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Volumn 33, Issue 6, 2004, Pages 477-489

Homology modelling and molecular dynamics simulations: Comparative studies of human aquaporin-1

Author keywords

Aquaporin; Homology model; MD simulation; Membrane protein

Indexed keywords

AQUAPORIN 1; CARRIER PROTEIN; WATER TRANSPORT AGENT;

EID: 5644279114     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-004-0398-z     Document Type: Article
Times cited : (26)

References (83)
  • 2
    • 0031708266 scopus 로고    scopus 로고
    • Electrostatics and the ion selectivity of ligand-gated ion channels
    • Adcock C, Smith GR, Sansom MSP (1998) Electrostatics and the ion selectivity of ligand-gated ion channels. Biophys J 75:1211-1222
    • (1998) Biophys J , vol.75 , pp. 1211-1222
    • Adcock, C.1    Smith, G.R.2    Sansom, M.S.P.3
  • 3
    • 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
  • 4
    • 0025823857 scopus 로고
    • Proton conductance by the gramicidin water wire
    • Akeson M, Deamer DW (1991) Proton conductance by the gramicidin water wire. Biophys J 60:101-109
    • (1991) Biophys J , vol.60 , pp. 101-109
    • Akeson, M.1    Deamer, D.W.2
  • 5
    • 2242431668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel
    • Bass RB, Strop P, Barclay M, Rees DC (2002) Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel. Science 298:1582-1587
    • (2002) Science , vol.298 , pp. 1582-1587
    • Bass, R.B.1    Strop, P.2    Barclay, M.3    Rees, D.C.4
  • 6
    • 0038472282 scopus 로고    scopus 로고
    • Liquid-vapor oscillations of water in hydrophobic nanopores
    • Beckstein O, Sansom MSP (2003) Liquid-vapor oscillations of water in hydrophobic nanopores. Proc Nat Acad Sci USA 100:7063-7068
    • (2003) Proc Nat Acad Sci USA , vol.100 , pp. 7063-7068
    • Beckstein, O.1    Sansom, M.S.P.2
  • 8
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • Berendsen HJC, van der Spoel D, van Drunen R (1995) GROMACS: A message-passing parallel molecular dynamics implementation. Comp Phys Comm 95:43-56
    • (1995) Comp Phys Comm , vol.95 , pp. 43-56
    • Berendsen, H.J.C.1    Van Der Spoel, D.2    Van Drunen, R.3
  • 10
    • 0035996998 scopus 로고    scopus 로고
    • OmpA - A pore or not a pore? Simulation and modelling studies
    • Bond P, Faraldo-Goméz J, Sansom MSP (2002) OmpA - A pore or not a pore? Simulation and modelling studies. Biophys J 83:763-775
    • (2002) Biophys J , vol.83 , pp. 763-775
    • Bond, P.1    Faraldo-Goméz, J.2    Sansom, M.S.P.3
  • 11
    • 0038724257 scopus 로고    scopus 로고
    • Membrane protein dynamics vs. environment: Simulations of OmpA in a micelle and in a bilayer
    • Bond P, Sansom MSP (2003) Membrane protein dynamics vs. environment: simulations of OmpA in a micelle and in a bilayer. J Mol Biol 329:1035-1053
    • (2003) J Mol Biol , vol.329 , pp. 1035-1053
    • Bond, P.1    Sansom, M.S.P.2
  • 12
    • 0032853219 scopus 로고    scopus 로고
    • Cellular and molecular biology of the aquaporin water channels
    • Borgnia M, Nielsen S, Engel A, Agre P (1999) Cellular and molecular biology of the aquaporin water channels. Annu Rev Biochem 68:425-458
    • (1999) Annu Rev Biochem , vol.68 , pp. 425-458
    • Borgnia, M.1    Nielsen, S.2    Engel, A.3    Agre, P.4
  • 13
    • 0029863372 scopus 로고    scopus 로고
    • Molecular dynamics simulations of water within models of transbilayer pores
    • Breed J, Sankararamakrishnan R, Kerr ID, Sansom MSP (1996) Molecular dynamics simulations of water within models of transbilayer pores. Biophys J 70:1643-1661
    • (1996) Biophys J , vol.70 , pp. 1643-1661
    • Breed, J.1    Sankararamakrishnan, R.2    Kerr, I.D.3    Sansom, M.S.P.4
  • 14
    • 0344825877 scopus 로고    scopus 로고
    • What really prevents proton transport through aquaporin? Charge self-energy versus proton wire proposals
    • Burykin, A., Warshel, A. (2003). What really prevents proton transport through aquaporin? Charge self-energy versus proton wire proposals. Biophys J 85:3696-3706
    • (2003) Biophys J , vol.85 , pp. 3696-3706
    • Burykin, A.1    Warshel, A.2
  • 15
