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Volumn 94, Issue 9, 2008, Pages 3565-3576

Molecular dynamics simulations of asymmetric NaCI and KCl solutions separated by phosphatidylcholine bilayers: Potential drops and structural changes induced by strong Na+-lipid interactions and finite size effects

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHATIDYLCHOLINE; POTASSIUM CHLORIDE; SODIUM; SODIUM CHLORIDE; WATER;

EID: 43649093151     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.116335     Document Type: Article
Times cited : (110)

References (72)
  • 1
    • 0036275087 scopus 로고    scopus 로고
    • The effect of metal cations on the phase behavior and hydration characteristics of phospholipid membranes
    • Binder, H., and O. Zschörnig. 2002. The effect of metal cations on the phase behavior and hydration characteristics of phospholipid membranes. Chem. Phys. Lipids. 115:39-61.
    • (2002) Chem. Phys. Lipids , vol.115 , pp. 39-61
    • Binder, H.1    Zschörnig, O.2
  • 3
    • 0032598457 scopus 로고    scopus 로고
    • Interaction of alkaline earth cations with the negatively charged phospholipid 1,2-dimyristoyl-sn-glycero-3- phosphoglycerol: A differential scanning and isothermal titration calorimetric study
    • Garidel, P., and A. Blume. 1999. Interaction of alkaline earth cations with the negatively charged phospholipid 1,2-dimyristoyl-sn-glycero-3- phosphoglycerol: a differential scanning and isothermal titration calorimetric study. Langmuir. 15:5526-5534.
    • (1999) Langmuir , vol.15 , pp. 5526-5534
    • Garidel, P.1    Blume, A.2
  • 5
    • 0025230394 scopus 로고
    • Surface dielectric constant, surface hydrophobicity and membrane fusion
    • Ohki, S., and K. Arnold. 1990. Surface dielectric constant, surface hydrophobicity and membrane fusion. J. Membr. Biol. 114:195-203.
    • (1990) J. Membr. Biol , vol.114 , pp. 195-203
    • Ohki, S.1    Arnold, K.2
  • 6
    • 0027177939 scopus 로고
    • Internal electrostatic potentials in bilayers: Measuring and controlling dipole potentials in lipid vesicles
    • Franklin, J. C., and D. S. Cafiso. 1993. Internal electrostatic potentials in bilayers: measuring and controlling dipole potentials in lipid vesicles. Biophys. J. 65:289-299.
    • (1993) Biophys. J , vol.65 , pp. 289-299
    • Franklin, J.C.1    Cafiso, D.S.2
  • 7
    • 0019126875 scopus 로고
    • Measurement of surface potential and surface charge densities of sar-coplasmic reticulum membranes
    • Chiu, V. C. K., D. Mouring, B. D. Watson, and D. H. Haynes. 1980. Measurement of surface potential and surface charge densities of sar-coplasmic reticulum membranes. J. Membr. Biol. 56:121-132.
    • (1980) J. Membr. Biol , vol.56 , pp. 121-132
    • Chiu, V.C.K.1    Mouring, D.2    Watson, B.D.3    Haynes, D.H.4
  • 8
    • 24144502022 scopus 로고    scopus 로고
    • Effect of ion-binding and chemical phospholipid structure on the nanomechanics of lipid bilayers studied by force spectroscopy
    • Garcia-Manyes, S., G. Oncins, and F. Sanz. 2005. Effect of ion-binding and chemical phospholipid structure on the nanomechanics of lipid bilayers studied by force spectroscopy. Biophys. J. 89:1812-1826.
    • (2005) Biophys. J , vol.89 , pp. 1812-1826
    • Garcia-Manyes, S.1    Oncins, G.2    Sanz, F.3
  • 9
    • 33847721438 scopus 로고    scopus 로고
    • Direct imaging of lipid-ion network formation under physiological conditions by frequency modulation atomic force microscopy
    • Fukuma, T., M. J. Higgins, and S. P. Jarvis. 2007. Direct imaging of lipid-ion network formation under physiological conditions by frequency modulation atomic force microscopy. Phys. Rev. Lett. 98:106101.
