메뉴 건너뛰기




Volumn 8, Issue 2, 1998, Pages 237-244

Models and simulations of ion channels and related membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

ALAMETHICIN; GRAMICIDIN; ION CHANNEL; MEMBRANE PROTEIN; NICOTINIC RECEPTOR; VIRUS PROTEIN; WATER;

EID: 0032054195     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80045-6     Document Type: Article
Times cited : (37)

References (83)
  • 2
    • 0027959026 scopus 로고
    • Seven-helix receptors: Structure and modelling
    • Donnelly D, Findlay JBC. Seven-helix receptors: structure and modelling. Curr Opin Struct Biol. 4:1994;582-589.
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 582-589
    • Donnelly, D.1    Findlay, J.B.C.2
  • 3
    • 0003535316 scopus 로고    scopus 로고
    • of special interest. Birkhäuser, Boston, An excellent survey of all aspects of computational studies of biological membranes.
    • Merz KM, Roux B. . of special interest Biological Membranes: A Molecular Perspective from Computation and Experiment. 1996;587 Birkhäuser, Boston, An excellent survey of all aspects of computational studies of biological membranes.
    • (1996) Biological Membranes: a Molecular Perspective from Computation and Experiment , pp. 587
    • Merz, K.M.1    Roux, B.2
  • 4
    • 0031438285 scopus 로고    scopus 로고
    • A computer perspective of membranes: Molecular dynamics studies of lipid bilayer systems
    • of special interest. A careful and thorough survey of MD simulations of lipid bilayers.
    • Tieleman DP, Marrink SJ, Berendsen HJC. A computer perspective of membranes: molecular dynamics studies of lipid bilayer systems. of special interest Biochim Biophys Acta. 1331:1997;235-269 A careful and thorough survey of MD simulations of lipid bilayers.
    • (1997) Biochim Biophys Acta , vol.1331 , pp. 235-269
    • Tieleman, D.P.1    Marrink, S.J.2    Berendsen, H.J.C.3
  • 5
    • 0028321565 scopus 로고
    • Molecular dynamics simulations of the gramicidin channel
    • Roux B, Karplus M. Molecular dynamics simulations of the gramicidin channel. Annu Rev Biophys Biomol Struct. 23:1994;731-761.
    • (1994) Annu Rev Biophys Biomol Struct , vol.23 , pp. 731-761
    • Roux, B.1    Karplus, M.2
  • 7
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR
    • Ketchem RR, Hu W, Cross TA. High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR. Science. 261:1993;1457-1460.
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 8
    • 0030050164 scopus 로고    scopus 로고
    • A semi-microscopic Monte Carlo study of permeation energetics in a gramicidin-like channel: The origin of cation selectivity
    • of special interest. Monte Carlo simulations on a gramicidin-like channel combined with careful treatment of electrostatics suggest that the channel is cation selective because anions bind hydration water more strong (read in conjunction with Roux [9]).
    • Dorman V, Partenskii MB, Jordan PC. A semi-microscopic Monte Carlo study of permeation energetics in a gramicidin-like channel: the origin of cation selectivity. of special interest Biophys J. 70:1996;121-134 Monte Carlo simulations on a gramicidin-like channel combined with careful treatment of electrostatics suggest that the channel is cation selective because anions bind hydration water more strong (read in conjunction with Roux [9]).
    • (1996) Biophys J , vol.70 , pp. 121-134
    • Dorman, V.1    Partenskii, M.B.2    Jordan, P.C.3
  • 9
    • 0029731562 scopus 로고    scopus 로고
    • Valence selectivity of the gramicidin channel: A molecular dynamics free energy perturbation study
    • - ions (read in conjunction with Dorman et al. [8]).
    • - ions (read in conjunction with Dorman et al. [8]).
    • (1996) Biophys J , vol.71 , pp. 3177-3185
    • Roux, B.1
  • 10
    • 0030995981 scopus 로고    scopus 로고
    • The binding site of sodium in the gramicidin A channel: Comparison of molecular dynamics with solid-state NMR data
    • Woolf TB, Roux B. The binding site of sodium in the gramicidin A channel: comparison of molecular dynamics with solid-state NMR data. Biophys J. 72:1997;1930-1945.
    • (1997) Biophys J , vol.72 , pp. 1930-1945
    • Woolf, T.B.1    Roux, B.2
  • 11
    • 0030965871 scopus 로고    scopus 로고
    • Ion-water and water-water interactions in a gramicidin-like channel: Effects due to group polarization and backbone flexibility
    • Duca KA, Jordan PC. Ion-water and water-water interactions in a gramicidin-like channel: effects due to group polarization and backbone flexibility. Biophys Chem. 65:1997;123-141.