    • 0037007814 scopus 로고    scopus 로고
    • MD Simulations of a K channel model-sensitivity to changes in ions, waters and membrane environment
    • Capener CE, Sansom MSP (2002) MD 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
  • 16
    • 0036286854 scopus 로고    scopus 로고
    • The role and perspective of ab initio molecular dynamics in the study of biological systems
    • Carloni P, Rothlisberger U, Parrinello M (2002) The role and perspective of ab initio molecular dynamics in the study of biological systems. Acc Chem Res 35:455-464
    • (2002) Acc Chem Res , vol.35 , pp. 455-464
    • Carloni, P.1    Rothlisberger, U.2    Parrinello, M.3
  • 17
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang G, Roth CB (2001) Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science 293:1793-1800
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 18
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang G, Spencer RH, Lee AT, Barclay MT, Rees DC (1998) Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science 282:2220-2226
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 19
    • 33846823909 scopus 로고
    • Particle mesh Ewald - An N.log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L (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
  • 20
    • 0026124585 scopus 로고
    • Electrostatics and diffusion of molecules in solution: Simulations with the University of Houston Brownian dynamics program
    • Davis ME, Madura JD, Luty BA, McCammon JA (1991) Electrostatics and diffusion of molecules in solution: simulations with the University of Houston Brownian dynamics program. Comput Phys Comm 62:187-197
    • (1991) Comput Phys Comm , vol.62 , pp. 187-197
    • Davis, M.E.1    Madura, J.D.2    Luty, B.A.3    McCammon, J.A.4
  • 21
    • 0035861454 scopus 로고    scopus 로고
    • Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and GlpF
    • de Groot BL, Grubmuller H (2001) Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and GlpF. Science 294:2353-2357
    • (2001) Science , vol.294 , pp. 2353-2357
    • De Groot, B.L.1    Grubmuller, H.2
  • 22
    • 0035979744 scopus 로고    scopus 로고
    • A refined structure of human aquaporin-1
    • de Groot BL, Engel A, Grubmüller H (2001) A refined structure of human aquaporin-1. FEBS Lett 504:206-211
    • (2001) FEBS Lett , vol.504 , pp. 206-211
    • De Groot, B.L.1    Engel, A.2    Grubmüller, H.3
  • 23
    • 0141534474 scopus 로고    scopus 로고
    • The mechanism of proton exclusion in the aquaporin-1 water channel
    • de Groot BL, Frigato T, Helms V, Grubmuller H (2003) The mechanism of proton exclusion in the aquaporin-1 water channel. J Mol Biol 333:279-293
    • (2003) J Mol Biol , vol.333 , pp. 279-293
    • De Groot, B.L.1    Frigato, T.2    Helms, V.3    Grubmuller, H.4
  • 25
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
    • Dutzler R, Campbell EB, Cadene M, Chait BT, MacKinnon R (2002) X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature 415:287-294
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 26
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser A, Kinh Gian Do R, Sali A (2000) Modeling of loops in protein structures. Prot Sci 9:1753-1773
    • (2000) Prot Sci , vol.9 , pp. 1753-1773
    • Fiser, A.1    Kinh Gian Do, R.2    Sali, A.3
  • 27
    • 0034030929 scopus 로고    scopus 로고
    • Exploring models of the Influenza A M2 channel:- MD Simulations in a lipid bilayer
    • Forrest LR, Kukol A, Arkin IT, Tieleman DP, Sansom MSP (2000) Exploring models of the Influenza A M2 channel:- MD Simulations in a lipid bilayer. Biophys J 78:55-69
    • (2000) Biophys J , vol.78 , pp. 55-69
    • Forrest, L.R.1    Kukol, A.2    Arkin, I.T.3    Tieleman, D.P.4    Sansom, M.S.P.5
  • 30
    • 0037071785 scopus 로고    scopus 로고
    • Potassium permeation through the KcsA channel: A density functional study
    • Guidoni L, Carloni P (2002) Potassium permeation through the KcsA channel: a density functional study. Biochim Biophys Acta 1563:1-6
    • (2002) Biochim Biophys Acta , vol.1563 , pp. 1-6
    • Guidoni, L.1    Carloni, P.2
  • 31
    • 0034623015 scopus 로고    scopus 로고
