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Volumn 89, Issue 2, 2005, Pages 768-781

Molecular dynamics of a protein surface: Ion-residues interactions

Author keywords

[No Author keywords available]

Indexed keywords

CHLORIDE ION; PROTEIN S6; RIBOSOME PROTEIN; SODIUM ION;

EID: 23244452408     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.058917     Document Type: Article
Times cited : (63)

References (122)
  • 1
    • 0001549718 scopus 로고
    • Protein hydration and behavior; many aspects of protein behavior can be interpreted in terms of frozen water of hydration
    • Klotz, I. M. 1958. Protein hydration and behavior; many aspects of protein behavior can be interpreted in terms of frozen water of hydration. Science. 128:815-822.
    • (1958) Science , vol.128 , pp. 815-822
    • Klotz, I.M.1
  • 2
    • 0014674115 scopus 로고
    • Extension of the theory of linked functions to incorporate the effects of protein hydration
    • Tanford, C. 1969. Extension of the theory of linked functions to incorporate the effects of protein hydration. J. Mol. Biol. 39:539-544.
    • (1969) J. Mol. Biol. , vol.39 , pp. 539-544
    • Tanford, C.1
  • 3
  • 4
    • 0000807992 scopus 로고
    • Protein-water interaction studied by solvent 1H, 2H, and 170 magnetic relaxation
    • Koenig, S. H., K. Hallenga, and M. Shporer. 1975. Protein-water interaction studied by solvent 1H, 2H, and 170 magnetic relaxation. Proc. Natl. Acad. Sci. USA. 72:2667-2671.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 2667-2671
    • Koenig, S.H.1    Hallenga, K.2    Shporer, M.3
  • 5
    • 0018356110 scopus 로고
    • Protein-water interactions. Heat capacity of the lysozyme-water system
    • Yang, P. H., and J. A. Rupley. 1979. Protein-water interactions. Heat capacity of the lysozyme-water system. Biochemistry. 18:2654-2661.
    • (1979) Biochemistry , vol.18 , pp. 2654-2661
    • Yang, P.H.1    Rupley, J.A.2
  • 6
    • 0019160657 scopus 로고
    • The thermodynamics of water-protein interactions
    • Bryan, W. P. 1980. The thermodynamics of water-protein interactions. J. Theor. Biol. 87:639-661.
    • (1980) J. Theor. Biol. , vol.87 , pp. 639-661
    • Bryan, W.P.1
  • 7
    • 0025260385 scopus 로고
    • Excluded volume approximation to protein-solvent interaction. The solvent contact model
    • Colonna-Cesari, F., and C. Sander. 1990. Excluded volume approximation to protein-solvent interaction. The solvent contact model. Biophys. J. 57:1103-1107.
    • (1990) Biophys. J. , vol.57 , pp. 1103-1107
    • Colonna-Cesari, F.1    Sander, C.2
  • 8
    • 0026326956 scopus 로고
    • Protein hydration in aqueous solution
    • Otting, G., E. Liepinsh, and K. Wuthrich. 1991. Protein hydration in aqueous solution. Science. 254:974-980.
    • (1991) Science , vol.254 , pp. 974-980
    • Otting, G.1    Liepinsh, E.2    Wuthrich, K.3
  • 9
    • 0026193384 scopus 로고
    • Protein hydration studied with homonuclear 3D 1H NMR experiments
    • Otting, G., E. Liepinsh, B. T. Farmer 2nd, and K. Wuthrich. 1991. Protein hydration studied with homonuclear 3D 1H NMR experiments. J. Biomol. NMR. 1:209-215.
    • (1991) J. Biomol. NMR , vol.1 , pp. 209-215
    • Otting, G.1    Liepinsh, E.2    Farmer II, B.T.3    Wuthrich, K.4
  • 10
    • 0027431378 scopus 로고
    • Protein hydration elucidated by molecular dynamics simulation
    • Steinbach, P. J., and B. R. Brooks. 1993. Protein hydration elucidated by molecular dynamics simulation. Proc. Natl. Acad. Sci. USA. 90:9135-9139.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9135-9139
    • Steinbach, P.J.1    Brooks, B.R.2
  • 11
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures
    • Jiang, J. S., and A. T. Brunger. 1994. Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 243:100-115.
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.S.1    Brunger, A.T.2
  • 12
    • 0028670567 scopus 로고
    • Comparison of the three-dimensional molecular models of bovine submicellar caseins with small-angle X-ray scattering. Influence of protein hydration
    • Kumosinski, T. F., G. King, and H. M. Farrell, Jr. 1994. Comparison of the three-dimensional molecular models of bovine submicellar caseins with small-angle X-ray scattering. Influence of protein hydration. J. Protein Chem. 13:701-714.
    • (1994) J. Protein Chem. , vol.13 , pp. 701-714
    • Kumosinski, T.F.1    King, G.2    Farrell Jr., H.M.3
  • 13
    • 0029993330 scopus 로고    scopus 로고
    • On the sensitivity of MD trajectories to changes in water-protein interaction parameters: The potato carboxypeptidase inhibitor in water as a test case for the GROMOS force field
    • Daura, X., B. Oliva, E. Querol, F. X. Aviles, and O. Tapia. 1996. On the sensitivity of MD trajectories to changes in water-protein interaction parameters: the potato carboxypeptidase inhibitor in water as a test case for the GROMOS force field. Proteins. 25:89-103.
    • (1996) Proteins , vol.25 , pp. 89-103
    • Daura, X.1    Oliva, B.2    Querol, E.3    Aviles, F.X.4    Tapia, O.5
  • 14
    • 0030325741 scopus 로고    scopus 로고
    • Protein hydration dynamics in aqueous solution
    • Denisov, V. P., and B. Halle. 1996. Protein hydration dynamics in aqueous solution. Faraday Discuss. 103:227-244.
    • (1996) Faraday Discuss. , vol.103 , pp. 227-244
    • Denisov, V.P.1    Halle, B.2
  • 15
    • 0031762253 scopus 로고    scopus 로고
    • Cluster analysis of consensus water sites in thrombin and trypsin shows conservation between serine proteases and contributions to ligand specificity
    • Sanschagrin, P. C., and L. A. Kuhn. 1998. Cluster analysis of consensus water sites in thrombin and trypsin shows conservation between serine proteases and contributions to ligand specificity. Protein Sci. 7:2054-2064.