    • (1997) Biophys Chem , vol.65 , pp. 123-141
    • Duca, K.A.1    Jordan, P.C.2
  • 12
    • 0030808398 scopus 로고    scopus 로고
    • Molecular dynamics study of free energy profiles for organic cations in gramicidin A channels
    • of special interest. Free-energy profiles for organic cations show a remarkable correlation with experimental data for three types of ion - channel interaction: permeation versus no permeation versus block.
    • Hao Y, Pear MR, Busath DD. Molecular dynamics study of free energy profiles for organic cations in gramicidin A channels. of special interest Biophys J. 73:1997;1699-1716 Free-energy profiles for organic cations show a remarkable correlation with experimental data for three types of ion - channel interaction: permeation versus no permeation versus block.
    • (1997) Biophys J , vol.73 , pp. 1699-1716
    • Hao, Y.1    Pear, M.R.2    Busath, D.D.3
  • 13
    • 0025823857 scopus 로고
    • Proton conductance by the gramicidin water wire
    • Akeson M, Deamer DW. Proton conductance by the gramicidin water wire. Biophys J. 60:1991;101-109.
    • (1991) Biophys J , vol.60 , pp. 101-109
    • Akeson, M.1    Deamer, D.W.2
  • 14
    • 0030183308 scopus 로고    scopus 로고
    • Visualizing proton conductance in the gramicidin channel
    • Deamer DW. Visualizing proton conductance in the gramicidin channel. Biophys J. 71:1996;5.
    • (1996) Biophys J , vol.71 , pp. 5
    • Deamer, D.W.1
  • 15
    • 0029878757 scopus 로고    scopus 로고
    • Structure and dynamics of hydronium in the ion channel gramicidin A
    • + simulated inside a gramicidin channel changes the pattern of H-bonding in the single-file water and inhibits water reorientational motions (read in conjunction with Pomes and Roux [16]).
    • + simulated inside a gramicidin channel changes the pattern of H-bonding in the single-file water and inhibits water reorientational motions (read in conjunction with Pomes and Roux [16]).
    • (1996) Biophys J , vol.70 , pp. 2043-2051
    • Sagnella, D.E.1    Voth, G.A.2
  • 16
    • 0030011088 scopus 로고    scopus 로고
    • + translocation along the single-file water chain in the gramicidin A channel
    • of special interest. Dynamics of a proton wire in gramicidin show fast migration of a proton along the single-file water (read in conjunction with Sagnella and Voth [15]).
    • + translocation along the single-file water chain in the gramicidin A channel. of special interest Biophys J. 71:1996;19-39 Dynamics of a proton wire in gramicidin show fast migration of a proton along the single-file water (read in conjunction with Sagnella and Voth [15]).
    • (1996) Biophys J , vol.71 , pp. 19-39
    • Pomes, R.1    Roux, B.2
  • 17
    • 0029775587 scopus 로고    scopus 로고
    • Ab initio molecular dynamics study of proton transfer in a polyglycine analog of the ion channel gramicidin A
    • Sagnella DE, Laasonen K, Klein ML. Ab initio molecular dynamics study of proton transfer in a polyglycine analog of the ion channel gramicidin A. Biophys J. 71:1996;1172-1178.
    • (1996) Biophys J , vol.71 , pp. 1172-1178
    • Sagnella, D.E.1    Laasonen, K.2    Klein, M.L.3
  • 18
    • 0027817476 scopus 로고
    • Structure and function of channel-forming peptaibols
    • Sansom MSP. Structure and function of channel-forming peptaibols. Quart Rev Biophys. 26:1993;365-421.
    • (1993) Quart Rev Biophys , vol.26 , pp. 365-421
    • Sansom, M.S.P.1
  • 19
    • 0031001316 scopus 로고    scopus 로고
    • Alamethicin channels - Molecular modelling via restrained molecular dynamics simulations
    • Breed J, Biggin PC, Kerr ID, Smart OS, Sansom MSP. Alamethicin channels - molecular modelling via restrained molecular dynamics simulations. Biochim Biophys Acta. 1325:1997;235-249.
    • (1997) Biochim Biophys Acta , vol.1325 , pp. 235-249
    • Breed, J.1    Biggin, P.C.2    Kerr, I.D.3    Smart, O.S.4    Sansom, M.S.P.5
  • 20
    • 0029913429 scopus 로고    scopus 로고
    • Ion-channel stabilization of synthetic alamethicin analogs by rings of inter-helix H-bonds
    • Molle G, Dugast JY, Spach G, Duclohier H. Ion-channel stabilization of synthetic alamethicin analogs by rings of inter-helix H-bonds. Biophys J. 70:1996;1669-1675.