    • Statistical alignment: Computational properties, homology testing and goodness-of-fit
    • Hein J, Wiuf C, Knudsen B, Moller MB, Wibling G (2000) Statistical alignment: computational properties, homology testing and goodness-of-fit. J Mol Biol 302:265-279
    • (2000) J Mol Biol , vol.302 , pp. 265-279
    • Hein, J.1    Wiuf, C.2    Knudsen, B.3    Moller, M.B.4    Wibling, G.5
  • 34
    • 0034723156 scopus 로고    scopus 로고
    • Structural clues in the sequences of the aquaporins
    • Heymann JB, Engel A (2000) Structural clues in the sequences of the aquaporins. J Mol Biol 295:1039-1053
    • (2000) J Mol Biol , vol.295 , pp. 1039-1053
    • Heymann, J.B.1    Engel, A.2
  • 36
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Huang Y, Lemieux MJ, Song J, Auer M, Wang DN (2003) Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301:616-620
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 38
    • 0035183282 scopus 로고    scopus 로고
    • The mechanism of glycerol conduction in aquaglyceroporins
    • Jensen MO, Tajkhorshid E, Schulten K (2001) The mechanism of glycerol conduction in aquaglyceroporins. Structure 9:1083-1093
    • (2001) Structure , vol.9 , pp. 1083-1093
    • Jensen, M.O.1    Tajkhorshid, E.2    Schulten, K.3
  • 39
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R (2002) Crystal structure and mechanism of a calcium-gated potassium channel. Nature 417:515-522
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 41
    • 0028318868 scopus 로고
    • Molecular structure of the water channel through aquaporin CHIP: The hourglass model
    • Jung JS, Preston GM, Smith BL, Guggino WB, Agre P (1994) Molecular structure of the water channel through aquaporin CHIP: the hourglass model. J Biol Chem 269:14648-14654
    • (1994) J Biol Chem , vol.269 , pp. 14648-14654
    • Jung, J.S.1    Preston, G.M.2    Smith, B.L.3    Guggino, W.B.4    Agre, P.5
  • 42
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure:- Pattern-recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C (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
  • 43
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24:946-950
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 45
    • 0000243829 scopus 로고
    • Procheck - A program to check the stereochemical quality of protein structures
    • Laskowski RA, Macarthur MW, Moss DS, Thornton JM (1993) Procheck - a program to check the stereochemical quality of protein structures. J Appl Cryst 26:283-291
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 46
    • 0033996292 scopus 로고    scopus 로고
    • Structure and dynamics of the pore-lining helix of the nicotinic receptor: MD simulations in water, lipid bilayers and transbilayer bundles
    • Law RJ, Forrest LR, Ranatunga KM, La Rocca P, Tieleman DP, Sansom MSP (2000) Structure and dynamics of the pore-lining helix of the nicotinic receptor: MD simulations in water, lipid bilayers and transbilayer bundles. Proteins Struct Funct Genet 39:47-55
    • (2000) Proteins Struct Funct Genet , vol.39 , pp. 47-55
    • Law, R.J.1    Forrest, L.R.2    Ranatunga, K.M.3    La Rocca, P.4    Tieleman, D.P.5    Sansom, M.S.P.6
  • 47
    • 12244294449 scopus 로고    scopus 로고
    • Pores formed by the nicotinic receptor M2δ peptide: A molecular dynamics simulation study
    • Law RJ, Tieleman DP, Sansom MSP (2003) Pores formed by the nicotinic receptor M2δ peptide: a molecular dynamics simulation study. Biophys J 84:14-27
    • (2003) Biophys J , vol.84 , pp. 14-27
    • Law, R.J.1    Tieleman, D.P.2    Sansom, M.S.P.3
  • 48
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher KP, Lee AT, Rees DC (2002) The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296:1091-1098
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 53
    • 0029910115 scopus 로고    scopus 로고
    • Phylogenetic characterization of the MIP family of transmembrane channel proteins
    • Park JH, Saier MH (1996) Phylogenetic characterization of the MIP family of transmembrane channel proteins. J Membr Biol 153:171-180
    • (1996) J Membr Biol , vol.153 , pp. 171-180
