메뉴 건너뛰기




Volumn 141, Issue 1-2, 2006, Pages 2-29

Modelling of proteins in membranes

Author keywords

Coarse grain model; Cooperative behavior; Dissipative particle dynamics; Hydrophobic mismatch; Ion channel; Lipid protein interaction; Mesoscopic model; Molecular dynamics; Monte Carlo; Phase transition; Poisson Boltzmann; Protein insertion; Tilting

Indexed keywords

ADSORPTION; CELL MEMBRANE; CHEMICAL STRUCTURE; ELASTICITY; ELECTRON MICROSCOPY; ELECTRON SPIN RESONANCE; HYDROPHOBICITY; LIPID ANALYSIS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN INTERACTION; REVIEW; THEORETICAL MODEL; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY; BINDING SITE; CHEMICAL MODEL; CHEMISTRY; COMPUTER SIMULATION; LIPID BILAYER; MEMBRANE FLUIDITY; METABOLISM; MONTE CARLO METHOD; POISSON DISTRIBUTION; PROTEIN CONFORMATION;

EID: 33746722844     PISSN: 00093084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2006.02.024     Document Type: Review
Times cited : (59)

References (198)
  • 1
    • 0343636630 scopus 로고
    • Theories of protein-lipid and protein-protein interactions in membranes
    • Watts A., and De Pont J. (Eds), Elsevier Science Publishers, New York
    • Abney J.R., and Owicki J.C. Theories of protein-lipid and protein-protein interactions in membranes. In: Watts A., and De Pont J. (Eds). Progress in Protein-Lipid Interactions (1985), Elsevier Science Publishers, New York
    • (1985) Progress in Protein-Lipid Interactions
    • Abney, J.R.1    Owicki, J.C.2
  • 2
    • 2242431668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel
    • Bass R.B., Strop P., Barclay M., and Rees D.C. Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel. Science 298 (2002) 1582-1587
    • (2002) Science , vol.298 , pp. 1582-1587
    • Bass, R.B.1    Strop, P.2    Barclay, M.3    Rees, D.C.4
  • 3
    • 0029762032 scopus 로고    scopus 로고
    • Insertion and hairpin formation of membrane proteins
    • Baumgaertner A. Insertion and hairpin formation of membrane proteins. Biophys. J. 71 (1996) 1248-1255
    • (1996) Biophys. J. , vol.71 , pp. 1248-1255
    • Baumgaertner, A.1
  • 5
    • 0030920604 scopus 로고    scopus 로고
    • Structure and dynamics of the M13 coat signal sequence in membranes by multidimensional high-resolution and solid-state NMR spectroscopy
    • Bechinger B. Structure and dynamics of the M13 coat signal sequence in membranes by multidimensional high-resolution and solid-state NMR spectroscopy. Proteins: Struct. Funct. Genet. 27 (1997) 481-492
    • (1997) Proteins: Struct. Funct. Genet. , vol.27 , pp. 481-492
    • Bechinger, B.1
  • 6
    • 0030733344 scopus 로고    scopus 로고
    • Structure and dynamics of an amphiphilic peptide in a bilayer: a molecular dynamics study
    • Belohorcová K., Davis J.H., Woolf T.B., and Roux B. Structure and dynamics of an amphiphilic peptide in a bilayer: a molecular dynamics study. Biophys. J. 73 (1997) 3039-3055
    • (1997) Biophys. J. , vol.73 , pp. 3039-3055
    • Belohorcová, K.1    Davis, J.H.2    Woolf, T.B.3    Roux, B.4
  • 7
    • 0001165244 scopus 로고
    • Molecular theory of chain packing, elasticity and lipid protein interaction in lipid bilayers
    • Lipowsky R., and Sackmann E. (Eds), Elsevier, Amsterdam
    • Ben-Shaul A. Molecular theory of chain packing, elasticity and lipid protein interaction in lipid bilayers. In: Lipowsky R., and Sackmann E. (Eds). Structure and Dynamics of Membranes (1995), Elsevier, Amsterdam
    • (1995) Structure and Dynamics of Membranes
    • Ben-Shaul, A.1
  • 8
    • 0011613265 scopus 로고    scopus 로고
    • Molecular dynamics simulation of melittin in a POPC bilayer membrane
    • Bernéche S., Nina N., and Roux B. Molecular dynamics simulation of melittin in a POPC bilayer membrane. Biophys. J. 75 (1998) 1603-1618
    • (1998) Biophys. J. , vol.75 , pp. 1603-1618
    • Bernéche, S.1    Nina, N.2    Roux, B.3
  • 9
    • 0037418587 scopus 로고    scopus 로고
    • Mechanosensitive channels: stress relief