    • (1996) Biophys J , vol.70 , pp. 1669-1675
    • Molle, G.1    Dugast, J.Y.2    Spach, G.3    Duclohier, H.4
  • 21
    • 0030807799 scopus 로고    scopus 로고
    • Ion channel stability. Molecular modelling of channels formed by synthetic alamethicin analogues
    • Breed J, Kerr ID, Molle G, Duclohier H, Sansom MSP. Ion channel stability. Molecular modelling of channels formed by synthetic alamethicin analogues. Biochim Biophys Acta. 1330:1997;103-109.
    • (1997) Biochim Biophys Acta , vol.1330 , pp. 103-109
    • Breed, J.1    Kerr, I.D.2    Molle, G.3    Duclohier, H.4    Sansom, M.S.P.5
  • 22
    • 0031042584 scopus 로고    scopus 로고
    • A novel method for structure-based prediction of ion channel conductance properties
    • Smart OS, Breed J, Smith GR, Sansom MSP. A novel method for structure-based prediction of ion channel conductance properties. Biophys J. 72:1997;1109-1126.
    • (1997) Biophys J , vol.72 , pp. 1109-1126
    • Smart, O.S.1    Breed, J.2    Smith, G.R.3    Sansom, M.S.P.4
  • 25
    • 0030457853 scopus 로고    scopus 로고
    • Molecular dynamics simulations of ion channels formed by bundles of amphipathic α-helical peptides
    • Mitton P, Sansom MSP. Molecular dynamics simulations of ion channels formed by bundles of amphipathic α-helical peptides. Eur Biophys J. 25:1996;139-150.
    • (1996) Eur Biophys J , vol.25 , pp. 139-150
    • Mitton, P.1    Sansom, M.S.P.2
  • 26
    • 0028278173 scopus 로고
    • A helical-dipole model describes the single-channel current rectification of an uncharged peptide ion channel
    • Kienker PK, DeGrado WF, Lear JD. A helical-dipole model describes the single-channel current rectification of an uncharged peptide ion channel. Proc Natl Acad Sci USA. 91:1994;4859-4863.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4859-4863
    • Kienker, P.K.1    Degrado, W.F.2    Lear, J.D.3
  • 28
    • 0031451335 scopus 로고    scopus 로고
    • Channels formed by the transmembrane helix of phospholamban: A simulation study
    • Sansom MSP, Smith GR, Smart OS, Smith SO. Channels formed by the transmembrane helix of phospholamban: a simulation study. Biophys Chem. 69:1997;269-281.
    • (1997) Biophys Chem , vol.69 , pp. 269-281
    • Sansom, M.S.P.1    Smith, G.R.2    Smart, O.S.3    Smith, S.O.4
  • 30
    • 0029816765 scopus 로고    scopus 로고
    • Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells
    • Chizhmakov IV, Geraghty FM, Ogden DC, Hayhurst A, Antoniou M, Hay AJ. Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells. J Physiol. 494:1996;329-336.
    • (1996) J Physiol , vol.494 , pp. 329-336
    • Chizhmakov, I.V.1    Geraghty, F.M.2    Ogden, D.C.3    Hayhurst, A.4    Antoniou, M.5    Hay, A.J.6
  • 31
    • 0029794387 scopus 로고    scopus 로고
    • The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels
    • Ewart GD, Sutherland T, Gage PW, Cox GB. The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels. J Virol. 70:1996;7108-7115.
    • (1996) J Virol , vol.70 , pp. 7108-7115
    • Ewart, G.D.1    Sutherland, T.2    Gage, P.W.3    Cox, G.B.4
  • 32
    • 0030602182 scopus 로고    scopus 로고
    • Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells
    • Schubert U, Ferrer-Montiel AV, Oblatt-Montal M, Henklein P, Strebel K, Montal M. Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells. FEBS Lett. 398:1996;12-18.
    • (1996) FEBS Lett , vol.398 , pp. 12-18
    • Schubert, U.1    Ferrer-Montiel, A.V.2    Oblatt-Montal, M.3    Henklein, P.4    Strebel, K.5    Montal, M.6
  • 33
    • 0030803839 scopus 로고    scopus 로고
    • The influenza A virus M2 channel: - A molecular modelling and simulation study
    • of outstanding interest. of special interest. A model of the influenza M2 channel which accommodates a narrow column of water and suggests a possible gating mechanism (read in conjunction with Pinto et al. [34]).
    • of outstanding interest Sansom MSP, Kerr ID, Smith GR, Son HS. The influenza A virus M2 channel: - a molecular modelling and simulation study. of special interest Virology. 233:1997;163-173 A model of the influenza M2 channel which accommodates a narrow column of water and suggests a possible gating mechanism (read in conjunction with Pinto et al. [34]).