    • Park, J.H.1    Saier, M.H.2
  • 54
    • 0030011088 scopus 로고    scopus 로고
    • + translocation along the single-file water chain in the gramicidin A channel
    • + translocation along the single-file water chain in the gramicidin A channel. Biophys J 71:19-39
    • (1996) Biophys J , vol.71 , pp. 19-39
    • Pomes, R.1    Roux, B.2
  • 55
    • 0036225143 scopus 로고    scopus 로고
    • + conduction in the single-file water chain of the gramicidin channel
    • + conduction in the single-file water chain of the gramicidin channel. Biophys J 82:2304-2316
    • (2002) Biophys J , vol.82 , pp. 2304-2316
    • Pomes, R.1    Roux, B.2
  • 56
    • 0030598343 scopus 로고    scopus 로고
    • Deviations from standard atomic volumes as a quality measure for protein crystal structures
    • Pontius J, Richelle J, Wodak S (1996) Deviations from standard atomic volumes as a quality measure for protein crystal structures. J Mol Biol 264:121-136
    • (1996) J Mol Biol , vol.264 , pp. 121-136
    • Pontius, J.1    Richelle, J.2    Wodak, S.3
  • 57
    • 5644237695 scopus 로고
    • The mercury sensitive residue at cys-189 in CHIP28 protein
    • Preston GM, Jung JS, Guggino WB, Agre P (1993) The mercury sensitive residue at cys-189 in CHIP28 protein. Science 256:385-387
    • (1993) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Jung, J.S.2    Guggino, W.B.3    Agre, P.4
  • 58
    • 0035852730 scopus 로고    scopus 로고
    • Visualization of a water-selective pore by electron crystallography in vitreous ice
    • Ren G, Reddy VS, Cheng A, Melnyk P, Mitra AK (2001) Visualization of a water-selective pore by electron crystallography in vitreous ice. Proc Natl Acad Sci USA 98:1398-1403
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1398-1403
    • Ren, G.1    Reddy, V.S.2    Cheng, A.3    Melnyk, P.4    Mitra, A.K.5
  • 59
    • 0029781535 scopus 로고    scopus 로고
    • Grand canonical ensemble Monte Carlo simulation of the dCpG/proflavine crystal hydrate
    • Resat H, Mezei M (1996) Grand canonical ensemble Monte Carlo simulation of the dCpG/proflavine crystal hydrate. Biophys J 71:1179-1190
    • (1996) Biophys J , vol.71 , pp. 1179-1190
    • Resat, H.1    Mezei, M.2
  • 60
    • 0031718310 scopus 로고    scopus 로고
    • Homology modelling, model and software evaluation: Three related sources
    • Rodriguez R, Chinea G, Lopez N, Pons T, Vriend G (1998) Homology modelling, model and software evaluation: three related sources. CABIOS 14:523-528
    • (1998) CABIOS , vol.14 , pp. 523-528
    • Rodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 61
    • 0030735981 scopus 로고    scopus 로고
    • Influence of the membrane potential on the free energy of an intrinsic protein
    • Roux B (1997) Influence of the membrane potential on the free energy of an intrinsic protein. Biophys J 73:2980-2989
    • (1997) Biophys J , vol.73 , pp. 2980-2989
    • Roux, B.1
  • 62
    • 0033019968 scopus 로고    scopus 로고
    • Statistical mechanical equilibrium theory of selective ion channels
    • Roux B (1999) Statistical mechanical equilibrium theory of selective ion channels. Biophys J 77:139-153
    • (1999) Biophys J , vol.77 , pp. 139-153
    • Roux, B.1
  • 63
    • 0037084366 scopus 로고    scopus 로고
    • Electrostatic interactions in a neutral model phospholipid bilayer by molecular dynamics simulations
    • Saiz L, Klein ML (2002) Electrostatic interactions in a neutral model phospholipid bilayer by molecular dynamics simulations. J Chem Phys 116:3052-3057
    • (2002) J Chem Phys , vol.116 , pp. 3052-3057
    • Saiz, L.1    Klein, M.L.2
  • 64
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A, Blundell TL (1993) Comparative protein modeling by satisfaction of spatial restraints. J Mol Biol 234:779-815
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 66
    • 11644271492 scopus 로고    scopus 로고
    • Multistate empirical valence bond model for proton transport in water
    • Schmitt UW, Voth GA (1998) Multistate empirical valence bond model for proton transport in water. J Phys Chem B 102:5547-5551
    • (1998) J Phys Chem B , vol.102 , pp. 5547-5551