    • (2007) Phys. Rev. Lett , vol.98 , pp. 106101
    • Fukuma, T.1    Higgins, M.J.2    Jarvis, S.P.3
  • 11
    • 0025332359 scopus 로고
    • The determination of binding site density and association constants for monovalent cation adsorption onto liposomes made from mixtures of zwitterionic and charged lipids
    • Ermakov, Y. A. 1990. The determination of binding site density and association constants for monovalent cation adsorption onto liposomes made from mixtures of zwitterionic and charged lipids. Biochim. Biophys. Acta. 1023:91-97.
    • (1990) Biochim. Biophys. Acta , vol.1023 , pp. 91-97
    • Ermakov, Y.A.1
  • 12
    • 0025701567 scopus 로고
    • Diffuse-double layer at a membrane-aqueous interface measured with x-ray standing waves
    • Bedzyk, M. J., G. M. Bommarito, M. Caffrey, and T. L. Penner. 1990. Diffuse-double layer at a membrane-aqueous interface measured with x-ray standing waves. Science. 248:52-56.
    • (1990) Science , vol.248 , pp. 52-56
    • Bedzyk, M.J.1    Bommarito, G.M.2    Caffrey, M.3    Penner, T.L.4
  • 13
    • 0001374494 scopus 로고
    • Phospholipid headgroup behavior in biological assemblies
    • Yeagle, P. L. 1978. Phospholipid headgroup behavior in biological assemblies. Acc. Chem. Res. 11:321-327.
    • (1978) Acc. Chem. Res , vol.11 , pp. 321-327
    • Yeagle, P.L.1
  • 14
    • 0021762389 scopus 로고
    • 2+ complex with two phospholipid molecules
    • 2+ complex with two phospholipid molecules. Biochemistry. 23:3913-3920.
    • (1984) Biochemistry , vol.23 , pp. 3913-3920
    • Altenbach, C.1    Seelig, J.2
  • 15
    • 0031175513 scopus 로고    scopus 로고
    • + with a phospholipid bilayer: A molecular dynamics study
    • + with a phospholipid bilayer: a molecular dynamics study. J. Phys. Chem. B. 101:6066-6072.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 6066-6072
    • Gambu, I.1    Roux, B.2
  • 16
    • 22544459056 scopus 로고    scopus 로고
    • Asymmetry of lipid bilayers induced by monovalent salt: Atomistic molecular-dynamics study
    • Gurtovenko, A. A. 2005. Asymmetry of lipid bilayers induced by monovalent salt: atomistic molecular-dynamics study. J. Chem. Phys. 122:244902.
    • (2005) J. Chem. Phys , vol.122 , pp. 244902
    • Gurtovenko, A.A.1
  • 17
    • 11144342719 scopus 로고    scopus 로고
    • Atomistic simulations of biologically realistic transmembrane potential gradients
    • Sachs, J. N., P. S. Crozier, and T. B. Woolf. 2004. Atomistic simulations of biologically realistic transmembrane potential gradients. J. Chem. Phys. 121:10847-10851.
    • (2004) J. Chem. Phys , vol.121 , pp. 10847-10851
    • Sachs, J.N.1    Crozier, P.S.2    Woolf, T.B.3
  • 18
    • 33947697196 scopus 로고    scopus 로고
    • Nanopore-facilitated, voltage-driven phosphatidylserine translocation in lipid bilayers in cells and in silico
    • Vernier, P. T., M. J. Ziegler, Y. Sun, M. A. Gundersen, and D. P. Tieleman. 2006. Nanopore-facilitated, voltage-driven phosphatidylserine translocation in lipid bilayers in cells and in silico. Phys. Biol. 3: 233-247.
