메뉴 건너뛰기




Volumn 21, Issue 3, 2004, Pages 151-161

The simulation approach to bacterial outer membrane proteins

Author keywords

Brownian dynamics simulation; Lipid protein interactions; Molecular dynamics simulation; Outer membrane protein; Porin

Indexed keywords

MEMBRANE ENZYME; MEMBRANE PROTEIN; PORIN; SOLVENT;

EID: 2942564158     PISSN: 09687688     EISSN: None     Source Type: Journal    
DOI: 10.1080/0968760410001699169     Document Type: Review
Times cited : (60)

References (82)
  • 2
    • 0035443197 scopus 로고    scopus 로고
    • Biophysical approaches to membrane protein structure determination
    • Arora, A. and Tamm, L. K., 2001, Biophysical approaches to membrane protein structure determination. Curr. Opin. Struct Biol., 11, 540-547.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 540-547
    • Arora, A.1    Tamm, L.K.2
  • 3
    • 0034695440 scopus 로고    scopus 로고
    • Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers
    • Arora, A., Rinehart, D., Szabo, G. and Tamm, L. K., 2000, Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers. J. Biol. Chem., 275, 1594-1600.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1594-1600
    • Arora, A.1    Rinehart, D.2    Szabo, G.3    Tamm, L.K.4
  • 4
    • 0035066331 scopus 로고    scopus 로고
    • Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
    • Arora, A., Abildgaard, F., Bushweller, J. H. and Tamm, L. K., 2001, Structure of outer membrane protein A transmembrane domain by NMR spectroscopy. Nat. Struct. Biol., 8, 334-338.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 334-338
    • Arora, A.1    Abildgaard, F.2    Bushweller, J.H.3    Tamm, L.K.4
  • 5
    • 0037485850 scopus 로고    scopus 로고
    • A molecular dynamics investigation of mono and dimeric states of the outer membrane enzyme OMPLA
    • Baaden, M., Meier, C. and Sansom, M. S. P., 2003, A molecular dynamics investigation of mono and dimeric states of the outer membrane enzyme OMPLA. J. Mol. Biol., 331, 177-189.
    • (2003) J. Mol. Biol. , vol.331 , pp. 177-189
    • Baaden, M.1    Meier, C.2    Sansom, M.S.P.3
  • 6
    • 0032563173 scopus 로고    scopus 로고
    • Voltage gating is a fundamental feature of porin and toxin beta-barrel membrane channels
    • Bainbridge, G., Gokce, I. and Lakey, J. H., 1998, Voltage gating is a fundamental feature of porin and toxin beta-barrel membrane channels. FEBS Lett., 431, 305-308.
    • (1998) FEBS Lett. , vol.431 , pp. 305-308
    • Bainbridge, G.1    Gokce, I.2    Lakey, J.H.3
  • 7
    • 0030966570 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Benz, J. and Hofmann, A., 1997, Annexins: from structure to function. Biol. Chem., 378, 177-183.
    • (1997) Biol. Chem. , vol.378 , pp. 177-183
    • Benz, J.1    Hofmann, A.2
  • 8
    • 0028269774 scopus 로고
    • On the stability and plastic properties of the interior L3 loop in R. capsulatus porin. A molecular dynamics study
    • Björkstén, J., Soares, C. M., Nilsson, O. and Tapia, O., 1994, On the stability and plastic properties of the interior L3 loop in R. capsulatus porin. A molecular dynamics study. Prot. Eng., 7, 487-493.