    • Biggin P.C., and Sansom M.S.P. Mechanosensitive channels: stress relief. Curr. Biol. 13 (2003) 183-185
    • (2003) Curr. Biol. , vol.13 , pp. 183-185
    • Biggin, P.C.1    Sansom, M.S.P.2
  • 11
    • 0142211230 scopus 로고    scopus 로고
    • Interaction between two cylindrical inclusions in a symmetric lipid-bilayer
    • Bohinc K., Kralj-Iglič V., and May S. Interaction between two cylindrical inclusions in a symmetric lipid-bilayer. J. Chem. Phys. 119 (2003) 7435-7444
    • (2003) J. Chem. Phys. , vol.119 , pp. 7435-7444
    • Bohinc, K.1    Kralj-Iglič, V.2    May, S.3
  • 12
    • 27244453417 scopus 로고    scopus 로고
    • Flexible lipid bilayers in implicit solvent
    • Brannigan C., Philips P.F., and Brown F.L.H. Flexible lipid bilayers in implicit solvent. Phys. Rev. E 72 (2005) 011915
    • (2005) Phys. Rev. E , vol.72 , pp. 011915
    • Brannigan, C.1    Philips, P.F.2    Brown, F.L.H.3
  • 13
    • 4143150532 scopus 로고    scopus 로고
    • Molecular dynamics simulations of micelle formation around dimeric glycophorin A transmembrane helices
    • Braun R., Engelman D.M., and Schulten K. Molecular dynamics simulations of micelle formation around dimeric glycophorin A transmembrane helices. Biophys. J. 87 (2004) 754-763
    • (2004) Biophys. J. , vol.87 , pp. 754-763
    • Braun, R.1    Engelman, D.M.2    Schulten, K.3
  • 14
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher M.S., and Munro S. Cholesterol and the Golgi apparatus. Science 261 (1993) 1280-1281
    • (1993) Science , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 15
    • 0035114879 scopus 로고    scopus 로고
    • The role of retinal in the long-range protein-lipid interactions in bacteriorhodopsin-phosphatidylcholine vesicles
    • Bryl K., and Yoshihara K. The role of retinal in the long-range protein-lipid interactions in bacteriorhodopsin-phosphatidylcholine vesicles. Eur. Biophys. J. 29 (2001) 628-640
    • (2001) Eur. Biophys. J. , vol.29 , pp. 628-640
    • Bryl, K.1    Yoshihara, K.2
  • 16
    • 34548090976 scopus 로고    scopus 로고
    • Multiscale coupling of mesoscopic- and atomistic-level lipid bilayer simulations
    • Chang R., Ayton G.S., and Voth G.A. Multiscale coupling of mesoscopic- and atomistic-level lipid bilayer simulations. J. Chem. Phys. 122 (2005) 244716
    • (2005) J. Chem. Phys. , vol.122 , pp. 244716
    • Chang, R.1    Ayton, G.S.2    Voth, G.A.3
  • 17
    • 0033061633 scopus 로고    scopus 로고
    • Simulation study of a gramicidin/lipid bilayer system in excess water and lipid. I. Structure of the molecular complex
    • Chiu S.-W., Subramaniam S., and Jakobsson E. Simulation study of a gramicidin/lipid bilayer system in excess water and lipid. I. Structure of the molecular complex. Biophys. J. 76 (1999) 1929-1938
    • (1999) Biophys. J. , vol.76 , pp. 1929-1938
    • Chiu, S.-W.1    Subramaniam, S.2    Jakobsson, E.3
  • 18
    • 27244452976 scopus 로고    scopus 로고
    • Tunable generic model for fluid bilayer membranes
    • Cooke I.-R., Kremer K., and Deserno M. Tunable generic model for fluid bilayer membranes. Phys. Rev. E 72 (2005) 1-4
    • (2005) Phys. Rev. E , vol.72 , pp. 1-4
    • Cooke, I.-R.1    Kremer, K.2    Deserno, M.3
  • 19
    • 33645705346 scopus 로고
    • Membrane-induced interactions between inclusions
    • Dan N., Pincus P., and Safran S.A. Membrane-induced interactions between inclusions. Langmuir 9 (1993) 2768-2771
    • (1993) Langmuir , vol.9 , pp. 2768-2771
    • Dan, N.1    Pincus, P.2    Safran, S.A.3
  • 20
    • 0242659352 scopus 로고    scopus 로고
    • Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring
    • de Planque M.R.R., and Killian J.A. Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring. Mol. Membrane Biol. 20 (2003) 271-284
    • (2003) Mol. Membrane Biol. , vol.20 , pp. 271-284
    • de Planque, M.R.R.1    Killian, J.A.2
  • 21
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution
    • Deisenhofer J., Epp O., Miki K., Huber R., and Michael H. Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution. Nature 318 (1985) 618-624
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michael, H.5
  • 22
    • 0030823233 scopus 로고    scopus 로고
    • Molecular sorting of lipids by bacteriorhodopsin in dilauroylphosphatidylcholine/distearoyl-phosphatidylcholine lipid bilayers
    • Dumas F., Sperotto M.M., Lebrum M.C., Tocanne J.-F., and Mouritsen O.G. Molecular sorting of lipids by bacteriorhodopsin in dilauroylphosphatidylcholine/distearoyl-phosphatidylcholine lipid bilayers. Biophys. J. 73 (1997) 1940-1953
    • (1997) Biophys. J. , vol.73 , pp. 1940-1953
    • Dumas, F.1    Sperotto, M.M.2    Lebrum, M.C.3    Tocanne, J.-F.4    Mouritsen, O.G.5
  • 23
    • 0032877355 scopus 로고    scopus 로고
    • Is the protein/lipid hydrophobic matching principle relevant to membrane organization and functions?
    • Dumas F., Lebrum M.C., and Tocanne J.-F. Is the protein/lipid hydrophobic matching principle relevant to membrane organization and functions?. FEBS Lett. 458 (1999) 271-277
    • (1999) FEBS Lett. , vol.458 , pp. 271-277
    • Dumas, F.1    Lebrum, M.C.2    Tocanne, J.-F.3
  • 24
    • 0024288356 scopus 로고
    • The structure of membrane-spanning polypeptide studied by molecular dynamics
    • Edholm O., and Jähnig F. The structure of 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
  • 26
    • 0032991265 scopus 로고    scopus 로고
    • A solvent model for simulations of peptides in bilayers. I. Membrane-promoting alpha-helix formation
    • Efremov R.G., Nolde D.E., Vergoten G., and Arseniev A.S. A solvent model for simulations of peptides in bilayers. I. Membrane-promoting alpha-helix formation. Biophys. J. 76 (1999) 2448-2459
    • (1999) Biophys. J. , vol.76 , pp. 2448-2459
    • Efremov, R.G.1    Nolde, D.E.2    Vergoten, G.3    Arseniev, A.S.4
  • 27
    • 0032991267 scopus 로고    scopus 로고
    • A solvent model for simulations of peptides in bilayers. II. Membrane-spanning alpha-helices
    • Efremov R.G., Nolde D.E., Vergoten G., and Arseniev A.S. A solvent model for simulations of peptides in bilayers. II. Membrane-spanning alpha-helices. Biophys. J. 76 (1999) 2460-2471
    • (1999) Biophys. J. , vol.76 , pp. 2460-2471
    • Efremov, R.G.1    Nolde, D.E.2    Vergoten, G.3    Arseniev, A.S.4
  • 29
    • 0034859342 scopus 로고    scopus 로고
    • Molecular dynamics simulations of wild-type and mutant forms of the Mycobacterium tuberculosis MscL channel
    • Elmore D.E., and Dougherty D.A. Molecular dynamics simulations of wild-type and mutant forms of the Mycobacterium tuberculosis MscL channel. Biophys. J. 81 (2001) 1345-1359
    • (2001) Biophys. J. , vol.81 , pp. 1345-1359
    • Elmore, D.E.1    Dougherty, D.A.2
  • 30
    • 0019464222 scopus 로고
    • The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis
    • Engelman D.M., and Steitz T.A. The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis. Cell 23 (1981) 411-422
    • (1981) Cell , vol.23 , pp. 411-422
    • Engelman, D.M.1    Steitz, T.A.2
  • 31
    • 0029146071 scopus 로고
    • Mechanisms for the modulation of membrane bilayer properties by amphipathic helical peptides
    • Epand R.M., Shai Y., Segrest J.P., and Anantharamaiah G.M. Mechanisms for the modulation of membrane bilayer properties by amphipathic helical peptides. Biopolymers (Peptide Sci.) 37 (1995) 319-338
    • (1995) Biopolymers (Peptide Sci.) , vol.37 , pp. 319-338
    • Epand, R.M.1    Shai, Y.2    Segrest, J.P.3    Anantharamaiah, G.M.4
  • 32
    • 0031795752 scopus 로고    scopus 로고
    • Lipid polymorphism and lipid-protein interactions
    • Epand R.M. Lipid polymorphism and lipid-protein interactions. Biochim. Biophys. Acta 1376 (1998) 353-368
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 353-368
    • Epand, R.M.1
  • 33
    • 7044241296 scopus 로고    scopus 로고
    • Do proteins facilitate the formation of cholesterol-rich domains?