    • (1998) Protein Sci. , vol.7 , pp. 2054-2064
    • Sanschagrin, P.C.1    Kuhn, L.A.2
  • 17
    • 0033069433 scopus 로고    scopus 로고
    • Editing of chemical exchange-relayed NOEs in NMR experiments for the observation of protein-water interactions
    • Melacini, G., R. Kaptein, and R. Boelens. 1999. Editing of chemical exchange-relayed NOEs in NMR experiments for the observation of protein-water interactions. J. Magn. Reson. 136:214-218.
    • (1999) J. Magn. Reson. , vol.136 , pp. 214-218
    • Melacini, G.1    Kaptein, R.2    Boelens, R.3
  • 18
    • 0032790344 scopus 로고    scopus 로고
    • Accessibility and order of water sites in and around proteins: A crystallographic time-averaging study
    • Schiffer, C. A., and W. F. van Gunsteren. 1999. Accessibility and order of water sites in and around proteins: a crystallographic time-averaging study. Proteins. 36:501-511.
    • (1999) Proteins , vol.36 , pp. 501-511
    • Schiffer, C.A.1    Van Gunsteren, W.F.2
  • 19
    • 0033637521 scopus 로고    scopus 로고
    • The dynamics of protein hydration water: A quantitative comparison of molecular dynamics simulations and neutron-scattering experiments
    • Tarek, M., and D. J. Tobias. 2000. The dynamics of protein hydration water: a quantitative comparison of molecular dynamics simulations and neutron-scattering experiments. Biophys. J. 79:3244-3257.
    • (2000) Biophys. J. , vol.79 , pp. 3244-3257
    • Tarek, M.1    Tobias, D.J.2
  • 20
    • 0035965870 scopus 로고    scopus 로고
    • A unified picture of protein hydration: Prediction of hydrodynamic properties from known structures
    • Zhou, H. X. 2001. A unified picture of protein hydration: prediction of hydrodynamic properties from known structures. Biophys. Chem. 93:171-179.
    • (2001) Biophys. Chem. , vol.93 , pp. 171-179
    • Zhou, H.X.1
  • 22
    • 0037110473 scopus 로고    scopus 로고
    • Hydration structure of human lysozyme investigated by molecular dynamics simulation and cryogenic X-ray crystal structure analyses: On the correlation between crystal water sites, solvent density, and solvent dipole
    • Higo, J., and M. Nakasako. 2002. Hydration structure of human lysozyme investigated by molecular dynamics simulation and cryogenic X-ray crystal structure analyses: on the correlation between crystal water sites, solvent density, and solvent dipole. J. Comput. Chem. 23:1323-1336.
    • (2002) J. Comput. Chem. , vol.23 , pp. 1323-1336
    • Higo, J.1    Nakasako, M.2
  • 23
    • 0036836450 scopus 로고    scopus 로고
    • Protein hydration water: Structure and thermodynamics
    • Smith, J. C., F. Merzel, C. S. Verma, and S. Fischer. 2002. Protein hydration water: structure and thermodynamics. J. Mol. Liq. 101:27-33.
    • (2002) J. Mol. Liq. , vol.101 , pp. 27-33
    • Smith, J.C.1    Merzel, F.2    Verma, C.S.3    Fischer, S.4
  • 24
    • 85035242434 scopus 로고    scopus 로고
    • Structure, dynamics, and energetics of water at the surface of a small globular protein: A molecular dynamics simulation
    • Dastidar, S. G., and C. Mukhopadhyay. 2003. Structure, dynamics, and energetics of water at the surface of a small globular protein: A molecular dynamics simulation. Phys. Rev. E. Stat. Nonlin. Soft Matter Phys. 68:02921-02925.
    • (2003) Phys. Rev. E. Stat. Nonlin. Soft Matter Phys. , vol.68 , pp. 2921-2925
    • Dastidar, S.G.1    Mukhopadhyay, C.2
  • 26
    • 2542633488 scopus 로고    scopus 로고
    • Protein-water interactions in ribonuclease a and angiogenin: A molecular dynamics study
    • Sanjeev, B. S., and S. Vishveshwara. 2004. Protein-water interactions in ribonuclease A and angiogenin: a molecular dynamics study. Proteins. 55:915-923.
    • (2004) Proteins , vol.55 , pp. 915-923
    • Sanjeev, B.S.1    Vishveshwara, S.2
  • 27
    • 0037019460 scopus 로고    scopus 로고
    • Molecular dynamics of water at the protein-solvent interface
    • Bizzarri, A. R., and S. Cannistraro. 2002. Molecular dynamics of water at the protein-solvent interface. J. Phys. Chem. B. 106:6617-6633.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 6617-6633
    • Bizzarri, A.R.1    Cannistraro, S.2
  • 28
    • 0036286851 scopus 로고    scopus 로고
    • Solvation and hydration of proteins and nucleic acids: A theoretical view of simulation and experiment
    • Makarov, V., B. M. Pettitt, and M. Feig. 2002. Solvation and hydration of proteins and nucleic acids: a theoretical view of simulation and experiment. Acc. Chem. Res. 35:376-384.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 376-384
    • Makarov, V.1    Pettitt, B.M.2    Feig, M.3
  • 29
    • 2342527858 scopus 로고    scopus 로고
    • Dynamics of water in biological recognition
    • Pal, S. K., and A. H. Zewail. 2004. Dynamics of water in biological recognition. Chem. Rev. 104:2099-2123.
    • (2004) Chem. Rev. , vol.104 , pp. 2099-2123
    • Pal, S.K.1    Zewail, A.H.2
  • 30
    • 0032484699 scopus 로고    scopus 로고
    • Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes
    • Curtis, R. A., J. M. Prausnitz, and H. W. Blanch. 1998. Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes. Biotechnol. Bioeng. 57:11-21.
    • (1998) Biotechnol. Bioeng. , vol.57 , pp. 11-21
    • Curtis, R.A.1    Prausnitz, J.M.2    Blanch, H.W.3
  • 31
    • 0034615759 scopus 로고    scopus 로고
    • Structure of the S15, S6, S18-rRNA complex: Assembly of the 30S ribosome central domain
    • Agalarov, S. C., G. S. Prasad, P. M. Funke, C. D. Stout, and J. R. Williamson. 2000. Structure of the S15, S6, S18-rRNA complex: assembly of the 30S ribosome central domain. Science. 288:107-112.