    • Schmitt, U.W.1    Voth, G.A.2
  • 67
    • 0034036372 scopus 로고    scopus 로고
    • Simulations of ion permeation through a potassium channel: Molecular dynamics of KcsA in a phospholipid bilayer
    • Shrivastava IH, Sansom MSP (2000) Simulations of ion permeation through a potassium channel: molecular dynamics of KcsA in a phospholipid bilayer. Biophys J 78:557-570
    • (2000) Biophys J , vol.78 , pp. 557-570
    • Shrivastava, I.H.1    Sansom, M.S.P.2
  • 69
    • 0030404988 scopus 로고    scopus 로고
    • Hole: A program for the analysis of the pore dimensions of ion channel structural models
    • Smart OS, Neduvelil JG, Wang X, Wallace BA, Sansom MSP (1996) Hole: A program for the analysis of the pore dimensions of ion channel structural models. J Mol Graph 14:354-360
    • (1996) J Mol Graph , vol.14 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.P.5
  • 70
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • Sui HX, Han BG, Lee JK, Walian P, Jap BK (2001) Structural basis of water-specific transport through the AQP1 water channel. Nature 414:872-878
    • (2001) Nature , vol.414 , pp. 872-878
    • Sui, H.X.1    Han, B.G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 72
    • 0035979797 scopus 로고    scopus 로고
    • Overexpression of mammalian integral membrane proteins for structural studies
    • Tate CG (2001) Overexpression of mammalian integral membrane proteins for structural studies. FEBS Lett 504:94-98
    • (2001) FEBS Lett , vol.504 , pp. 94-98
    • Tate, C.G.1
  • 73
    • 0033035249 scopus 로고    scopus 로고
    • An alamethicin channel in a lipid bilayer: Molecular dynamics simulations
    • Tieleman DP, Berendsen HJC, Sansom MSP (1999) An alamethicin channel in a lipid bilayer: molecular dynamics simulations. Biophys J 76:1757-1769
    • (1999) Biophys J , vol.76 , pp. 1757-1769
    • Tieleman, D.P.1    Berendsen, H.J.C.2    Sansom, M.S.P.3
  • 74
    • 0035132984 scopus 로고    scopus 로고
    • Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces
    • Tieleman DP, Berendsen HJC, Sansom MSP (2001a) Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces. Biophys J 80:331-346
    • (2001) Biophys J , vol.80 , pp. 331-346
    • Tieleman, D.P.1    Berendsen, H.J.C.2    Sansom, M.S.P.3
  • 75
    • 0035705881 scopus 로고    scopus 로고
    • Simulation approaches to ion channel structure-function relationships
    • Tieleman DP, Biggin PC, Smith GR, Sansom MSP (2001b) Simulation approaches to ion channel structure-function relationships. Q Rev Biophys 34:473-561
    • (2001) Q Rev Biophys , vol.34 , pp. 473-561
    • Tieleman, D.P.1    Biggin, P.C.2    Smith, G.R.3    Sansom, M.S.P.4
  • 76
    • 0036841855 scopus 로고    scopus 로고
    • Analysis and evaluation of channel models: Simulations of alamethicin
    • Tieleman DP, Hess B, Sansom MSP (2002) Analysis and evaluation of channel models: simulations of alamethicin. Biophys J 83:2393-3407
    • (2002) Biophys J , vol.83 , pp. 2393-3407
    • Tieleman, D.P.1    Hess, B.2    Sansom, M.S.P.3
  • 77
    • 0035312897 scopus 로고    scopus 로고
    • Electrostatics calculations: Recent methodological advances and applications to membranes
    • Tobias DJ (2001) Electrostatics calculations: recent methodological advances and applications to membranes. Curr Opin Struct Biol 11:253-261
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 253-261
    • Tobias, D.J.1
  • 81
    • 5644251597 scopus 로고    scopus 로고
    • Computer simulation studies of proton transport in a synthetic ion channel
    • Wu Y, Voth G (2002) Computer simulation studies of proton transport in a synthetic ion channel. Biophys J 82:1016
    • (2002) Biophys J , vol.82 , pp. 1016
    • Wu, Y.1    Voth, G.2
  • 83
    • 0035979666 scopus 로고    scopus 로고
    • Molecular dynamics study of aquaporin-1 water channel in a lipid bilayer
    • Zhu FQ, Tajkhorshid E, Schulten K (2001) Molecular dynamics study of aquaporin-1 water channel in a lipid bilayer. FEBS Lett 504:212-218
    • (2001) FEBS Lett , vol.504 , pp. 212-218
    • Zhu, F.Q.1    Tajkhorshid, E.2    Schulten, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.