    • (1994) Prot. Eng. , vol.7 , pp. 487-493
    • Björkstén, J.1    Soares, C.M.2    Nilsson, O.3    Tapia, O.4
  • 9
    • 0038724257 scopus 로고    scopus 로고
    • Membrane protein dynamics vs. environment: Simulations of OmpA in a micelle and in a bilayer
    • Bond, P. and Sansom, M. S. P., 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
  • 10
    • 0035996998 scopus 로고    scopus 로고
    • OmpAA pore or not a pore? Simulation and modelling studies
    • Bond, P., Faraldo-Goméz, J. and Sansom, M. S. P., 2002, OmpAA 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
  • 12
    • 0242670022 scopus 로고    scopus 로고
    • Substrate-induced transmembrane signaling in the cobalamin transporter BtuB
    • Chimento, D. P., Mohanty, A. K., Kadner, R. J. and Wiener, M. C., 2003, Substrate-induced transmembrane signaling in the cobalamin transporter BtuB. Nat. Struct. Biol., 10, 394-401.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 394-401
    • Chimento, D.P.1    Mohanty, A.K.2    Kadner, R.J.3    Wiener, M.C.4
  • 13
    • 0037470691 scopus 로고    scopus 로고
    • Ab initio folding simulation of the trp-cage mini-protein approaches NMR resolution
    • Chowdhury, S., Lee, M. C., Xiong, G. and Duan, Y., 2003, Ab initio folding simulation of the trp-cage mini-protein approaches NMR resolution. J. Mol. Biol., 327, 711-717.
    • (2003) J. Mol. Biol. , vol.327 , pp. 711-717
    • Chowdhury, S.1    Lee, M.C.2    Xiong, G.3    Duan, Y.4
  • 14
    • 0036656435 scopus 로고    scopus 로고
    • Ion channels: Recent progress and prospects
    • Chung, S. H. and Kuyucak, S., 2002, Ion channels: recent progress and prospects. Eur. Biophys. J., 31, 283-293.
    • (2002) Eur. Biophys. J. , vol.31 , pp. 283-293
    • Chung, S.H.1    Kuyucak, S.2
  • 15
    • 0041663886 scopus 로고    scopus 로고
    • Molecular origin of the cation selectivity in OmpF porin: Single channel conductances vs. free energy calculation
    • Danelon, C., Suenaga, A., Winterhalter, M. and Yamato, I., 2003, Molecular origin of the cation selectivity in OmpF porin: single channel conductances vs. free energy calculation. Biophys. Chem., 104, 591-603.
    • (2003) Biophys. Chem. , vol.104 , pp. 591-603
    • Danelon, C.1    Suenaga, A.2    Winterhalter, M.3    Yamato, I.4
  • 16
    • 4243463817 scopus 로고
    • Electrostatics in biomolecular structure and dynamics
    • Davis, M. E. and McCammon, J. A., 1990, Electrostatics in biomolecular structure and dynamics. Chem. Rev., 90, 509-521.
    • (1990) Chem. Rev. , vol.90 , pp. 509-521
    • Davis, M.E.1    McCammon, J.A.2
  • 17
    • 0242696086 scopus 로고    scopus 로고
    • Membrane protein simulation: Ion channels and bacterial outer membrane proteins
    • Domene, C., Bond, P. and Sansom, M. S. P., 2003a, Membrane protein simulation: ion channels and bacterial outer membrane proteins. Adv. Prot. Chem., 66, 159-193.
    • (2003) Adv. Prot. Chem. , vol.66 , pp. 159-193
    • Domene, C.1    Bond, P.2    Sansom, M.S.P.3
  • 18
    • 0344236133 scopus 로고    scopus 로고
    • Lipid-protein interactions and the membrane/water interfacial region
    • Domene, C., Bond, P. J., Deol, S. S. and Sansom, M. S. P., 2003b, Lipid-protein interactions and the membrane/water interfacial region. J. Amer. Chem. Soc., 125, 14966-14967.
    • (2003) J. Amer. Chem. Soc. , vol.125 , pp. 14966-14967
    • Domene, C.1    Bond, P.J.2    Deol, S.S.3    Sansom, M.S.P.4
  • 20
    • 0036710071 scopus 로고    scopus 로고
    • Translocation mechanism of long sugar chains across the maltoporin membrane channel
    • Dutzler, R., Schirmer, T., Karplus, M. and Fischer, S., 2002, Translocation mechanism of long sugar chains across the maltoporin membrane channel. Structure, 10, 1273-1284.
    • (2002) Structure , vol.10 , pp. 1273-1284
    • Dutzler, R.1    Schirmer, T.2    Karplus, M.3    Fischer, S.4
  • 21
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • Dutzler, R., Campbell, E. B. and MacKinnon, R., 2003, Gating the selectivity filter in ClC chloride channels. Science, 300, 108-112.