    • Epand R.M. Do proteins facilitate the formation of cholesterol-rich domains?. Biochim. Biophys. Acta: Biomembranes 1666 (2004) 227-238
    • (2004) Biochim. Biophys. Acta: Biomembranes , vol.1666 , pp. 227-238
    • Epand, R.M.1
  • 34
    • 0036283098 scopus 로고    scopus 로고
    • Modulation of concentration fluctuations in phase-separated lipid membranes by polypeptide insertion
    • Fahsel S., Pospiech E.-M., Zein M., Hazlet T.L., Gratton E., and Winter R. Modulation of concentration fluctuations in phase-separated lipid membranes by polypeptide insertion. Biophys. J. 83 (2002) 334-344
    • (2002) Biophys. J. , vol.83 , pp. 334-344
    • Fahsel, S.1    Pospiech, E.-M.2    Zein, M.3    Hazlet, T.L.4    Gratton, E.5    Winter, R.6
  • 35
    • 33847738814 scopus 로고    scopus 로고
    • Lipid rafts: structure, function and role in HIV, Alzheimer's and prion diseases
    • Cambridge University Press, UK pp. 1-22
    • Fantini J., Garmy N., Mahfoud R., and Yahi N. Lipid rafts: structure, function and role in HIV, Alzheimer's and prion diseases. Expert Reviews in Molecular Medicine (2002), Cambridge University Press, UK pp. 1-22
    • (2002) Expert Reviews in Molecular Medicine
    • Fantini, J.1    Garmy, N.2    Mahfoud, R.3    Yahi, N.4
  • 36
    • 0027362726 scopus 로고
    • A molecular model for lipid-protein interactions in membranes: the role of hydrophobic mismatch
    • Fattal D.R., and Ben-Shaul A. A molecular model for lipid-protein interactions in membranes: the role of hydrophobic mismatch. Biophys. J. 65 (1993) 1795-1809
    • (1993) Biophys. J. , vol.65 , pp. 1795-1809
    • Fattal, D.R.1    Ben-Shaul, A.2
  • 37
    • 0029767694 scopus 로고    scopus 로고
    • On simulating lipid bilayers with an applied surface tension: periodic boundary conditions and undulations
    • Feller S.E., and Pastor R.W. On simulating lipid bilayers with an applied surface tension: periodic boundary conditions and undulations. Biophys. J. 71 (1996) 1350-1355
    • (1996) Biophys. J. , vol.71 , pp. 1350-1355
    • Feller, S.E.1    Pastor, R.W.2
  • 38
    • 0032614136 scopus 로고    scopus 로고
    • Constant surface tension simulations of lipid bilayers: the sensitivity of surface areas and compressibilities
    • Feller S.E., and Pastor R.W. Constant surface tension simulations of lipid bilayers: the sensitivity of surface areas and compressibilities. J. Chem. Phys. 111 (1999) 1281-1287
    • (1999) J. Chem. Phys. , vol.111 , pp. 1281-1287
    • Feller, S.E.1    Pastor, R.W.2
  • 39
    • 0141785142 scopus 로고    scopus 로고
    • Dependence of M13 major coat protein oligomerization and lateral segregation on bilayer composition
    • Fernandes F., Loura L.M.S., Prieto M., Koehorst R., Spruijt R.B., and Hemminga M.A. Dependence of M13 major coat protein oligomerization and lateral segregation on bilayer composition. Biophys. J. 85 (2003) 2430-2441