    • (1997) Virology , vol.233 , pp. 163-173
    • Sansom, M.S.P.1    Kerr, I.D.2    Smith, G.R.3    Son, H.S.4
  • 34
    • 0030881872 scopus 로고    scopus 로고
    • 2 proton channel of influenza A virus suggests a mechanism for its ion selectivity
    • of special interest. of outstanding interest. A rigorous analysis of site-directed mutagenesis data results in a persuasive model for the influenza M2 channel (read in conjunction with Sansom et al. [33]).
    • 2 proton channel of influenza A virus suggests a mechanism for its ion selectivity. of outstanding interest Proc Natl Acad Sci USA. 94:1997;11301-11306 A rigorous analysis of site-directed mutagenesis data results in a persuasive model for the influenza M2 channel (read in conjunction with Sansom et al. [33]).
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11301-11306
    • Pinto, L.H.1    Dieckmann, G.R.2    Gandhi, C.S.3    Papworth, C.G.4    Braman, J.5    Shaughnessy, M.A.6    Lear, J.D.7    Lamb, R.A.8    Degrado, W.F.9
  • 35
    • 0030891182 scopus 로고    scopus 로고
    • Ion channels formed by HIV-1 Vpu: A modelling and simulation study
    • Grice A, Kerr ID, Sansom MSP. Ion channels formed by HIV-1 Vpu: a modelling and simulation study. FEBS Lett. 405:1997;299-304.
    • (1997) FEBS Lett , vol.405 , pp. 299-304
    • Grice, A.1    Kerr, I.D.2    Sansom, M.S.P.3
  • 36
    • 0029813087 scopus 로고    scopus 로고
    • The pore domain of the nicotinic acetylcholine receptor: Molecular modelling and electrostatics
    • Sankararamakrishnan R, Adcock C, Sansom MSP. The pore domain of the nicotinic acetylcholine receptor: molecular modelling and electrostatics. Biophys J. 71:1996;1659-1671.
    • (1996) Biophys J , vol.71 , pp. 1659-1671
    • Sankararamakrishnan, R.1    Adcock, C.2    Sansom, M.S.P.3
  • 37
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin N. Acetylcholine receptor channel imaged in the open state. Nature. 373:1995;37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 38
    • 0030876984 scopus 로고    scopus 로고
    • + ions in models of the pore region of the nicotinic acetylcholine receptor
    • + ions in models of the pore region of the nicotinic acetylcholine receptor. Biophys J. 73:1997;1364-1381.
    • (1997) Biophys J , vol.73 , pp. 1364-1381
    • Smith, G.R.1    Sansom, M.S.P.2
  • 39
    • 0030777710 scopus 로고    scopus 로고
    • The dielectric properties of water within model transbilayer pores
    • of special interest. MD simulations of water within a simple model channel suggest altered dielectric behaviour.
    • Sansom MSP, Smith GR, Adcock C, Biggin PC. The dielectric properties of water within model transbilayer pores. of special interest Biophys J. 73:1997;2404-2415 MD simulations of water within a simple model channel suggest altered dielectric behaviour.
    • (1997) Biophys J , vol.73 , pp. 2404-2415
    • Sansom, M.S.P.1    Smith, G.R.2    Adcock, C.3    Biggin, P.C.4
  • 40
    • 0029936679 scopus 로고    scopus 로고
    • A mixed helix-beta-sheet model of the transmembrane region of the nicotinic acetylcholine receptor
    • Ortells MO, Lunt GG. A mixed helix-beta-sheet model of the transmembrane region of the nicotinic acetylcholine receptor. Protein Eng. 9:1996;51-59.
    • (1996) Protein Eng , vol.9 , pp. 51-59
    • Ortells, M.O.1    Lunt, G.G.2
  • 41
    • 0030912140 scopus 로고    scopus 로고
    • Molecular modelling of the nicotinic acetylcholine receptor transmembrane region in the open state
    • Ortells MO, Barrantes GE, Wood C, Lunt GG, Barrantes FJ. Molecular modelling of the nicotinic acetylcholine receptor transmembrane region in the open state. Protein Eng. 10:1996;511-517.
    • (1996) Protein Eng , vol.10 , pp. 511-517
    • Ortells, M.O.1    Barrantes, G.E.2    Wood, C.3    Lunt, G.G.4    Barrantes, F.J.5
  • 42
    • 0030957191 scopus 로고    scopus 로고
    • A model of the nicotinic receptor extracellular domain based on sequence identity and residue location
    • Tsigelny I, Sugiyama N, Sine SM, Taylor P. A model of the nicotinic receptor extracellular domain based on sequence identity and residue location. Biophys J. 73:1997;52-66.