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 23
    • 0036618993 scopus 로고    scopus 로고
    • Setup and optimisation of membrane protein simulations
    • Faraldo-Gȯmez, J., Smith, G. R. and Sansom, M. S. P., 2002, Setup and optimisation of membrane protein simulations. Eur. Biophys. J., 31, 217-227.
    • (2002) Eur. Biophys. J. , vol.31 , pp. 217-227
    • Faraldo-Gomez, J.1    Smith, G.R.2    Sansom, M.S.P.3
  • 24
    • 0037671392 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the bacterial outer membrane protein FhuA: A comparative study of the ferrichrome-free and bound states
    • Faraldo-Gȯmez, J., Smith, G. R. and Sansom, M. S. P., 2003, Molecular dynamics simulations of the bacterial outer membrane protein FhuA: a comparative study of the ferrichrome-free and bound states. Biophys. J., 85, 1-15.
    • (2003) Biophys. J. , vol.85 , pp. 1-15
    • Faraldo-Gomez, J.1    Smith, G.R.2    Sansom, M.S.P.3
  • 25
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K. and Welte, W., 1998, Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science, 282, 2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 28
    • 0242488921 scopus 로고    scopus 로고
    • NMR solution structure determination of membrane proteins reconstituted in detergent micelles
    • Fernȧndez, C. and Wüthrich, K., 2003, NMR solution structure determination of membrane proteins reconstituted in detergent micelles. FEBS Lett., 555, 144-150.
    • (2003) FEBS Lett. , vol.555 , pp. 144-150
    • Fernandez, C.1    Wüthrich, K.2
  • 30
    • 0035252652 scopus 로고    scopus 로고
    • Probing the interface between membrane proteins and membrane lipids by X-ray crystallography
    • Fyfe, P. K., McAuley, K. E., Roszak, A. W., Isaacs, N. W., Codgell, R. J. and Jones, M. R., 2001, Probing the interface between membrane proteins and membrane lipids by X-ray crystallography. Trends Biochem. Sci., 26, 106-112.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 106-112
    • Fyfe, P.K.1    McAuley, K.E.2    Roszak, A.W.3    Isaacs, N.W.4    Codgell, R.J.5    Jones, M.R.6
  • 33
    • 0035828343 scopus 로고    scopus 로고
    • Brownian dynamics simulations of ion channels: A general treatment of electrostatic reaction fields for molecular pores of arbitrary geometry
    • Im, W. and Roux, B., 2001, Brownian dynamics simulations of ion channels: a general treatment of electrostatic reaction fields for molecular pores of arbitrary geometry. J. Chem. Phys., 115, 4850-4861.
    • (2001) J. Chem. Phys. , vol.115 , pp. 4850-4861
    • Im, W.1    Roux, B.2
  • 34
    • 0036389892 scopus 로고    scopus 로고
    • Ion permeation and selectivity of OmpF porin: A theoretical study based on molecular dynamics, Brownian dynamics, and continuum electrodiffusion theory
    • Im, W. and Roux, B., 2002a, Ion permeation and selectivity of OmpF porin: a theoretical study based on molecular dynamics, Brownian dynamics, and continuum electrodiffusion theory. J. Mol. Biol., 322, 851-869.
    • (2002) J. Mol. Biol. , vol.322 , pp. 851-869
    • Im, W.1    Roux, B.2
  • 35
    • 0036301334 scopus 로고    scopus 로고
    • Ions and counterions in a biological channel: A molecular dynamics simulation of OmpF porin from Escherichia coli in an explicit membrane with 1 M KCl aqueous salt solution
    • Im, W. and Roux, B., 2002b, Ions and counterions in a biological channel: a molecular dynamics simulation of OmpF porin from Escherichia coli in an explicit membrane with 1 M KCl aqueous salt solution. J. Mol. Biol., 319, 1177-1197.