    • (2006) Phys. Biol , vol.3 , pp. 233-247
    • Vernier, P.T.1    Ziegler, M.J.2    Sun, Y.3    Gundersen, M.A.4    Tieleman, D.P.5
  • 19
    • 2942648828 scopus 로고    scopus 로고
    • Changes in phosphatidylcholine headgroup tilt and water order induced by monovalent salts: Molecular dynamics simulations
    • Sachs, J. N., H. Nanda, H. I. Petrache, and T. B. Woolf. 2004. Changes in phosphatidylcholine headgroup tilt and water order induced by monovalent salts: molecular dynamics simulations. Biophys. J. 86: 3772-3782.
    • (2004) Biophys. J , vol.86 , pp. 3772-3782
    • Sachs, J.N.1    Nanda, H.2    Petrache, H.I.3    Woolf, T.B.4
  • 20
    • 33947704765 scopus 로고    scopus 로고
    • Ion leakage through transient water pores in protein-free lipid membranes driven by trans- membrane ionic charge imbalance
    • Gurtovenko, A. A., and I. Vattulainen. 2007. Ion leakage through transient water pores in protein-free lipid membranes driven by trans- membrane ionic charge imbalance. Biophys. J. 92:1878-1890.
    • (2007) Biophys. J , vol.92 , pp. 1878-1890
    • Gurtovenko, A.A.1    Vattulainen, I.2
  • 21
    • 26644433416 scopus 로고    scopus 로고
    • Molecular dynamics simulations of salicylate effects on the micro- and mesoscopic properties of a dipalmitoylphosphatidylcholine bilayer
    • Song, Y., V. Guallar, and N. A. Baker. 2005. Molecular dynamics simulations of salicylate effects on the micro- and mesoscopic properties of a dipalmitoylphosphatidylcholine bilayer. Biochemistry. 44: 13425-13438.
    • (2005) Biochemistry , vol.44 , pp. 13425-13438
    • Song, Y.1    Guallar, V.2    Baker, N.A.3
  • 23
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • Berger, O., O. Edholm, and F. Jahnig. 1997. Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature. Biophys. J. 72: 2002-2013.
    • (1997) Biophys. J , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 25
    • 0001563899 scopus 로고
    • Free energy of ionic hydration: Analysis of a thermodynamic integration technique to evaluate free energy differences by molecular dynamics simulations
    • Straatsma, T. P., and H. J. C. Berendsen. 1988. Free energy of ionic hydration: analysis of a thermodynamic integration technique to evaluate free energy differences by molecular dynamics simulations. J. Chem. Phys. 89:5876-5886.
    • (1988) J. Chem. Phys , vol.89 , pp. 5876-5886
    • Straatsma, T.P.1    Berendsen, H.J.C.2
  • 26
    • 1842738717 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the spontaneous formation of a small DPPC vesicle in water in atomistic detail
    • de Vries, A. H., A. E. Mark, and S. J. Marrink. 2004. Molecular dynamics simulation of the spontaneous formation of a small DPPC vesicle in water in atomistic detail. J. Am. Chem. Soc. 126:4488-4489.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 4488-4489
    • de Vries, A.H.1    Mark, A.E.2    Marrink, S.J.3
  • 27
    • 0033932839 scopus 로고    scopus 로고
    • Mesoscopic undulations and thickness fluctuations in lipid bilayers
    • Lindahl, E., and O. Edholm. 2000. Mesoscopic undulations and thickness fluctuations in lipid bilayers. Biophys. J. 79:426-433.
    • (2000) Biophys. J , vol.79 , pp. 426-433
    • Lindahl, E.1    Edholm, O.2
  • 28
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log(N) method for Ewald sums in large systems
    • Darden, T., D. York, and L. G. 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.G.3
  • 29
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • Parrinello, M., and A. Rahman. 1981. Polymorphic transitions in single crystals: a new molecular dynamics method. J. Appl. Phys. 52:7182-7190.
    • (1981) J. Appl. Phys , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 30
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover, W. G. 1985. Canonical dynamics: equilibrium phase-space distributions. Phys. Rev. A. 31:1695-1697.
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 31
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J. P., G. Ciccotti, and H. J. C. Berendsen. 1977. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys. 23:327-341.