    • (1997) Biophys J , vol.73 , pp. 52-66
    • Tsigelny, I.1    Sugiyama, N.2    Sine, S.M.3    Taylor, P.4
  • 43
    • 0030902081 scopus 로고    scopus 로고
    • Predicted structure of the extracellular region of ligand-gated ion-channel receptors shows SH2-like and SH3-like domains forming the ligand binding site
    • Gready JE, Ranganathan S, Schofield PR, Matsuo Y, Nishikawa K. Predicted structure of the extracellular region of ligand-gated ion-channel receptors shows SH2-like and SH3-like domains forming the ligand binding site. Protein Sci. 6:1997;52-66.
    • (1997) Protein Sci , vol.6 , pp. 52-66
    • Gready, J.E.1    Ranganathan, S.2    Schofield, P.R.3    Matsuo, Y.4    Nishikawa, K.5
  • 44
    • 0029966280 scopus 로고    scopus 로고
    • Three-dimensional models of non-NMDA glutamate receptors
    • Sutcliffe MJ, Wo ZG, Oswald RE. Three-dimensional models of non-NMDA glutamate receptors. Biophys J. 70:1996;1575-1589.
    • (1996) Biophys J , vol.70 , pp. 1575-1589
    • Sutcliffe, M.J.1    Wo, Z.G.2    Oswald, R.E.3
  • 45
    • 0030748569 scopus 로고    scopus 로고
    • The pore-lining region of Shaker voltage-gated potassium channels: Comparison of β-barrel and α-helix bundle models
    • Kerr ID, Sansom MSP. The pore-lining region of Shaker voltage-gated potassium channels: comparison of β-barrel and α-helix bundle models. Biophys J. 73:1997;581-602.
    • (1997) Biophys J , vol.73 , pp. 581-602
    • Kerr, I.D.1    Sansom, M.S.P.2
  • 46
    • 4243468773 scopus 로고    scopus 로고
    • Protein-water-ion interactions in a model of the pore domain of a potassium channel: A simulation study
    • in press
    • Ranatunga KR, Kerr ID, Adcock C, Smith GR, Sansom MSP. Protein-water-ion interactions in a model of the pore domain of a potassium channel: a simulation study. Biochim Biophys Acta. 1997;. in press.
    • (1997) Biochim Biophys Acta
    • Ranatunga, K.R.1    Kerr, I.D.2    Adcock, C.3    Smith, G.R.4    Sansom, M.S.P.5
  • 47
    • 0030988203 scopus 로고    scopus 로고
    • Shaker pore structure as predicted by annealed atomic simulation using symmetry and novel geometric restraints
    • Yang PK, Lee CY, Hwang MJ. Shaker pore structure as predicted by annealed atomic simulation using symmetry and novel geometric restraints. Biophys J. 72:1997;2479-2489.
    • (1997) Biophys J , vol.72 , pp. 2479-2489
    • Yang, P.K.1    Lee, C.Y.2    Hwang, M.J.3
  • 49
    • 0029914063 scopus 로고    scopus 로고
    • Solvation, water permeation, and ionic selectivity of the voltage-gated sodium channel
    • Singh C, Sankararamakrishnan R, Subramanian S, Jakobsson E. Solvation, water permeation, and ionic selectivity of the voltage-gated sodium channel. Biophys J. 71:1996;2276-2288.
    • (1996) Biophys J , vol.71 , pp. 2276-2288
    • Singh, C.1    Sankararamakrishnan, R.2    Subramanian, S.3    Jakobsson, E.4
  • 50
    • 0029555967 scopus 로고
    • Models of ion pores in N-type voltage-gated calcium channels
    • Doughty SW, Blaney FE, Richards GW. Models of ion pores in N-type voltage-gated calcium channels. J Mol Graph. 13:1995;342.
    • (1995) J Mol Graph , vol.13 , pp. 342
    • Doughty, S.W.1    Blaney, F.E.2    Richards, G.W.3
  • 52
    • 0030895157 scopus 로고    scopus 로고
    • Computer simulations of the OmpF porin from the outer membrane of Escherichia coli
    • Watanabe M, Rosenbusch J, Schirmer T, Karplus M. Computer simulations of the OmpF porin from the outer membrane of Escherichia coli. Biophys J. 72:1997.
    • (1997) Biophys J , vol.72
    • Watanabe, M.1    Rosenbusch, J.2    Schirmer, T.3    Karplus, M.4
  • 53
    • 0010557822 scopus 로고    scopus 로고
    • A molecular dynamics study of the pores formed by E. coli OmpF porin in a fully hydrated POPE bilayer
    • of special interest
    • Tieleman DP, Berendsen HJC. A molecular dynamics study of the pores formed by E. coli OmpF porin in a fully hydrated POPE bilayer. of special interest Biophys J. 1998; A technical tour de force deploying nanosecond MD simulations of an OmpF porin trimer in a lipid bilayer.