    • (2002) J. Mol. Biol. , vol.319 , pp. 1177-1197
    • Im, W.1    Roux, B.2
  • 36
    • 0036301334 scopus 로고    scopus 로고
    • Ions and counterions in a biological channel: A molecular dynamics simulation of OmpF porin from Escherichia coli in an explicit membrane with 1 M KCl aqueous salt solution
    • Im, W. and Roux, B., 2002c, Ions and counterions in a biological channel: a molecular dynamics simulation of OmpF porin from Escherichia coli in an explicit membrane with 1 M KCl aqueous salt solution. J. Mol. Biol., 319, 1177-1197.
    • (2002) J. Mol. Biol. , vol.319 , pp. 1177-1197
    • Im, W.1    Roux, B.2
  • 37
    • 0033884302 scopus 로고    scopus 로고
    • Grand canonical Monte Carlo-Brownian dynamics algorithm for simulating ion channels
    • Im, W., Seefeld, S. and Roux, B., 2000, Grand canonical Monte Carlo-Brownian dynamics algorithm for simulating ion channels. Biophys. J., 79, 788-801.
    • (2000) Biophys. J. , vol.79 , pp. 788-801
    • Im, W.1    Seefeld, S.2    Roux, B.3
  • 38
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • Karplus, M. and McCammon, J. A., 2002a, Molecular dynamics simulations of biomolecules. Nat. Struct. Biol., 9, 646-652.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 39
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • Karplus, M. J. and McCammon, J. A., 2002b, Molecular dynamics simulations of biomolecules. Nat. Struct. Biol., 9, 646-652.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 646-652
    • Karplus, M.J.1    McCammon, J.A.2
  • 41
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • Killian, J. A. and von Heijne, G., 2000, How proteins adapt to a membrane-water interface. Trends Biochem. Sci., 25, 429-434.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 429-434
    • Killian, J.A.1    Von Heijne, G.2
  • 42
    • 0033942874 scopus 로고    scopus 로고
    • Structure and function of bacterial outer membrane proteins: Barrels in a nutshell
    • Koebnik, R., Locher, K. P. and Van Gelder, P., 2000, Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol. Microbiol., 37, 239-253.
    • (2000) Mol. Microbiol. , vol.37 , pp. 239-253
    • Koebnik, R.1    Locher, K.P.2    Van Gelder, P.3
  • 43
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis, V., Sharff, A., Koronakis, E., Luisi, B. and Hughes, C., 2000, Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature, 405, 914-919.
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 44
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee, A. G., 2003, Lipid-protein interactions in biological membranes: a structural perspective. Biochim. Biophys. Acta, 1612, 1-40.
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 45
    • 0034907678 scopus 로고    scopus 로고
    • Computer simulation of the rough lipopolysaccharide membrane of Pseudomonas aeruginosa
    • Lins, R. D. and Straatsma, T. P., 2001, Computer simulation of the rough lipopolysaccharide membrane of Pseudomonas aeruginosa. Biophys. J., 81, 1037-1046.
    • (2001) Biophys. J. , vol.81 , pp. 1037-1046
    • Lins, R.D.1    Straatsma, T.P.2
  • 46
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signalling across the ligand-gated FhuA receptor; crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • Locher, K. P., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J. and Moras, D., 1998, Transmembrane signalling across the ligand-gated FhuA receptor; crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell, 95, 771-778.
    • (1998) Cell , vol.95 , pp. 771-778
    • Locher, K.P.1    Rees, B.2    Koebnik, R.3    Mitschler, A.4    Moulinier, L.5    Rosenbusch, J.6    Moras, D.7
  • 49
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. and Honig, B., 1991, Protein folding and association: insights from the interfacial thermodynamic properties of hydrocarbons. Proteins: Struct. Func. Genet., 11, 281-296.
    • (1991) Proteins: Struct. Func. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 50
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H., 2003, Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Molec. Biol. Rev., 67, 593-656.
    • (2003) Microbiol. Molec. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 51
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • Pautsch, A. and Schulz, G. E., 1998, Structure of the outer membrane protein A transmembrane domain. Nat. Struct. Biol., 5, 1013-1017.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 52
    • 0034724567 scopus 로고    scopus 로고
    • High-resolution structure of the OmpA membrane domain
    • Pautsch, A. and Schulz, G. E., 2000, High-resolution structure of the OmpA membrane domain. J. Mol. Biol., 298, 273-282.