    • (2000) Science , vol.288 , pp. 107-112
    • Agalarov, S.C.1    Prasad, G.S.2    Funke, P.M.3    Stout, C.D.4    Williamson, J.R.5
  • 32
    • 0036212691 scopus 로고    scopus 로고
    • Molecular dynamics simulation of dipalmitoylphosphatidylserine bilayer with Na+ counterions
    • Pandit, S. A., and M. L. Berkowitz. 2002. Molecular dynamics simulation of dipalmitoylphosphatidylserine bilayer with Na+ counterions. Biophys. J. 82:1818-1827.
    • (2002) Biophys. J. , vol.82 , pp. 1818-1827
    • Pandit, S.A.1    Berkowitz, M.L.2
  • 33
    • 0037678992 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a dipalmitoylphosphatidylcholine bilayer with NaCl
    • Pandit, S. A., D. Bostic, and M. L. Berkowitz. 2003. Molecular dynamics simulation of a dipalmitoylphosphatidylcholine bilayer with NaCl. Biophys. J. 84:3743-3750.
    • (2003) Biophys. J. , vol.84 , pp. 3743-3750
    • Pandit, S.A.1    Bostic, D.2    Berkowitz, M.L.3
  • 34
    • 0242290834 scopus 로고    scopus 로고
    • Mixed bilayer containing dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylserine: Lipid complexation, ion binding, and electrostatics
    • Pandit, S. A., D. Bostick, and M. L. Berkowitz. 2003. Mixed bilayer containing dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylserine: lipid complexation, ion binding, and electrostatics. Biophys. J. 85:3120-3131.
    • (2003) Biophys. J. , vol.85 , pp. 3120-3131
    • Pandit, S.A.1    Bostick, D.2    Berkowitz, M.L.3
  • 35
    • 1542285301 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a palmitoyl-oleoyl phosphatidylserine bilayer with Na+ counterions and NaCl
    • Mukhopadhyay, P., L. Monticelli, and D. P. Tieleman. 2004. Molecular dynamics simulation of a palmitoyl-oleoyl phosphatidylserine bilayer with Na+ counterions and NaCl. Biophys. J. 86:1601-1609.
    • (2004) Biophys. J. , vol.86 , pp. 1601-1609
    • Mukhopadhyay, P.1    Monticelli, L.2    Tieleman, D.P.3
  • 36
    • 0001651751 scopus 로고
    • Effects of salt on the structure and dynamics of the bis(penicillamine) enkephalin zwitterion: A simulation study
    • Smith, P. E., and B. M. Pettitt. 1991. Effects of salt on the structure and dynamics of the bis(penicillamine) enkephalin zwitterion: a simulation study. J. Am. Chem. Soc. 113:6029-6037.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 6029-6037
    • Smith, P.E.1    Pettitt, B.M.2
  • 37
    • 0027272972 scopus 로고
    • Peptides in ionic-solutions: A simulation study of a bis(penicillamine) enkephalin in sodium-acetate solution
    • Smith, P. E., G. E. Marlow, and B. M. Pettitt. 1993. Peptides in ionic-solutions: a simulation study of a bis(penicillamine) enkephalin in sodium-acetate solution. J. Am. Chem. Soc. 115:7493-7498.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7493-7498
    • Smith, P.E.1    Marlow, G.E.2    Pettitt, B.M.3
  • 38
    • 0034864646 scopus 로고    scopus 로고
    • Simulations of the bis-penicillamine enkephalin in sodium chloride solution: A parameter study
    • Marlow, G. E., and B. M. Pettitt. 2001. Simulations of the bis-penicillamine enkephalin in sodium chloride solution: a parameter study. Biopolymers. 60:134-152.
    • (2001) Biopolymers , vol.60 , pp. 134-152
    • Marlow, G.E.1    Pettitt, B.M.2
  • 39
    • 0037323197 scopus 로고    scopus 로고
    • Simulation of the bis(penicillamine) enkephalin in ammonium chloride solution: A comparison with sodium chloride
    • Marlow, G. E., and B. M. Pettitt. 2003. Simulation of the bis(penicillamine) enkephalin in ammonium chloride solution: a comparison with sodium chloride. Biopolymers. 68:192-209.
    • (2003) Biopolymers , vol.68 , pp. 192-209
    • Marlow, G.E.1    Pettitt, B.M.2
  • 40
    • 0019729290 scopus 로고
    • Quantum chemical studies of proton transport through biomembranes
    • Scheiner, S. 1981. Quantum chemical studies of proton transport through biomembranes. Ann. N. Y. Acad. Sci. 367:493-509.
    • (1981) Ann. N. Y. Acad. Sci. , vol.367 , pp. 493-509
    • Scheiner, S.1
  • 41
    • 0020019479 scopus 로고
    • Kinetic studies of proton transfer in the microenvironment of a binding site
    • Gutman, M., D. Huppert, and E. Nachliel. 1982. Kinetic studies of proton transfer in the microenvironment of a binding site. Eur. J. Biochem. 121:637-642.
    • (1982) Eur. J. Biochem. , vol.121 , pp. 637-642
    • Gutman, M.1    Huppert, D.2    Nachliel, E.3
  • 42
    • 0025134851 scopus 로고
    • Pathway of proton transfer in bacterial reaction centers: Replacement of serine-L22 by alanine inhibits electron and proton transfers associated with reduction of quinone to dihydroquinone
    • Paddock, M. L., P. H. McPherson, G. Feher, and M. Y. Okamura. 1990. Pathway of proton transfer in bacterial reaction centers: replacement of serine-L22 by alanine inhibits electron and proton transfers associated with reduction of quinone to dihydroquinone. Proc. Natl. Acad. Sci. USA. 87:6803-6807.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6803-6807
    • Paddock, M.L.1    McPherson, P.H.2    Feher, G.3    Okamura, M.Y.4
  • 43
    • 0026612756 scopus 로고
    • Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin
    • Bashford, D., and K. Gerwert. 1992. Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin. J. Mol. Biol. 224:473-486.