    • (1977) J. Comput. Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 33
    • 34347362979 scopus 로고    scopus 로고
    • Quantitative characterization of ion pairing and cluster formation in strong 1:1 electrolytes
    • Chen, A. A., and R. V. Pappu. 2007. Quantitative characterization of ion pairing and cluster formation in strong 1:1 electrolytes. J. Phys. Chem. B. 111:6469-6478.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 6469-6478
    • Chen, A.A.1    Pappu, R.V.2
  • 35
    • 4544290164 scopus 로고    scopus 로고
    • Multistep binding of divalent cations to phospholipid bilayers: A molecular dynamics study
    • Böckmann, R. A., and H. Grubmüller. 2004. Multistep binding of divalent cations to phospholipid bilayers: a molecular dynamics study. Angew. Chem. Int. Ed. 43:1021-1024.
    • (2004) Angew. Chem. Int. Ed , vol.43 , pp. 1021-1024
    • Böckmann, R.A.1    Grubmüller, H.2
  • 38
    • 0037678992 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a dipalmitoylphosphatidylcholine bilayer with NaCl
    • Pandit, S. A., D. Bostick, 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    Bostick, D.2    Berkowitz, M.L.3
  • 39
    • 0016283654 scopus 로고
    • Dynamic structure of fatty acyl chains in a phospholipid bilayer measured by deuterium magnetic resonance
    • Seelig, A., and J. Seelig. 1974. Dynamic structure of fatty acyl chains in a phospholipid bilayer measured by deuterium magnetic resonance. Biochemistry. 13:4839-4845.
    • (1974) Biochemistry , vol.13 , pp. 4839-4845
    • Seelig, A.1    Seelig, J.2
  • 40
    • 0031438285 scopus 로고    scopus 로고
    • A computer perspective of membranes: Molecular dynamics studies of lipid bilayer systems
    • Tieleman, D. P., S. J. Marrink, and H. J. C. Berendsen. 1997. A computer perspective of membranes: molecular dynamics studies of lipid bilayer systems. Biochim. Biophys. Acta Rev. Biomembr. 1331:235-270.
    • (1997) Biochim. Biophys. Acta Rev. Biomembr , vol.1331 , pp. 235-270
    • Tieleman, D.P.1    Marrink, S.J.2    Berendsen, H.J.C.3
  • 41
    • 0000648885 scopus 로고    scopus 로고
    • A Critical analysis of methods of calculation of a potential in simulated polar liquids: Strong arguments in favor of "molecule-based" summation and of vacuum boundary conditions in Ewald summation
    • Vorobjev, Y. N., and J. Hermans. 1999. A Critical analysis of methods of calculation of a potential in simulated polar liquids: strong arguments in favor of "molecule-based" summation and of vacuum boundary conditions in Ewald summation. J. Phys. Chem. B. 103:10234-10242.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 10234-10242
    • Vorobjev, Y.N.1    Hermans, J.2
  • 43
    • 0035879987 scopus 로고    scopus 로고
    • Salt-induced phase separation in the liquid crystalline phase of phosphati-dylcholines
    • Rappolt, M., G. Pabst, H. Amenitsch, and P. Laggner. 2001. Salt-induced phase separation in the liquid crystalline phase of phosphati-dylcholines. Colloids Surfaces A. 183-5:171-181.
    • (2001) Colloids Surfaces A , vol.183 -5 , pp. 171-181
    • Rappolt, M.1    Pabst, G.2    Amenitsch, H.3    Laggner, P.4
  • 44
    • 23044478171 scopus 로고    scopus 로고
    • The effect of peptides and ions interacting with an electrically neutral membrane interface on the structure and stability of lipid membranes in the liquid-crystalline phase and in the liquid-ordered phase
    • Sano, R., S. M. Masum, T. Tanaka, Y. Yamashita, V. Levadny, and M. Yamakazi. 2005. The effect of peptides and ions interacting with an electrically neutral membrane interface on the structure and stability of lipid membranes in the liquid-crystalline phase and in the liquid-ordered phase. J. Phys. Condens. Matter. 17:S2979-S2989.