    • (1998) Biophys J
    • Tieleman, D.P.1    Berendsen, H.J.C.2
  • 54
    • 0029862941 scopus 로고    scopus 로고
    • Energy barrier presented to ions by the vestibule of the biological membrane channel
    • Hoyles M, Kuyucak S, Chung SH. Energy barrier presented to ions by the vestibule of the biological membrane channel. Biophys J. 70:1996;1628-1642.
    • (1996) Biophys J , vol.70 , pp. 1628-1642
    • Hoyles, M.1    Kuyucak, S.2    Chung, S.H.3
  • 55
    • 0000244470 scopus 로고
    • Integral weak diffusion and diffusion approximations applied to ion transport through biological ion channels
    • Syganow A, von Kitzing E. Integral weak diffusion and diffusion approximations applied to ion transport through biological ion channels. J Phys Chem. 99:1995;12030-12040.
    • (1995) J Phys Chem , vol.99 , pp. 12030-12040
    • Syganow, A.1    Von Kitzing, E.2
  • 56
    • 0031030225 scopus 로고    scopus 로고
    • Permeation through an open channel: Poisson-Nernst-Planck theory of a synthetic ionic channel
    • Chen D, Lear J, Eisenberg B. Permeation through an open channel: Poisson-Nernst-Planck theory of a synthetic ionic channel. Biophys J. 72:1997;97-116.
    • (1997) Biophys J , vol.72 , pp. 97-116
    • Chen, D.1    Lear, J.2    Eisenberg, B.3
  • 58
    • 0029863372 scopus 로고    scopus 로고
    • Molecular dynamics simulations of water within models of transbilayer pores
    • Breed J, Sankararamakrishnan R, Kerr ID, Sansom MSP. Molecular dynamics simulations of water within models of transbilayer pores. Biophys J. 70:1996;1643-1661.
    • (1996) Biophys J , vol.70 , pp. 1643-1661
    • Breed, J.1    Sankararamakrishnan, R.2    Kerr, I.D.3    Sansom, M.S.P.4
  • 59
    • 0007165005 scopus 로고    scopus 로고
    • Mobility and solvation of ions in channels
    • Lynden-Bell R, Rasaiah JC. Mobility and solvation of ions in channels. J Chem Phys. 105:1996;9266-9280.
    • (1996) J Chem Phys , vol.105 , pp. 9266-9280
    • Lynden-Bell, R.1    Rasaiah, J.C.2
  • 60
    • 0029038366 scopus 로고
    • Interaction of an amphiphilic peptide with a phospholipid-bilayer surface by molecular-dynamics simulation study
    • Huang P, Loew GH. Interaction of an amphiphilic peptide with a phospholipid-bilayer surface by molecular-dynamics simulation study. J Biomol Struct Dyn. 12:1995;937-956.
    • (1995) J Biomol Struct Dyn , vol.12 , pp. 937-956
    • Huang, P.1    Loew, G.H.2
  • 61
    • 0030579817 scopus 로고    scopus 로고
    • Simulation of voltage-dependent interactions of α-helical peptides with lipid bilayers
    • Biggin PC, Sansom MSP. Simulation of voltage-dependent interactions of α-helical peptides with lipid bilayers. Biophys Chem. 60:1996;99-110.
    • (1996) Biophys Chem , vol.60 , pp. 99-110
    • Biggin, P.C.1    Sansom, M.S.P.2
  • 62
    • 0028954965 scopus 로고
    • Calculations of the electrostatic potential adjacent to model phospholipid bilayers
    • Peitzsch RM, Eisenberg M, Sharp KA, McLaughlin S. Calculations of the electrostatic potential adjacent to model phospholipid bilayers. Biophys J. 68:1995;729-738.
    • (1995) Biophys J , vol.68 , pp. 729-738
    • Peitzsch, R.M.1    Eisenberg, M.2    Sharp, K.A.3    McLaughlin, S.4
  • 63
    • 0030754783 scopus 로고    scopus 로고
    • Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles
    • Ben-Tal N, Honig B, Miller C, McLaughlin S. Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles. Biophys J. 73:1997;1717-1727.
    • (1997) Biophys J , vol.73 , pp. 1717-1727
    • Ben-Tal, N.1    Honig, B.2    Miller, C.3    McLaughlin, S.4
  • 64
    • 0010638433 scopus 로고    scopus 로고
    • Simulation and experimental studies of dermaseptin/bilayer interactions
    • La Rocca P, Sansom MSP, Shai Y, Mor A. Simulation and experimental studies of dermaseptin/bilayer interactions. Protein Sci. 6:1997;54.