    • (1992) J. Mol. Biol. , vol.224 , pp. 473-486
    • Bashford, D.1    Gerwert, K.2
  • 44
    • 0028314473 scopus 로고
    • Protonation and free energy changes associated with formation of QBH2 in native and Glu-L212→Gln mutant reaction centers from Rhodobacter sphaeroides
    • McPherson, P. H., M. Schonfeld, M. L. Paddock, M. Y. Okamura, and G. Feher. 1994. Protonation and free energy changes associated with formation of QBH2 in native and Glu-L212→Gln mutant reaction centers from Rhodobacter sphaeroides. Biochemistry. 33:1181-1193.
    • (1994) Biochemistry , vol.33 , pp. 1181-1193
    • McPherson, P.H.1    Schonfeld, M.2    Paddock, M.L.3    Okamura, M.Y.4    Feher, G.5
  • 45
    • 0028102402 scopus 로고
    • Proton migration along the membrane surface and retarded surface to bulk transfer
    • Heberle, J., J. Riesle, G. Thiedemann, D. Oesterhelt, and N. A. Dencher, 1994. Proton migration along the membrane surface and retarded surface to bulk transfer. Nature. 370:379-382.
    • (1994) Nature , vol.370 , pp. 379-382
    • Heberle, J.1    Riesle, J.2    Thiedemann, G.3    Oesterhelt, D.4    Dencher, N.A.5
  • 46
    • 0030566867 scopus 로고    scopus 로고
    • Kinetic isotope effects reveal an ice-like and a liquid-phase-type intramolecular proton transfer in bacteriorhodopsin
    • le Coutre, J., and K. Gerwert. 1996. Kinetic isotope effects reveal an ice-like and a liquid-phase-type intramolecular proton transfer in bacteriorhodopsin. FEBS Lett. 398:333-336.
    • (1996) FEBS Lett. , vol.398 , pp. 333-336
    • Le Coutre, J.1    Gerwert, K.2
  • 47
    • 0034789953 scopus 로고    scopus 로고
    • Time-resolved FT-IR spectroscopic investigation of the pH-dependent proton transfer reactions in the E194Q mutant of bacteriorhodopsin
    • Zscherp, C., R. Schlesinger, and J. Heberle. 2001. Time-resolved FT-IR spectroscopic investigation of the pH-dependent proton transfer reactions in the E194Q mutant of bacteriorhodopsin. Biochem. Biophys. Res. Commun. 283:57-63.
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 57-63
    • Zscherp, C.1    Schlesinger, R.2    Heberle, J.3
  • 48
    • 0346850017 scopus 로고    scopus 로고
    • Ion solvation thermodynamics from simulation with a polarizable force field
    • Grossfield, A., P. Ren, and J. W. Ponder. 2003. Ion solvation thermodynamics from simulation with a polarizable force field. J. Am. Chem. Soc. 125:15671-15682.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 15671-15682
    • Grossfield, A.1    Ren, P.2    Ponder, J.W.3
  • 49
    • 0021763983 scopus 로고
    • Kinetic analysis of proton transfer between reactants adsorbed to the same micelle. The effect of proximity on the rate constants
    • Nachliel, E., and M. Gutman. 1984. Kinetic analysis of proton transfer between reactants adsorbed to the same micelle. The effect of proximity on the rate constants. Eur. J. Biochem. 143:83-88.
    • (1984) Eur. J. Biochem. , vol.143 , pp. 83-88
    • Nachliel, E.1    Gutman, M.2
  • 50
    • 0023651499 scopus 로고
    • Time-resolved protonation dynamics of a black lipid membrane monitored by capacitative currents
    • Gutman, M., E. Nachliel, E. Bamberg, and B. Christensen. 1987. Time-resolved protonation dynamics of a black lipid membrane monitored by capacitative currents. Biochim. Biophys. Acta. 905:390-398.
    • (1987) Biochim. Biophys. Acta , vol.905 , pp. 390-398
    • Gutman, M.1    Nachliel, E.2    Bamberg, E.3    Christensen, B.4
  • 51
    • 0000308038 scopus 로고    scopus 로고
    • Time resolved dynamics of proton transfer in proteinous systems
    • Gutman, M., and E. Nachliel. 1997. Time resolved dynamics of proton transfer in proteinous systems. Annu. Rev. Phys. Chem. 48:329-356.
    • (1997) Annu. Rev. Phys. Chem. , vol.48 , pp. 329-356
    • Gutman, M.1    Nachliel, E.2
  • 52
    • 0035810447 scopus 로고    scopus 로고
    • Evidence for a continuous transition from nonadiabatic to adiabatic proton transfer dynamics in protic liquids
    • Cohen, B., and D. Huppert. 2001. Evidence for a continuous transition from nonadiabatic to adiabatic proton transfer dynamics in protic liquids. J. Phys. Chem. A. 105:2980-2988.
    • (2001) J. Phys. Chem. A , vol.105 , pp. 2980-2988
    • Cohen, B.1    Huppert, D.2
  • 53
    • 0000895102 scopus 로고
    • Excited state proton transfer
    • Weller, A. 1961. Excited state proton transfer. Prog. React. Kinet. 1:198-214.
    • (1961) Prog. React. Kinet. , vol.1 , pp. 198-214
    • Weller, A.1
  • 54
    • 0002087362 scopus 로고
    • Kinetics of proton transfer reaction involving hydroxypyrene-trisulfonate in aqueous solution by nanosecond laser absorption spectroscopy
    • Forster, T., and S. Volker. 1975. Kinetics of proton transfer reaction involving hydroxypyrene-trisulfonate in aqueous solution by nanosecond laser absorption spectroscopy. Chem. Phys. Lett. 34:1-5.
    • (1975) Chem. Phys. Lett. , vol.34 , pp. 1-5
    • Forster, T.1    Volker, S.2
  • 55
    • 0018330692 scopus 로고
    • Rapid pH and deltamuH+ jump by short laser pulse
    • Gutman, M., and D. Huppert. 1979. Rapid pH and deltamuH+ jump by short laser pulse. J. Biochem. Biophys. Methods. 1:9-19.
    • (1979) J. Biochem. Biophys. Methods , vol.1 , pp. 9-19
    • Gutman, M.1    Huppert, D.2
  • 56
    • 0001200730 scopus 로고    scopus 로고
    • Primary ultrafast events preceding the photoinduced proton transfer from pyranine to water
    • Tran-Thi, T. H., T. Gustavsson, C. Prayer, S. Pommeret, and J. T. Hynes. 2000. Primary ultrafast events preceding the photoinduced proton transfer from pyranine to water. Chem. Phys. Lett. 329:421-430.
