 251-269
    • (1988) II. Detailed models. Biopolymers , vol.27 , pp. 251-269
    • Allison, S.A.1    Bacquet, R.J.2    McCammon, J.A.3
  • 142
    • 33750652614 scopus 로고
    • Brownian dynamics with hydrodynamic interactions
    • Ermak D.L., and McCammon J.A. Brownian dynamics with hydrodynamic interactions. J Chem Phys 69 (1978) 1352-1360
    • (1978) J Chem Phys , vol.69 , pp. 1352-1360
    • Ermak, D.L.1    McCammon, J.A.2
  • 143
    • 0345108810 scopus 로고
    • Superperfect enzymes
    • McCammon J.A. Superperfect enzymes. Curr Biol 2 11 (1992) 585-586
    • (1992) Curr Biol , vol.2 , Issue.11 , pp. 585-586
    • McCammon, J.A.1
  • 145
    • 0000958642 scopus 로고
    • Brownian dynamics simulations of diffusional encounters between triose phosphate isomerase and glyceraldehyde phosphate: Electrostatic steering of glyceraldehyde phosphate
    • Luty B.A., Wade R.C., Madura J.D., Davis M.E., Briggs J.M., and McCammon J.A. Brownian dynamics simulations of diffusional encounters between triose phosphate isomerase and glyceraldehyde phosphate: Electrostatic steering of glyceraldehyde phosphate. J Phys Chem 97 (1993) 233-237
    • (1993) J Phys Chem , vol.97 , pp. 233-237
    • Luty, B.A.1    Wade, R.C.2    Madura, J.D.3    Davis, M.E.4    Briggs, J.M.5    McCammon, J.A.6
  • 146
    • 0027446430 scopus 로고
    • Gating of the active site of triose phosphate isomerase: Brownian dynamics simulation of flexible peptide loops in the enzyme
    • Wade R.C., Davis M.E., Luty B.A., Madura J.D., and McCammon J.A. Gating of the active site of triose phosphate isomerase: Brownian dynamics simulation of flexible peptide loops in the enzyme. Biophys J 64 (1993) 9-15
    • (1993) Biophys J , vol.64 , pp. 9-15
    • Wade, R.C.1    Davis, M.E.2    Luty, B.A.3    Madura, J.D.4    McCammon, J.A.5
  • 147
    • 0024280501 scopus 로고
    • Dissecting the catalytic triad of a serine protease
    • Carter P., and Wells J.A. Dissecting the catalytic triad of a serine protease. Nature 332 6164 (1988) 564-568
    • (1988) Nature , vol.332 , Issue.6164 , pp. 564-568
    • Carter, P.1    Wells, J.A.2
  • 148
    • 0021978310 scopus 로고
    • The role of the alpha-helix dipole in protein function and structure
    • Hol W.J. The role of the alpha-helix dipole in protein function and structure. Prog Biophys Mol Biol 45 (1985) 149-195
    • (1985) Prog Biophys Mol Biol , vol.45 , pp. 149-195
    • Hol, W.J.1
  • 149
    • 0025763437 scopus 로고
    • Enzyme catalysis: not different, just better
    • Knowles J.R. Enzyme catalysis: not different, just better. Nature 350 (1991) 121-124
    • (1991) Nature , vol.350 , pp. 121-124
    • Knowles, J.R.1
  • 150
    • 0022174926 scopus 로고
    • Liquid-liquid extraction of biopolymers
    • Cooney C.L., and Humphrey A.E. (Eds), Pergamon Press, London
    • Kula M.R. Liquid-liquid extraction of biopolymers. In: Cooney C.L., and Humphrey A.E. (Eds). Comprehensive Biotechnology, vol 2 (1979), Pergamon Press, London 451-470
    • (1979) Comprehensive Biotechnology, vol 2 , pp. 451-470
    • Kula, M.R.1
  • 151
    • 0037872416 scopus 로고
    • Reversed micelles in liquid-liquid extraction
    • Kennedy J.F., and Cabral J.M.S. (Eds), Wiley, London
    • Cabral J.M.S., and Aires-Barros M.R. Reversed micelles in liquid-liquid extraction. In: Kennedy J.F., and Cabral J.M.S. (Eds). Recovery Processes for Biological Materials (1993), Wiley, London 247-271
    • (1993) Recovery Processes for Biological Materials , pp. 247-271
    • Cabral, J.M.S.1    Aires-Barros, M.R.2
  • 152
    • 0022031519 scopus 로고
    • Protein extraction using reverse micelles
    • Gocklen K.E., and Hatton T.A. Protein extraction using reverse micelles. Biotechnol Progr 1 (1985) 69-74
    • (1985) Biotechnol Progr , vol.1 , pp. 69-74
    • Gocklen, K.E.1    Hatton, T.A.2
  • 154
  • 155
    • 0028282819 scopus 로고
    • Predicting partition coefficients of multi-charged solutes in aqueous two-phase systems
    • Eiteman M.A. Predicting partition coefficients of multi-charged solutes in aqueous two-phase systems. J Chromatogr A 668 (1994) 21-30
    • (1994) J Chromatogr A , vol.668 , pp. 21-30
    • Eiteman, M.A.1
  • 156
    • 0026281150 scopus 로고
    • A model for the prediction of partition coefficients in aqueous two-phase systems
    • Eiteman M.A., and Gainer J.L. A model for the prediction of partition coefficients in aqueous two-phase systems. Bioseparation 2 (1991) 31-41
    • (1991) Bioseparation , vol.2 , pp. 31-41
    • Eiteman, M.A.1    Gainer, J.L.2
  • 158
    • 12244263676 scopus 로고
    • Density functional theory for the solid alkali cyanides
    • LeSar R., and Gordon R.G. Density functional theory for the solid alkali cyanides. J Chem Phys 77 (1982) 3682-3692
    • (1982) J Chem Phys , vol.77 , pp. 3682-3692
    • LeSar, R.1    Gordon, R.G.2
  • 159
    • 4243606192 scopus 로고
    • Unified approach for molecular dynamics and density functional theory
    • Car R., and Parrinelo M. Unified approach for molecular dynamics and density functional theory. Phys Rev Lett 55 (1985) 2471-2474
    • (1985) Phys Rev Lett , vol.55 , pp. 2471-2474
    • Car, R.1    Parrinelo, M.2
  • 160
    • 0000709802 scopus 로고
    • The inducible multipole solvation method: A new model for solvation effects on solute electrostatics
    • Davis M.E. The inducible multipole solvation method: A new model for solvation effects on solute electrostatics. J Chem Phys 7 (1994) 5149-5159
    • (1994) J Chem Phys , vol.7 , pp. 5149-5159
    • Davis, M.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.