    • (2005) J. Phys. Condens. Matter , vol.17
    • Sano, R.1    Masum, S.M.2    Tanaka, T.3    Yamashita, Y.4    Levadny, V.5    Yamakazi, M.6
  • 45
    • 0020328144 scopus 로고
    • Effect of calcium ion on the mechanical properties of lipid bilayer membrane
    • Mitaku, S., and S. Aruga. 1982. Effect of calcium ion on the mechanical properties of lipid bilayer membrane. Biorheology. 19:185-196.
    • (1982) Biorheology , vol.19 , pp. 185-196
    • Mitaku, S.1    Aruga, S.2
  • 49
    • 0024280716 scopus 로고
    • Structure of fully hydrated bilayer dispersions
    • Nagle, J. F., and M. C. Wiener. 1988. Structure of fully hydrated bilayer dispersions. Biochim. Biophys. Acta. 942:1-10.
    • (1988) Biochim. Biophys. Acta , vol.942 , pp. 1-10
    • Nagle, J.F.1    Wiener, M.C.2
  • 50
    • 37049023237 scopus 로고    scopus 로고
    • On the orientation of a designed transmembrane peptide: Toward the right tilt angle?
    • In press
    • Ozdirekcan, S., C. Etchebest, J. A. Killian, and P. F. J. Fuchs. On the orientation of a designed transmembrane peptide: toward the right tilt angle? J. Am. Chem. Soc. In press. http://dx.doi.org/10.1021/ja073784q.
    • J. Am. Chem. Soc
    • Ozdirekcan, S.1    Etchebest, C.2    Killian, J.A.3    Fuchs, P.F.J.4
  • 51
    • 33847361456 scopus 로고    scopus 로고
    • Convergence of molecular dynamics simulations of membrane proteins
    • Grossfield, A., S. E. Feller, and M. C. Pitman. 2007. Convergence of molecular dynamics simulations of membrane proteins. Proteins. 67: 31-40.
    • (2007) Proteins , vol.67 , pp. 31-40
    • Grossfield, A.1    Feller, S.E.2    Pitman, M.C.3
  • 52
    • 33751556346 scopus 로고    scopus 로고
    • Dynamics in atomistic simulations of phospholipid membranes: Nuclear magnetic resonance relaxation rates and lateral diffusion
    • Wohlert, J., and O. Edholm. 2006. Dynamics in atomistic simulations of phospholipid membranes: nuclear magnetic resonance relaxation rates and lateral diffusion. J. Chem. Phys. 125:204703.
    • (2006) J. Chem. Phys , vol.125 , pp. 204703
    • Wohlert, J.1    Edholm, O.2
  • 53
    • 33746897341 scopus 로고    scopus 로고
    • A molecular dynamics investigation of the influence of hydration and temperature on structural and dynamical properties of a dimyristoylphosphatidylcholine bilayer
    • Högberg, C. J., and A. P. Lyubartsev. 2006. A molecular dynamics investigation of the influence of hydration and temperature on structural and dynamical properties of a dimyristoylphosphatidylcholine bilayer. J. Phys. Chem. B. 110:14326-14336.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 14326-14336
    • Högberg, C.J.1    Lyubartsev, A.P.2
  • 55
    • 0017850042 scopus 로고
    • High-sensitivity scanning calorimetric study of mixtures of cholesterol with dimyristoyl- and dipalmitoylphosphatidylcholines
    • Mabrey, S., P. L. Mateo, and J. M. Sturtevant. 1978. High-sensitivity scanning calorimetric study of mixtures of cholesterol with dimyristoyl- and dipalmitoylphosphatidylcholines. Biochemistry. 17:2464-2468.
    • (1978) Biochemistry , vol.17 , pp. 2464-2468
    • Mabrey, S.1    Mateo, P.L.2    Sturtevant, J.M.3
  • 56
    • 34250336942 scopus 로고    scopus 로고
    • Ion transport across transmembrane pores
    • Leontiadou, H., A. E. Mark, and S. J. Marrink. 2007. Ion transport across transmembrane pores. Biophys. J. 92:4209-4215.