    • (2000) J. Mol. Biol. , vol.298 , pp. 273-282
    • Pautsch, A.1    Schulz, G.E.2
  • 54
    • 0035967529 scopus 로고    scopus 로고
    • Role of charged residues at the OmpF porin channel constriction probed by mutagenesis and simulation
    • Phale, P. S., Philippsen, A., Widmer, C., Phale, V. P., Rosenbusch, J. P. and Schirmer, T., 2001, Role of charged residues at the OmpF porin channel constriction probed by mutagenesis and simulation. Biochemistry, 40, 6319-6325.
    • (2001) Biochemistry , vol.40 , pp. 6319-6325
    • Phale, P.S.1    Philippsen, A.2    Widmer, C.3    Phale, V.P.4    Rosenbusch, J.P.5    Schirmer, T.6
  • 55
    • 0037133637 scopus 로고    scopus 로고
    • Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis
    • Prince, S. M., Achtman, M. and Derrick, J. P., 2002, Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis. Proc. Natl Acad. Sci. USA, 99, 3417-3421.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3417-3421
    • Prince, S.M.1    Achtman, M.2    Derrick, J.P.3
  • 56
    • 0037174185 scopus 로고    scopus 로고
    • Orientation and interactions of dipolar molecules during transport through OmpF porin
    • Robertson, K. M. and Tieleman, D. P., 2002, Orientation and interactions of dipolar molecules during transport through OmpF porin. FEBS Lett., 528, 53-57.
    • (2002) FEBS Lett. , vol.528 , pp. 53-57
    • Robertson, K.M.1    Tieleman, D.P.2
  • 57
    • 0039179572 scopus 로고    scopus 로고
    • Ion channels, permeation and electrostatics: Insight into the function of KcsA
    • Roux, B., Bernèche, S. and Im, W., 2000, Ion channels, permeation and electrostatics: insight into the function of KcsA. Biochemistry, 39, 13295-13306.
    • (2000) Biochemistry , vol.39 , pp. 13295-13306
    • Roux, B.1    Bernèche, S.2    Im, W.3
  • 58
    • 0031857538 scopus 로고    scopus 로고
    • General and specific porins from bacterial outer membranes
    • Schirmer, T., 1998, General and specific porins from bacterial outer membranes. J. Struct. Biol., 121, 101-109.
    • (1998) J. Struct. Biol. , vol.121 , pp. 101-109
    • Schirmer, T.1
  • 59
    • 0033579482 scopus 로고    scopus 로고
    • Brownian dynamics simulation of ion flow through porin channels
    • Schirmer, T. and Phale, P. S., 1999, Brownian dynamics simulation of ion flow through porin channels. J. Mol. Biol., 294, 1159-1167.
    • (1999) J. Mol. Biol. , vol.294 , pp. 1159-1167
    • Schirmer, T.1    Phale, P.S.2
  • 60
    • 0037114710 scopus 로고    scopus 로고
    • Molecular structure of the outer bacterial membrane of Pseudomonas aeruginosa via classical simulation
    • Schroll, R. M. and Straatsma, T. P., 2002, Molecular structure of the outer bacterial membrane of Pseudomonas aeruginosa via classical simulation. Biopolymers, 65, 395-407.