    • (2003) Biophys. J. , vol.85 , pp. 2430-2441
    • Fernandes, F.1    Loura, L.M.S.2    Prieto, M.3    Koehorst, R.4    Spruijt, R.B.5    Hemminga, M.A.6
  • 41
    • 0020681373 scopus 로고
    • Structure of the lac carrier protein of Escherichia coli
    • Foster D.L., Boublik M., and Kaback H.R. Structure of the lac carrier protein of Escherichia coli. J. Biol. Chem. 258 (1983) 31-34
    • (1983) J. Biol. Chem. , vol.258 , pp. 31-34
    • Foster, D.L.1    Boublik, M.2    Kaback, H.R.3
  • 42
    • 0019887784 scopus 로고
    • Cardiolipin requirement for electron transfer in complexes I and III of the mitochondrial respiratory chain
    • Fry M., and Green D.E. Cardiolipin requirement for electron transfer in complexes I and III of the mitochondrial respiratory chain. J. Biol. Chem. 256 (1981) 1874-1880
    • (1981) J. Biol. Chem. , vol.256 , pp. 1874-1880
    • Fry, M.1    Green, D.E.2
  • 46
    • 0033960609 scopus 로고    scopus 로고
    • Miscibility of phosphatidylethanolamine-phosphatidylglycerol mixtures as a function of pH and acyl chain length
    • Garidel P., and Blume A. Miscibility of phosphatidylethanolamine-phosphatidylglycerol mixtures as a function of pH and acyl chain length. Eur. Biophys. J. 28 (2000) 629-638
    • (2000) Eur. Biophys. J. , vol.28 , pp. 629-638
    • Garidel, P.1    Blume, A.2
  • 47
    • 0001704050 scopus 로고    scopus 로고
    • Compositional-mechanical instability of interacting mixed lipid membranes
    • Gelbart W.M., and Bruinsma R. Compositional-mechanical instability of interacting mixed lipid membranes. Phys. Rev. E 55 (1997) 831-835
    • (1997) Phys. Rev. E , vol.55 , pp. 831-835
    • Gelbart, W.M.1    Bruinsma, R.2
  • 50
    • 0000206982 scopus 로고    scopus 로고
    • Computer simulations of bilayer membranes: self-assembly and interfacial tension
    • Goetz R., and Lipowsky R. Computer simulations of bilayer membranes: self-assembly and interfacial tension. J. Chem. Phys. 108 (1998) 7397-7409
    • (1998) J. Chem. Phys. , vol.108 , pp. 7397-7409
    • Goetz, R.1    Lipowsky, R.2
  • 51
    • 0000283071 scopus 로고    scopus 로고
    • Mobility and elasticity of self-assembled membranes
    • Goetz R., Gompper G., and Lipowsky R. Mobility and elasticity of self-assembled membranes. Phys. Rev. Lett. 82 (1998) 221-224
    • (1998) Phys. Rev. Lett. , vol.82 , pp. 221-224
    • Goetz, R.1    Gompper, G.2    Lipowsky, R.3
  • 52
    • 33747423529 scopus 로고    scopus 로고
    • Golebiewska, U., Gambhir, A., Hangyás-Mihályné, G., Zaitseva, I., Radler, J., McLaughlin, S., 2005. Membrane-bound basic peptides sequester the multivalent lipid PIP2 but not the monovalent lipid PS, preprint.