    • (2007) Biophys. J , vol.92 , pp. 4209-4215
    • Leontiadou, H.1    Mark, A.E.2    Marrink, S.J.3
  • 57
    • 0034123344 scopus 로고    scopus 로고
    • Homology modeling and molecular dynamics simulation studies of an inward rectifier potassium channel
    • Capener, C. E., I. H. Shrivastava, K. M. Ranatunga, L. R. Forrest, G. R. Smith, and M. S. P. Sansom. 2000. Homology modeling and molecular dynamics simulation studies of an inward rectifier potassium channel. Biophys. J. 78:2929-2942.
    • (2000) Biophys. J , vol.78 , pp. 2929-2942
    • Capener, C.E.1    Shrivastava, I.H.2    Ranatunga, K.M.3    Forrest, L.R.4    Smith, G.R.5    Sansom, M.S.P.6
  • 58
    • 33750606030 scopus 로고    scopus 로고
    • Molecular dynamics-potential of mean force calculations as a tool for understanding ion permeation and selectivity in narrow channels
    • Allen, T. W., O. S. Andersen, and B. Roux. 2006. Molecular dynamics-potential of mean force calculations as a tool for understanding ion permeation and selectivity in narrow channels. Biophys. Chem. 124:251-267 http://dx.doi.org/10.1016/j.bpc.2006.04.015.
    • (2006) Biophys. Chem , vol.124 , pp. 251-267
    • Allen, T.W.1    Andersen, O.S.2    Roux, B.3
  • 59
    • 0344796204 scopus 로고
    • Ion-water interaction potentials derived from free energy perturbation simulations
    • Åqvist, J. 1990. Ion-water interaction potentials derived from free energy perturbation simulations. J. Phys. Chem. 94:8021-8024.
    • (1990) J. Phys. Chem , vol.94 , pp. 8021-8024
    • Åqvist, J.1
  • 60
    • 0029731562 scopus 로고    scopus 로고
    • Valence selectivity of the gramicidin channel: A molecular dynamics free energy perturbation study
    • Roux, B. 1996. Valence selectivity of the gramicidin channel: a molecular dynamics free energy perturbation study. Biophys. J. 71:3177-3185.
    • (1996) Biophys. J , vol.71 , pp. 3177-3185
    • Roux, B.1
  • 61
    • 0037007814 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a K channel model: Sensitivity to changes in ions, waters, and membrane environment
    • Capener, C. E., and M. S. P. Sansom. 2002. Molecular dynamics simulations of a K channel model: sensitivity to changes in ions, waters, and membrane environment. J. Phys. Chem. B. 106:4543-4551.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 4543-4551
    • Capener, C.E.1    Sansom, M.S.P.2
  • 62
    • 0036618993 scopus 로고    scopus 로고
    • Setting up and optimization of membrane protein simulations
    • Faraldo-Gómez, J. D., G. R. Smith, and M. S. P. Sansom. 2002. Setting up and optimization of membrane protein simulations. Eur. Biophys. J. 31:217-227.
    • (2002) Eur. Biophys. J , vol.31 , pp. 217-227
    • Faraldo-Gómez, J.D.1    Smith, G.R.2    Sansom, M.S.P.3
  • 63
    • 33644770589 scopus 로고    scopus 로고
    • Model of an asymmetric DPPC/DPPS membrane: Effect of asymmetry on the lipid properties. a molecular dynamics simulation study
    • López Cascales, J. J., T. F. Otero, B. D. Smith, C. González, and M. Márquez. 2006. Model of an asymmetric DPPC/DPPS membrane: effect of asymmetry on the lipid properties. a molecular dynamics simulation study. J. Phys. Chem. B. 110:2358-2363.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 2358-2363
    • López Cascales, J.J.1    Otero, T.F.2    Smith, B.D.3    González, C.4    Márquez, M.5
  • 64
    • 0029099308 scopus 로고
    • Incorporation of surface tension into molecular dynamics simulation of an interface: A fluid phase lipid bilayer membrane
    • Chiu, S. W., M. Clark, V. Balaji, S. Subramaniam, H. L. Scott, and E. Jakobsson. 1995. Incorporation of surface tension into molecular dynamics simulation of an interface: a fluid phase lipid bilayer membrane. Biophys. J. 69:1230-1245.