    • (2002) Biopolymers , vol.65 , pp. 395-407
    • Schroll, R.M.1    Straatsma, T.P.2
  • 61
    • 0033932639 scopus 로고    scopus 로고
    • β-barrel membrane proteins
    • Schulz, G. E., 2000, β-Barrel membrane proteins. Curr. Opin. Struct. Biol., 10, 443-447.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 443-447
    • Schulz, G.E.1
  • 63
    • 0037174385 scopus 로고    scopus 로고
    • All-atom structure prediction and folding simulations of a stable protein
    • Simmerling, C., Strockbine, B. and Roitberg, A. E., 2002, All-atom structure prediction and folding simulations of a stable protein. J. Am. Chem. Soc., 124, 11258-11259.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11258-11259
    • Simmerling, C.1    Strockbine, B.2    Roitberg, A.E.3
  • 64
    • 0030404988 scopus 로고    scopus 로고
    • Hole: A program for the analysis of the pore dimensions of ion channel structural models
    • Smart, O. S., Neduvelil, J. G., Wang, X., Wallace, B. A. and Sansom, M. S. P., 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
  • 65
    • 0034739438 scopus 로고    scopus 로고
    • Bacterial phospholipase A: Structure and function of an integral membrane phospholipase
    • Snijder, H. J. and Dijkstra, B. W., 2000, Bacterial phospholipase A: structure and function of an integral membrane phospholipase. Biochim. Biophys. Acta, 1488, 91-101.
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 91-101
    • Snijder, H.J.1    Dijkstra, B.W.2
  • 67
    • 0035367725 scopus 로고    scopus 로고
    • Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli
    • Snijder, H. J., Kingma, R. L., Kalk, K. H., Dekker, N., Egmond, M. R. and Dijkstra, B. W., 2001, Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli. J. Mol. Biol., 309, 477-489.
    • (2001) J. Mol. Biol. , vol.309 , pp. 477-489
    • Snijder, H.J.1    Kingma, R.L.2    Kalk, K.H.3    Dekker, N.4    Egmond, M.R.5    Dijkstra, B.W.6
  • 68
    • 0028939947 scopus 로고
    • L3 loop-mediated mechanisms of pore closing in porin: A molecular dynamics perturbation approach
    • Soares, C. M., Björkstén, J. and Tapia, O., 1995, L3 loop-mediated mechanisms of pore closing in porin: a molecular dynamics perturbation approach. Prot. Eng., 8, 5-12.
    • (1995) Prot. Eng. , vol.8 , pp. 5-12
    • Soares, C.M.1    Björkstén, J.2    Tapia, O.3
  • 70
    • 0242657339 scopus 로고    scopus 로고
    • Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR
    • Tamm, L. K., Abildgaard, F., Arora, A., Blad, H. and Bushweller, J. H., 2003, Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR. FEBS Lett., 555, 139-143.
    • (2003) FEBS Lett. , vol.555 , pp. 139-143
    • Tamm, L.K.1    Abildgaard, F.2    Arora, A.3    Blad, H.4    Bushweller, J.H.5
  • 71
    • 0031860932 scopus 로고    scopus 로고
    • A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer
    • Tieleman, D. P. and Berendsen, H. J. C., 1998, A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer. Biophys. J., 74, 2786-2801.
    • (1998) Biophys. J. , vol.74 , pp. 2786-2801
    • Tieleman, D.P.1    Berendsen, H.J.C.2
  • 72
    • 0031438285 scopus 로고    scopus 로고
    • A computer perspective of membranes: Molecular dynamics studies of lipid bilayer systems
    • Tieleman, D. P., Marrink, S. J. and Berendsen, H. J. C., 1997, A computer perspective of membranes: molecular dynamics studies of lipid bilayer systems. Biochim. Biophys. Acta, 1331, 235-270.
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 235-270
    • Tieleman, D.P.1    Marrink, S.J.2    Berendsen, H.J.C.3
  • 73
    • 0032534843 scopus 로고    scopus 로고
    • Lipid properties and the orientation of aromatic residues in OmpF, influenza M2 and alamethicin systems: Molecular dynamics simulations
    • Tieleman, D. P., Forrest, L. R., Berendsen, H. J. C. and Sansom, M. S. P., 1999, Lipid properties and the orientation of aromatic residues in OmpF, influenza M2 and alamethicin systems: molecular dynamics simulations. Biochem., 37, 17554-17561.
    • (1999) Biochem. , vol.37 , pp. 17554-17561
    • Tieleman, D.P.1    Forrest, L.R.2    Berendsen, H.J.C.3    Sansom, M.S.P.4
  • 74
    • 0002883739 scopus 로고    scopus 로고
    • Atomic-scale molecular dynamics simulations of lipid membranes
    • Tobias, D. J., Tu, K. C. and Klein, M. L., 1997, Atomic-scale molecular dynamics simulations of lipid membranes. Curr. Opin. Coll. Interface Sci., 2, 15-26.