    • (2000) Chem. Phys. Lett. , vol.329 , pp. 421-430
    • Tran-Thi, T.H.1    Gustavsson, T.2    Prayer, C.3    Pommeret, S.4    Hynes, J.T.5
  • 57
    • 0030665489 scopus 로고    scopus 로고
    • Mechanism of proton entry into the cytoplasmic section of the proton-conducting channel of bacteriorhodopsin
    • Checover, S., E. Nachliel, N. A. Dencher, and M. Gutman. 1997. Mechanism of proton entry into the cytoplasmic section of the proton-conducting channel of bacteriorhodopsin. Biochemistry. 36:13919-13928.
    • (1997) Biochemistry , vol.36 , pp. 13919-13928
    • Checover, S.1    Nachliel, E.2    Dencher, N.A.3    Gutman, M.4
  • 58
    • 0032555160 scopus 로고    scopus 로고
    • The proton collecting function of the inner surface of cytochrome C oxidase from Rhodobacter sphaeroides
    • Marantz, Y., E. Nachliel, A. Aagaard, P. Brzezinski, and M. Gutman. 1998. The proton collecting function of the inner surface of cytochrome C oxidase from Rhodobacter sphaeroides. Proc. Natl. Acad. Sci. USA. 95:8590-8595.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8590-8595
    • Marantz, Y.1    Nachliel, E.2    Aagaard, A.3    Brzezinski, P.4    Gutman, M.5
  • 59
    • 0035789518 scopus 로고    scopus 로고
    • Gromacs 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., B. Hess, and D. van der Spoel. 2001. Gromacs 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 7:306-317.
    • (2001) J. Mol. Model , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 62
    • 0027642798 scopus 로고
    • Molecular dynamics simulation of the stability of a 22 residue alpha-helix in water and 30% trifluoroethanol
    • van Buuren, A. R., and H. J. C. Berendsen. 1993. Molecular dynamics simulation of the stability of a 22 residue alpha-helix in water and 30% trifluoroethanol. Biopolymers. 33:1159-1166.
    • (1993) Biopolymers , vol.33 , pp. 1159-1166
    • Van Buuren, A.R.1    Berendsen, H.J.C.2
  • 63
    • 0011746241 scopus 로고
    • A molecular dynamics study of the decane/water interface
    • van Buuren, A. R., S. J. Marrink, and H. J. C. Berendsen. 1993. A molecular dynamics study of the decane/water interface. J. Phys. Chem. 97:9206-9212.
    • (1993) J. Phys. Chem. , vol.97 , pp. 9206-9212
    • Van Buuren, A.R.1    Marrink, S.J.2    Berendsen, H.J.C.3
  • 64
    • 0008025298 scopus 로고
    • Convergence properties of free energy calculations: Alpha-cyclodextrin complexes as a case study
    • Mark, A. E., S. P. van Helden, P. E. Smith, L. H. M. Janssen, and W, F. van Gunsteren. 1994. Convergence properties of free energy calculations: alpha-cyclodextrin complexes as a case study. J. Am. Chem. Soc. 116:6293-6302.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 6293-6302
    • Mark, A.E.1    Van Helden, S.P.2    Smith, P.E.3    Janssen, L.H.M.4    Van Gunsteren, W.F.5
  • 65
    • 0000454818 scopus 로고
    • A force field for liquid dimethyl sulfoxide and liquid properties of liquid dimethyl sulfoxide calculated using molecular dynamics simulation
    • Liu, H., F. Muller-Plathe, and W. F. van Gunsteren. 1995. A force field for liquid dimethyl sulfoxide and liquid properties of liquid dimethyl sulfoxide calculated using molecular dynamics simulation. J. Am. Chem. Soc. 117:4363-4366.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 4363-4366
    • Liu, H.1    Muller-Plathe, F.2    Van Gunsteren, W.F.3
  • 68
    • 15544371572 scopus 로고
    • Interaction models for water in relation to protein hydration
    • Berendsen, H. J. C., J. P. M. Postma, W. F. van Gunsteren, and J. Hermans. 1969. Interaction models for water in relation to protein hydration. Nature. 224:175-177.
    • (1969) Nature , vol.224 , pp. 175-177
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Van Gunsteren, W.F.3    Hermans, J.4
  • 69
    • 0030972502 scopus 로고    scopus 로고
    • Molecular dynamics simulations of Leu-enkephalin in water and DMSO
    • van der Spoel, D., and H. J. C. Berendsen. 1997. Molecular dynamics simulations of Leu-enkephalin in water and DMSO. Biophys. J. 72:2032-2041.
    • (1997) Biophys. J. , vol.72 , pp. 2032-2041
    • Van Der Spoel, D.1    Berendsen, H.J.C.2
  • 70
    • 0000112789 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fully hydrated dipalmitoylphosphatidylcholine bilayer with different macroscopic boundary conditions and parameters
    • Tieleman, D. P., and H. J. C. Berendsen. 1996. Molecular dynamics simulations of a fully hydrated dipalmitoylphosphatidylcholine bilayer with different macroscopic boundary conditions and parameters. J. Chem. Phys. 105:4871-4880.
    • (1996) J. Chem. Phys. , vol.105 , pp. 4871-4880
    • Tieleman, D.P.1    Berendsen, H.J.C.2
  • 72
    • 84986440341 scopus 로고
    • SETTLE: An analytical version of the SHAKE and RATTLE algorithms for rigid water models
    • Miyamoto, S., and P. A. Kollman. 1992. SETTLE: an analytical version of the SHAKE and RATTLE algorithms for rigid water models. J. Comput. Chem. 13:952-962.
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 74
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N-log(N) method for Ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle mesh Ewald: an N-log(N) method for Ewald sums in large systems. J. Chem. Phys. 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 75
    • 0026596911 scopus 로고
    • Calculations of antibody-antigen interactions: Microscopic and semi-microscopic evaluation of the free energies of binding of phosphorylcholine analogs to McPC603
    • Lee, F. S., Z. T. Chu, M. B. Bolger, and A. Warshel. 1992. Calculations of antibody-antigen interactions: microscopic and semi-microscopic evaluation of the free energies of binding of phosphorylcholine analogs to McPC603. Protein Eng. 5:215-228.