    • (1995) Biophys. J , vol.69 , pp. 1230-1245
    • Chiu, S.W.1    Clark, M.2    Balaji, V.3    Subramaniam, S.4    Scott, H.L.5    Jakobsson, E.6
  • 65
    • 0037569250 scopus 로고    scopus 로고
    • A consistent potential energy parameter set for lipids: Dipalmitoylphosphatidylcho-line as a benchmark of the GROMOS96 45A3 force field
    • Chandrasekhar, I., M. Kastenholz, R. D. Lins, C. Oostenbrink, L. D. Schuler, D. P. Tieleman, and W. F. Van Gunsteren. 2003. A consistent potential energy parameter set for lipids: dipalmitoylphosphatidylcho-line as a benchmark of the GROMOS96 45A3 force field. Eur. Biophys. J. 32:67-77.
    • (2003) Eur. Biophys. J , vol.32 , pp. 67-77
    • Chandrasekhar, I.1    Kastenholz, M.2    Lins, R.D.3    Oostenbrink, C.4    Schuler, L.D.5    Tieleman, D.P.6    Van Gunsteren, W.F.7
  • 66
    • 33646192258 scopus 로고    scopus 로고
    • Ion permeation through a narrow channel: Using gramicidin to ascertain all-atom molecular dynamics potential of mean force methodology and biomolecular force fields
    • Allen, T. W., O. S. Andersen, and B. Roux. 2006. Ion permeation through a narrow channel: using gramicidin to ascertain all-atom molecular dynamics potential of mean force methodology and biomolecular force fields. Biophys. J. 90:3447-3468.
    • (2006) Biophys. J , vol.90 , pp. 3447-3468
    • Allen, T.W.1    Andersen, O.S.2    Roux, B.3
  • 68
    • 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
  • 69
    • 0242443693 scopus 로고    scopus 로고
    • Force fields for protein simulations
    • Ponder, J. W., and D. A. Case. 2003. Force fields for protein simulations. Adv. Protein Chem. 66:27-85.
    • (2003) Adv. Protein Chem , vol.66 , pp. 27-85
    • Ponder, J.W.1    Case, D.A.2
  • 70
    • 22844433642 scopus 로고    scopus 로고
    • Test of molecular dynamics force fields in gramicidin
    • Bastug, T., and S. Kuyucak. 2005. Test of molecular dynamics force fields in gramicidin. Eur. Biophys. J. 34:377-382.
    • (2005) Eur. Biophys. J , vol.34 , pp. 377-382
    • Bastug, T.1    Kuyucak, S.2
  • 71
    • 34247853295 scopus 로고    scopus 로고
    • Lipid transmembrane asymmetry and intrinsic membrane potential: Two sides of the same coin
    • Gurtovenko, A. A., and I. Vattulainen. 2007. Lipid transmembrane asymmetry and intrinsic membrane potential: two sides of the same coin. J. Am. Chem. Soc. 129:5358-5359.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 5358-5359
    • Gurtovenko, A.A.1    Vattulainen, I.2
  • 72
    • 0001008704 scopus 로고
    • Molecular dynamics simulation of a bilayer of 200 lipids in the gel and in the liquid crystal phase
    • Heller, H., M. Schaefer, and K. Schulten. 1993. Molecular dynamics simulation of a bilayer of 200 lipids in the gel and in the liquid crystal phase. J. Phys. Chem. 97:8343-8360.
    • (1993) J. Phys. Chem , vol.97 , pp. 8343-8360
    • Heller, H.1    Schaefer, M.2    Schulten, K.3


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