    • (1997) Curr. Opin. Coll. Interface Sci. , vol.2 , pp. 15-26
    • Tobias, D.J.1    Tu, K.C.2    Klein, M.L.3
  • 75
    • 0035903650 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site
    • Vandeputte-Rutten, L., Kramer, R. A., Kroon, J., Dekker, N., Egmond, M. R. and Gros, P., 2001a, Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site. EMBO J., 20, 5033-5039.
    • (2001) EMBO J. , vol.20 , pp. 5033-5039
    • Vandeputte-Rutten, L.1    Kramer, R.A.2    Kroon, J.3    Dekker, N.4    Egmond, M.R.5    Gros, P.6
  • 76
    • 0035903650 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site
    • Vandeputte-Rutten, L., Kramer, R. A., Kroon, J., Dekker, N., Egmond, M. R. and Gros, P., 2001b, Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site. EMBO J., 20, 5033-5039.
    • (2001) EMBO J. , vol.20 , pp. 5033-5039
    • Vandeputte-Rutten, L.1    Kramer, R.A.2    Kroon, J.3    Dekker, N.4    Egmond, M.R.5    Gros, P.6
  • 77
    • 0030895157 scopus 로고    scopus 로고
    • Computer simulations of the OmpF porin from the outer membrane of Escherichia coli
    • Watanabe, M., Rosenbusch, J., Schirmer, T. and Karplus, M., 1997, Computer simulations of the OmpF porin from the outer membrane of Escherichia coli. Biophys. J., 72, 2094-2102.
    • (1997) Biophys. J. , vol.72 , pp. 2094-2102
    • Watanabe, M.1    Rosenbusch, J.2    Schirmer, T.3    Karplus, M.4
  • 78
    • 0026331041 scopus 로고
    • Molecular architecture and electrostatic properties of a bacterial porin
    • Weiss, M. S., Abele, U., Weckesser, J., Welte, W., Schiltz, E. and Schulz, G. E., 1991, Molecular architecture and electrostatic properties of a bacterial porin. Science, 254, 1627-1630.
    • (1991) Science , vol.254 , pp. 1627-1630
    • Weiss, M.S.1    Abele, U.2    Weckesser, J.3    Welte, W.4    Schiltz, E.5    Schulz, G.E.6
  • 79
    • 0041428149 scopus 로고    scopus 로고
    • The versatile β-barrel membrane protein
    • Wimley, W. C., 2003, The versatile β-barrel membrane protein. Curr. Opin. Struct. Biol. 13, 404-411.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 404-411
    • Wimley, W.C.1
  • 80
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau, W. M., Wimley, W. C., Gawrisch, K. and White, S. H., 1998, The preference of tryptophan for membrane interfaces, Biochem., 37, 14713-14718,
    • (1998) Biochem. , vol.37 , pp. 14713-14718
    • Yau, W.M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 81
    • 0036105803 scopus 로고    scopus 로고
    • Electrostatic properties of the anion selective porin Omp32 from Delftia acidovorans and of the arginine cluster of bacterial porins
    • Zachariae, U., Koumanov, A., Engelhardt, H. and Karshikoff, A., 2002, Electrostatic properties of the anion selective porin Omp32 from Delftia acidovorans and of the arginine cluster of bacterial porins. Prot. Sci., 11, 1309-1319.
    • (2002) Prot. Sci. , vol.11 , pp. 1309-1319
    • Zachariae, U.1    Koumanov, A.2    Engelhardt, H.3    Karshikoff, A.4
  • 82
    • 0041343084 scopus 로고    scopus 로고
    • Multistep mechanism of chloride translocation in a strongly anion-selective porin channel
    • Zachariae, U., Helms, V. and Engelhardt, H., 2003, Multistep mechanism of chloride translocation in a strongly anion-selective porin channel. Biophys. J., 85, 954-962.
    • (2003) Biophys. J. , vol.85 , pp. 954-962
    • Zachariae, U.1    Helms, V.2    Engelhardt, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.