    • (1992) Protein Eng. , vol.5 , pp. 215-228
    • Lee, F.S.1    Chu, Z.T.2    Bolger, M.B.3    Warshel, A.4
  • 76
    • 0344418714 scopus 로고    scopus 로고
    • Simulating proton translocations in proteins: Probing proton transfer pathways in the Rhodobacter sphaeroides reaction center
    • Sham, Y. Y., I. Muegge, and A. Warshel. 1999. Simulating proton translocations in proteins: probing proton transfer pathways in the Rhodobacter sphaeroides reaction center. Proteins. 36:484-500.
    • (1999) Proteins , vol.36 , pp. 484-500
    • Sham, Y.Y.1    Muegge, I.2    Warshel, A.3
  • 77
    • 0342321950 scopus 로고    scopus 로고
    • Examining methods for calculations of binding free energies: LRA, LIE, PDLD-LRA, and PDLD/S-LRA calculations of ligands binding to an HIV protease
    • Sham, Y. Y., Z. T. Chu, H. Tao, and A. Warshel. 2000. Examining methods for calculations of binding free energies: LRA, LIE, PDLD-LRA, and PDLD/S-LRA calculations of ligands binding to an HIV protease. Proteins. 39:393-407.
    • (2000) Proteins , vol.39 , pp. 393-407
    • Sham, Y.Y.1    Chu, Z.T.2    Tao, H.3    Warshel, A.4
  • 78
    • 0035451052 scopus 로고    scopus 로고
    • What are the dielectric "constants" of proteins and how to validate electrostatic models?
    • Schutz, C. N., and A. Warshel. 2001. What are the dielectric "constants" of proteins and how to validate electrostatic models? Proteins. 44:400-417.
    • (2001) Proteins , vol.44 , pp. 400-417
    • Schutz, C.N.1    Warshel, A.2
  • 79
    • 0037093650 scopus 로고    scopus 로고
    • Simulations of ion current in realistic models of ion channels: The KcsA potassium channel
    • Burykin, A., C. N. Schutz, J. Villa, and A. Warshel. 2002. Simulations of ion current in realistic models of ion channels: the KcsA potassium channel. Proteins. 47:265-280.
    • (2002) Proteins , vol.47 , pp. 265-280
    • Burykin, A.1    Schutz, C.N.2    Villa, J.3    Warshel, A.4
  • 80
    • 0028155689 scopus 로고
    • New method for predicting binding-affinity in computer-aided drug design
    • Aqvist, J., C. Medina, and J. E. Samuelsson. 1994. New method for predicting binding-affinity in computer-aided drug design. Protein Eng. 7:385-391.
    • (1994) Protein Eng. , vol.7 , pp. 385-391
    • Aqvist, J.1    Medina, C.2    Samuelsson, J.E.3
  • 81
    • 0031637651 scopus 로고    scopus 로고
    • Ligand binding affinity prediction by linear interaction energy methods
    • Hansson, T., J. Marelius, and J. Aqvist. 1998. Ligand binding affinity prediction by linear interaction energy methods. J. Comput. Aided Mol. Des. 12:27-35.
    • (1998) J. Comput. Aided Mol. Des. , vol.12 , pp. 27-35
    • Hansson, T.1    Marelius, J.2    Aqvist, J.3
  • 82
    • 0035665229 scopus 로고    scopus 로고
    • The linear interaction energy method for predicting ligand binding free energies
    • Aqvist, J., and J. Marelius. 2001. The linear interaction energy method for predicting ligand binding free energies. Comb. Chem. High Throughput Screen. 4:613-626.
    • (2001) Comb. Chem. High Throughput Screen , vol.4 , pp. 613-626
    • Aqvist, J.1    Marelius, J.2
  • 83
    • 0036280661 scopus 로고    scopus 로고
    • Ligand binding affinities from MD simulations
    • Aqvist, J., V. B. Luzhkov, and B. O. Brandsdal. 2002. Ligand binding affinities from MD simulations. Acc. Chem. Res. 35:358-365.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 358-365
    • Aqvist, J.1    Luzhkov, V.B.2    Brandsdal, B.O.3
  • 84
    • 3042549928 scopus 로고    scopus 로고
    • Binding affinity prediction with different force fields: Examination of the linear interaction energy method
    • Almlof, M., B. O. Brandsdal, and J. Aqvist. 2004. Binding affinity prediction with different force fields: examination of the linear interaction energy method. J. Comput. Chem. 25:1242-1254.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1242-1254
    • Almlof, M.1    Brandsdal, B.O.2    Aqvist, J.3
  • 85
  • 86
    • 0037150088 scopus 로고    scopus 로고
    • Electrostatic interactions in an integral membrane protein
    • Johnson, E. T., and W. W. Parson. 2002. Electrostatic interactions in an integral membrane protein. Biochemistry. 41:6483-6494.
    • (2002) Biochemistry , vol.41 , pp. 6483-6494
    • Johnson, E.T.1    Parson, W.W.2
  • 87
    • 0021480222 scopus 로고
    • Macroscopic models for studies of electrostatic interactions in proteins: Limitations and applicability
    • Warshel, A., S. T. Russell, and A. K. Churg. 1984. Macroscopic models for studies of electrostatic interactions in proteins: limitations and applicability. Proc. Natl. Acad. Sci. USA. 81:4785-4789.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4785-4789
    • Warshel, A.1    Russell, S.T.2    Churg, A.K.3
  • 89
    • 0032190305 scopus 로고    scopus 로고
    • Analytical shape computation of macromolecules. I. Molecular area and volume through alpha shape
    • Liang, J., H. Edelsbrunner, P. Fu, P. V. Sudhakar, and S. Subramaniam. 1998. Analytical shape computation of macromolecules. I. Molecular area and volume through alpha shape. Proteins. 33:1-17.
    • (1998) Proteins , vol.33 , pp. 1-17
    • Liang, J.1    Edelsbrunner, H.2    Fu, P.3    Sudhakar, P.V.4    Subramaniam, S.5
  • 90
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and C. Sander. 1983. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 92
    • 0343614206 scopus 로고    scopus 로고
    • A systematic study of water models for molecular simulation: Derivation of water models optimized for use with a reaction field
    • van der Spoel, D., P. J. van Maaren, and H. J. C. Berendsen. 1998. A systematic study of water models for molecular simulation: derivation of water models optimized for use with a reaction field. J. Chem. Phys. 108:10220-10230.