    • (1997) Protein Sci , vol.6 , pp. 54
    • La Rocca, P.1    Sansom, M.S.P.2    Shai, Y.3    Mor, A.4
  • 65
    • 0027390459 scopus 로고
    • Insertion of peptide chains into lipid membranes: An off-lattice Monte Carlo dynamics model
    • Milik M, Skolnick J. Insertion of peptide chains into lipid membranes: an off-lattice Monte Carlo dynamics model. Proteins. 15:1993;10-25.
    • (1993) Proteins , vol.15 , pp. 10-25
    • Milik, M.1    Skolnick, J.2
  • 66
    • 0029099311 scopus 로고
    • A Monte Carlo model of fd and Pf1 coat proteins in lipid membranes
    • Milik M, Skolnick J. A Monte Carlo model of fd and Pf1 coat proteins in lipid membranes. Biophys J. 69:1995;1382-1386.
    • (1995) Biophys J , vol.69 , pp. 1382-1386
    • Milik, M.1    Skolnick, J.2
  • 67
    • 0024288356 scopus 로고
    • The structure of a membrane-spanning polypeptide studied by molecular dynamics
    • Edholm O, Jähnig F. The structure of a membrane-spanning polypeptide studied by molecular dynamics. Biophys Chem. 30:1988;279-292.
    • (1988) Biophys Chem , vol.30 , pp. 279-292
    • Edholm, O.1    Jähnig, F.2
  • 68
    • 0031022167 scopus 로고    scopus 로고
    • Simulation studies of alamethicin - Bilayer interactions
    • of special interest. MD simulations with a simple bilayer potential suggest voltage-dependent insertion of an alamethicin helix.
    • Biggin P, Breed J, Son HS, Sansom MSP. Simulation studies of alamethicin - bilayer interactions. of special interest Biophys J. 72:1997;627-636 MD simulations with a simple bilayer potential suggest voltage-dependent insertion of an alamethicin helix.
    • (1997) Biophys J , vol.72 , pp. 627-636
    • Biggin, P.1    Breed, J.2    Son, H.S.3    Sansom, M.S.P.4
  • 69
    • 0030916534 scopus 로고    scopus 로고
    • Helix bending in alamethicin: Molecular dynamics simulations and amide hydrogen exchange in methanol
    • Gibbs N, Sessions RB, Williams PB, Dempsey CE. Helix bending in alamethicin: molecular dynamics simulations and amide hydrogen exchange in methanol. Biophys J. 72:1997;2490-2495.
    • (1997) Biophys J , vol.72 , pp. 2490-2495
    • Gibbs, N.1    Sessions, R.B.2    Williams, P.B.3    Dempsey, C.E.4
  • 70
    • 0029669955 scopus 로고    scopus 로고
    • Free-energy determinants of α helix insertion into lipid bilayers
    • of special interest. See annotation [71].
    • Ben-Tal N, Benshaul A, Nicholls A, Honig B. Free-energy determinants of α helix insertion into lipid bilayers. of special interest Biophys J. 70:1996;1803-1812 See annotation [71].
    • (1996) Biophys J , vol.70 , pp. 1803-1812
    • Ben-Tal, N.1    Benshaul, A.2    Nicholls, A.3    Honig, B.4
  • 71
    • 0029768644 scopus 로고    scopus 로고
    • Helix-helix interactions in lipid bilayers
    • of special interest. This and Ben-Tal et al. [70] provide a detailed continuum analysis of hydrophobic helix insertion into and interactions within a lipid bilayer.
    • Ben-Tal N, Honig B. Helix-helix interactions in lipid bilayers. of special interest Biophys J. 71:1996;3046-3050 This and Ben-Tal et al. [70] provide a detailed continuum analysis of hydrophobic helix insertion into and interactions within a lipid bilayer.
    • (1996) Biophys J , vol.71 , pp. 3046-3050
    • Ben-Tal, N.1    Honig, B.2
  • 72
    • 0030038849 scopus 로고    scopus 로고
    • Structure, energetics, and dynamics of lipid-protein interactions - a molecular-dynamics study of the gramicidin-A channel in a DMPC bilayer
    • Woolf TB, Roux B. Structure, energetics, and dynamics of lipid-protein interactions - a molecular-dynamics study of the gramicidin-A channel in a DMPC bilayer. Proteins. 24:1996;92-114.
    • (1996) Proteins , vol.24 , pp. 92-114
    • Woolf, T.B.1    Roux, B.2
  • 73
    • 0030966534 scopus 로고    scopus 로고
    • Transmembrane helix structure, dynamics, and interactions: Multi-nanosecond molecular dynamics simulations
    • of outstanding interest. Nanosecond MD simulations and detailed analysis reveal the fundamentals of interactions of a hydrophobic TM helix with a lipid bilayer. Only the very centre of the helix remains unperturbed by interactions with lipid headgroups or water.