    • (1998) J. Chem. Phys. , vol.108 , pp. 10220-10230
    • Van Der Spoel, D.1    Van Maaren, P.J.2    Berendsen, H.J.C.3
  • 94
    • 0000210446 scopus 로고
    • Elementary properties of ions in solution
    • Macmillan Education, Melbourne, Australia
    • Hille, B. 1984. Elementary properties of ions in solution. In Ion Channels of Excitable Membranes. 2nd Ed. Macmillan Education, Melbourne, Australia.
    • (1984) Ion Channels of Excitable Membranes. 2nd Ed.
    • Hille, B.1
  • 95
    • 0033135037 scopus 로고    scopus 로고
    • + ions on simulated structure and dynamics of betaARK1 PH domain
    • + ions on simulated structure and dynamics of betaARK1 PH domain. Proteins. 35:206-217.
    • (1999) Proteins , vol.35 , pp. 206-217
    • Pfeiffer, S.1    Fushman, D.2    Cowburn, D.3
  • 96
    • 0023792592 scopus 로고
    • Anion binding to neutral and positively charged lipid membranes
    • Macdonald, P. M., and J. Seelig. 1988. Anion binding to neutral and positively charged lipid membranes. Biochemistry. 27:6769-6775.
    • (1988) Biochemistry , vol.27 , pp. 6769-6775
    • Macdonald, P.M.1    Seelig, J.2
  • 97
    • 0031404601 scopus 로고    scopus 로고
    • A fast estimate of electrostatic group contributions to the free energy of protein-inhibitor binding
    • Muegge, I., H. Tao, and A. Warshel. 1997. A fast estimate of electrostatic group contributions to the free energy of protein-inhibitor binding. Protein Eng. 10:1363-1372.
    • (1997) Protein Eng. , vol.10 , pp. 1363-1372
    • Muegge, I.1    Tao, H.2    Warshel, A.3
  • 98
    • 0030584674 scopus 로고    scopus 로고
    • Electrostatic control of GTP and GDP binding in the oncoprotein p21(ras)
    • Muegge, I., T. Schweins, R. Langen, and A. Warshel. 1996. Electrostatic control of GTP and GDP binding in the oncoprotein p21(ras). Structure. 4:475-489.
    • (1996) Structure , vol.4 , pp. 475-489
    • Muegge, I.1    Schweins, T.2    Langen, R.3    Warshel, A.4
  • 100
    • 0031008575 scopus 로고    scopus 로고
    • On the calculation of binding free energies using continuum methods: Application to MHC class I protein-peptide interactions
    • Froloff, N., A. Windemuth, and B. Honig. 1997. On the calculation of binding free energies using continuum methods: application to MHC class I protein-peptide interactions. Protein Sci. 6:1293-1301.
    • (1997) Protein Sci. , vol.6 , pp. 1293-1301
    • Froloff, N.1    Windemuth, A.2    Honig, B.3
  • 101
    • 0024086838 scopus 로고
    • A theoretical study of the dielectric constant of protein
    • Nakamura, H., T. Sakamoto, and A. Wada. 1988. A theoretical study of the dielectric constant of protein. Protein Eng. 2:177-183.
    • (1988) Protein Eng. , vol.2 , pp. 177-183
    • Nakamura, H.1    Sakamoto, T.2    Wada, A.3
  • 102
    • 0026663131 scopus 로고
    • Quantitation of physical-chemical properties of the aqueous phase inside the phoE ionic channel
    • Gutman, M., Y. Tsfadia, A. Masad, and E. Nachliel. 1992. Quantitation of physical-chemical properties of the aqueous phase inside the phoE ionic channel. Biochim. Biophys. Acta. 1109:141-148.
    • (1992) Biochim. Biophys. Acta , vol.1109 , pp. 141-148
    • Gutman, M.1    Tsfadia, Y.2    Masad, A.3    Nachliel, E.4
  • 103
    • 0027464736 scopus 로고
    • Gaugement of the inner space of the apomyoglobin's heme binding site by a single free diffusing proton. II. Interaction with a bulk proton
    • Shimoni, E., E. Nachliel, and M. Gutman. 1993. Gaugement of the inner space of the apomyoglobin's heme binding site by a single free diffusing proton. II. Interaction with a bulk proton. Biophys. J. 64:480-483.
    • (1993) Biophys. J. , vol.64 , pp. 480-483
    • Shimoni, E.1    Nachliel, E.2    Gutman, M.3
  • 105
    • 0031577320 scopus 로고    scopus 로고
    • Calculation of the dielectric properties of a protein and its solvent: Theory and a case study
    • Loffler, G., H. Schreiber, and O. Steinhauser. 1997. Calculation of the dielectric properties of a protein and its solvent: theory and a case study. J. Mol. Biol. 270:520-534.
    • (1997) J. Mol. Biol. , vol.270 , pp. 520-534
    • Loffler, G.1    Schreiber, H.2    Steinhauser, O.3
  • 107
    • 0035112524 scopus 로고    scopus 로고
    • Time-resolved study of the inner space of lactose permease
    • Nachliel, E., N. Pollak, D. Huppert, and M. Gutman. 2001. Time-resolved study of the inner space of lactose permease. Biophys. J. 80:1498-1506.
    • (2001) Biophys. J. , vol.80 , pp. 1498-1506
    • Nachliel, E.1    Pollak, N.2    Huppert, D.3    Gutman, M.4
  • 108
    • 0141885306 scopus 로고    scopus 로고
    • Continuum electrostatic model for the binding of cytochrome c2 to the photosynthesis reaction center from Rhodobacter sphaeroides
    • Miyashita, O., J. N. Onuchic, and M. Y. Okamura. 2003. Continuum electrostatic model for the binding of cytochrome c2 to the photosynthesis reaction center from Rhodobacter sphaeroides. Biochemistry. 42:11651-11660.
    • (2003) Biochemistry , vol.42 , pp. 11651-11660
    • Miyashita, O.1    Onuchic, J.N.2    Okamura, M.Y.3
  • 109
    • 0021476470 scopus 로고
    • Calculations of electrostatic interactions in biological systems and in solutions
    • Warshel, A., and S. T. Russell. 1984. Calculations of electrostatic interactions in biological systems and in solutions. Q. Rev. Biophys. 17:283-422.
    • (1984) Q. Rev. Biophys. , vol.17 , pp. 283-422
    • Warshel, A.1    Russell, S.T.2
  • 110
    • 0010624785 scopus 로고    scopus 로고
    • The effect of protein relaxation on charge-charge interactions and dielectric constants of proteins
    • Sham, Y. Y., I. Muegge, and A. Warshel. 1998. The effect of protein relaxation on charge-charge interactions and dielectric constants of proteins. Biophys. J. 74:1744-1753.
    • (1998) Biophys. J. , vol.74 , pp. 1744-1753
    • Sham, Y.Y.1    Muegge, I.2    Warshel, A.3
  • 111
    • 4043057278 scopus 로고    scopus 로고
    • CHARMM fluctuating charge force field for proteins. II. Protein/solvent properties from molecular dynamics simulations using a nonadditive electrostatic model
    • Patel, S., A. D. Mackerell, Jr., and C. L. Brooks, 3rd. 2004. CHARMM fluctuating charge force field for proteins. II. Protein/solvent properties from molecular dynamics simulations using a nonadditive electrostatic model. J. Comput. Chem. 25:1504-1514.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1504-1514
    • Patel, S.1    Mackerell Jr., A.D.2    Brooks III, C.L.3
  • 112
    • 0036882094 scopus 로고    scopus 로고
    • Development of a polarizable force field for proteins via ab initio quantum chemistry: First generation model and gas phase tests
    • Kaminski, G. A., H. A. Stern, B. J. Berne, R. A. Friesner, Y. X. Cao, R. B. Murphy, R. Zhou, and T. A. Halgren. 2002. Development of a polarizable force field for proteins via ab initio quantum chemistry: first generation model and gas phase tests. J. Comput. Chem. 23:1515-1531.
    • (2002) J. Comput. Chem. , vol.23 , pp. 1515-1531
    • Kaminski, G.A.1    Stern, H.A.2    Berne, B.J.3    Friesner, R.A.4    Cao, Y.X.5    Murphy, R.B.6    Zhou, R.7    Halgren, T.A.8
  • 113
    • 0029308703 scopus 로고
    • Reactive uptake of C12(G) and Br2(G) by aqueous surfaces as a function of Br- and I-ion concentration: The effect of chemical-reaction at the interface
    • Hu, J. H., Q. Shi, P. Davidovits, D. R. Worsnop, M. S. Zahniser, and C. E. Kolb. 1995. Reactive uptake of C12(G) and Br2(G) by aqueous surfaces as a function of Br- and I-ion concentration: the effect of chemical-reaction at the interface. J. Phys. Chem. 99:8768-8776.
    • (1995) J. Phys. Chem. , vol.99 , pp. 8768-8776
    • Hu, J.H.1    Shi, Q.2    Davidovits, P.3    Worsnop, D.R.4    Zahniser, M.S.5    Kolb, C.E.6
  • 114
    • 0035525939 scopus 로고    scopus 로고
    • Molecular structure of salt solutions: A new view of the interface with implications for heterogeneous atmospheric chemistry
    • Jungwirth, P., and D. J. Tobias. 2001. Molecular structure of salt solutions: a new view of the interface with implications for heterogeneous atmospheric chemistry. J. Phys. Chem. B. 105:10468-10472.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 10468-10472
    • Jungwirth, P.1    Tobias, D.J.2
  • 115
    • 0037183043 scopus 로고    scopus 로고
    • Ions at the air/water interface
    • Jungwirth, P., and D. J. Tobias. 2002. Ions at the air/water interface. J. Phys. Chem. B. 106:6361-6373.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 6361-6373
    • Jungwirth, P.1    Tobias, D.J.2
  • 116
    • 0000354626 scopus 로고
    • Investigation of the free-energy functions for electron-transfer reactions
    • King, G., and A. Warshel. 1990. Investigation of the free-energy functions for electron-transfer reactions. J. Chem. Phys. 93:8682-8692.
    • (1990) J. Chem. Phys. , vol.93 , pp. 8682-8692
    • King, G.1    Warshel, A.2
  • 117
    • 0036280692 scopus 로고    scopus 로고
    • Proton transfer dynamics on the surface of the late M state of bacteriorhodopsin
    • Nachliel, E., M. Gutman, J. Tittor, and D. Oesterhelt. 2002. Proton transfer dynamics on the surface of the late M state of bacteriorhodopsin. Biophys. J. 83:416-426.
    • (2002) Biophys. J. , vol.83 , pp. 416-426
    • Nachliel, E.1    Gutman, M.2    Tittor, J.3    Oesterhelt, D.4
  • 119
    • 0035909798 scopus 로고    scopus 로고
    • Proton-collecting properties of bovine heart cytochrome C oxidase: Kinetic and electrostatic analysis
    • Marantz, Y., O. O. Einarsdottir, E. Nachliel, and M. Gutman. 2001. Proton-collecting properties of bovine heart cytochrome C oxidase: kinetic and electrostatic analysis. Biochemistry. 40:15086-15097.
    • (2001) Biochemistry , vol.40 , pp. 15086-15097
    • Marantz, Y.1    Einarsdottir, O.O.2    Nachliel, E.3    Gutman, M.4
  • 120
    • 11744384413 scopus 로고
    • The Grotthuss mechanism
    • Agmon, N. 1995. The Grotthuss mechanism. Chem. Phys. Lett. 244:456-462.
    • (1995) Chem. Phys. Lett. , vol.244 , pp. 456-462
    • Agmon, N.1
  • 121
    • 0036197879 scopus 로고    scopus 로고
    • Molecular dynamics simulation of proton transport near the surface of a phospholipid membrane
    • Smondyrev, A. M., and G. A. Voth. 2002. Molecular dynamics simulation of proton transport near the surface of a phospholipid membrane. Biophys. J. 82:1460-1468.
    • (2002) Biophys. J. , vol.82 , pp. 1460-1468
    • Smondyrev, A.M.1    Voth, G.A.2
  • 122
    • 13844298839 scopus 로고    scopus 로고
    • The salt-dependence of a protein-ligand interaction: Ion-protein binding energetics
    • Waldron, T. T., G. L. Schrift, and K. P. Murphy. 2005. The salt-dependence of a protein-ligand interaction: ion-protein binding energetics. J. Mol. Biol. 346:895-905.
    • (2005) J. Mol. Biol. , vol.346 , pp. 895-905
    • Waldron, T.T.1    Schrift, G.L.2    Murphy, K.P.3


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