    • Shen L, Bassolino D, Stouch T. Transmembrane helix structure, dynamics, and interactions: multi-nanosecond molecular dynamics simulations. of outstanding interest Biophys J. 73:1997;3-20 Nanosecond MD simulations and detailed analysis reveal the fundamentals of interactions of a hydrophobic TM helix with a lipid bilayer. Only the very centre of the helix remains unperturbed by interactions with lipid headgroups or water.
    • (1997) Biophys J , vol.73 , pp. 3-20
    • Shen, L.1    Bassolino, D.2    Stouch, T.3
  • 74
    • 0000785909 scopus 로고    scopus 로고
    • Threonine mutations in proline helix II of bacteriorhodopsin: A molecular dynamics study
    • Iyer LK, Vishveshwara S. Threonine mutations in proline helix II of bacteriorhodopsin: a molecular dynamics study. J Mol Struct. 361:1996;269-281.
    • (1996) J Mol Struct , vol.361 , pp. 269-281
    • Iyer, L.K.1    Vishveshwara, S.2
  • 75
    • 0030731888 scopus 로고    scopus 로고
    • Molecular dynamics of individual α-helices of bacteriorhodopsin in dimyristoyl phosphatidylcholine. I. Structure and dynamics
    • of special interest. MD simulations of isolated bacteriorhodopsin helices with a bilayer provide insights into the roles of aromatic sidechains and proline residues in modulating the dynamics of TM helices.
    • Woolf TB. Molecular dynamics of individual α-helices of bacteriorhodopsin in dimyristoyl phosphatidylcholine. I. Structure and dynamics. of special interest Biophys J. 73:1997;2376-2392 MD simulations of isolated bacteriorhodopsin helices with a bilayer provide insights into the roles of aromatic sidechains and proline residues in modulating the dynamics of TM helices.
    • (1997) Biophys J , vol.73 , pp. 2376-2392
    • Woolf, T.B.1
  • 76
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerisation: The two stage model
    • Popot JL, Engelman DM. Membrane protein folding and oligomerisation: the two stage model. Biochemistry. 29:1990;4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 77
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R, Baldwin JM, Ceska TA, Zemlin F, Beckmann E, Downing KH. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol Biol. 213:1990;899-929.
    • (1990) J Mol Biol , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 78
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • PebayPeyroula E, Rummel G, Rosenbusch JP, Landau EM. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science. 277:1997;1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebaypeyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 79
    • 0029026347 scopus 로고
    • Structure and fluctuations of bacteriorhodopsin in the purple membrane: A molecular dynamics study
    • Edholm O, Berger O, Jähnig F. Structure and fluctuations of bacteriorhodopsin in the purple membrane: a molecular dynamics study. J Mol Biol. 250:1995;94-111.
    • (1995) J Mol Biol , vol.250 , pp. 94-111
    • Edholm, O.1    Berger, O.2    Jähnig, F.3
  • 80
    • 0029757992 scopus 로고    scopus 로고
    • Thermodynamic stability of water molecules in the bacteriorhodopsin proton channel: A molecular dynamics free energy perturbation study
    • Roux B, Nina M, Pomes R, Smith JC. Thermodynamic stability of water molecules in the bacteriorhodopsin proton channel: a molecular dynamics free energy perturbation study. Biophys J. 71:1996;670-681.
    • (1996) Biophys J , vol.71 , pp. 670-681
    • Roux, B.1    Nina, M.2    Pomes, R.3    Smith, J.C.4
  • 81
    • 0030968284 scopus 로고    scopus 로고
    • Investigation of the proton release channel of bacteriorhodopsin in different intermediates of the photo cycle. A molecular dynamics study
    • Nagel J, Edholm O, Berger O, Jahnig F. Investigation of the proton release channel of bacteriorhodopsin in different intermediates of the photo cycle. A molecular dynamics study. Biochemistry. 36:1997;2875-2883.
    • (1997) Biochemistry , vol.36 , pp. 2875-2883
    • Nagel, J.1    Edholm, O.2    Berger, O.3    Jahnig, F.4
  • 82
    • 0030908397 scopus 로고    scopus 로고
    • a calculations along a bacteriorhodopsin molecular dynamics trajectory
    • A values of ionisable sidechains within bacteriorhodopsin.
    • A values of ionisable sidechains within bacteriorhodopsin.
    • (1997) Biophys Chem , vol.65 , pp. 189-204
    • Sandberg, L.1    Edholm, O.2
  • 83
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr. 24:1991;946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.