  • 53
    • 0031249493 scopus 로고    scopus 로고
    • Network models of fluid, hexatic and polymerized membranes
    • Gompper G., and Kroll D.M. Network models of fluid, hexatic and polymerized membranes. J. Phys. Condens. Matter 9 (1997) 8795-8834
    • (1997) J. Phys. Condens. Matter , vol.9 , pp. 8795-8834
    • Gompper, G.1    Kroll, D.M.2
  • 54
    • 11244346029 scopus 로고    scopus 로고
    • Molecular dynamics simulation of trans-membrane polypeptide orientational fluctuations
    • Goodyear D.J., Sharpe S., and Grant W.M. Molecular dynamics simulation of trans-membrane polypeptide orientational fluctuations. Biophys. J. 88 (2005) 105-117
    • (2005) Biophys. J. , vol.88 , pp. 105-117
    • Goodyear, D.J.1    Sharpe, S.2    Grant, W.M.3
  • 55
    • 0034271702 scopus 로고    scopus 로고
    • Mesoscopic simulation of polymer-surfactant aggregation
    • Groot R.D. Mesoscopic simulation of polymer-surfactant aggregation. Langmuir 16 (2000) 7493-7502
    • (2000) Langmuir , vol.16 , pp. 7493-7502
    • Groot, R.D.1
  • 56
    • 0034909360 scopus 로고    scopus 로고
    • Mesoscopic simulation of cell membrane damage, morphology change and rupture by nonionic surfactant
    • Groot R.D., and Rabone K.L. Mesoscopic simulation of cell membrane damage, morphology change and rupture by nonionic surfactant. Biophys. J. 81 (2001) 725-736
    • (2001) Biophys. J. , vol.81 , pp. 725-736
    • Groot, R.D.1    Rabone, K.L.2
  • 57
    • 0036055199 scopus 로고    scopus 로고
    • Colloquium: the physics of charge inversion in chemical and biological systems
    • Grosberg A.Y., Nguyen T.T., and Shklovskii B.I. Colloquium: the physics of charge inversion in chemical and biological systems. Mod. Rev. Phys. 74 (2002) 329-345
    • (2002) Mod. Rev. Phys. , vol.74 , pp. 329-345
    • Grosberg, A.Y.1    Nguyen, T.T.2    Shklovskii, B.I.3
  • 58
    • 0035039272 scopus 로고    scopus 로고
    • Structural determination of MscL gating studied by MD simulations
    • Gullingsrud J., Kosztin D., and Schulten K. Structural determination of MscL gating studied by MD simulations. Biophys. J. 80 (2001) 2074-2081
    • (2001) Biophys. J. , vol.80 , pp. 2074-2081
    • Gullingsrud, J.1    Kosztin, D.2    Schulten, K.3
  • 59
    • 0141754098 scopus 로고    scopus 로고
    • Gating of MscL studied by steered molecular dynamics
    • Gullingsrud J., and Schulten K. Gating of MscL studied by steered molecular dynamics. Biophys. J. 85 (2003) 2087-2099
    • (2003) Biophys. J. , vol.85 , pp. 2087-2099
    • Gullingsrud, J.1    Schulten, K.2
  • 60
    • 0032988823 scopus 로고    scopus 로고
    • Experimental evidence for hydrophobic matching and membrane-mediated interactions in lipid bilayers containing gramicidin
    • Harroun T.A., Heller W.T., Wiess T.M., Yang L., and Huang H.W. Experimental evidence for hydrophobic matching and membrane-mediated interactions in lipid bilayers containing gramicidin. Biophys. J. 76 (1999) 937-945
    • (1999) Biophys. J. , vol.76 , pp. 937-945
    • Harroun, T.A.1    Heller, W.T.2    Wiess, T.M.3    Yang, L.4    Huang, H.W.5
  • 61
    • 0033783447 scopus 로고    scopus 로고
    • 31P solid-state NMR spectroscopy investigation
    • 31P solid-state NMR spectroscopy investigation. Biochemistry 39 (2000) 13106-13114
    • (2000) Biochemistry , vol.39 , pp. 13106-13114
    • Harzer, U.1    Bechinger, B.2
  • 62
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R., and Unwin P.N.T. Three-dimensional model of purple membrane obtained by electron microscopy. Nature 257 (1975) 28-32
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.T.2
  • 63
    • 0031807139 scopus 로고    scopus 로고
    • Structure, stability and thermodynamics of lamellar DNA-lipid complexes
    • Harries D., May S., Gelbart W.M., and Ben-Shaul A. Structure, stability and thermodynamics of lamellar DNA-lipid complexes. Biophys. J. 75 (1998) 159-173
    • (1998) Biophys. J. , vol.75 , pp. 159-173
    • Harries, D.1    May, S.2    Gelbart, W.M.3    Ben-Shaul, A.4
  • 64
    • 0033038093 scopus 로고    scopus 로고
    • Theoretical analysis of hydrophobic matching and membrane-mediated interactions in lipid bilayers containing gramicidin
    • Harroun T.A., Heller W.T., Weiss T.M., Yang L., and Huang H.W. Theoretical analysis of hydrophobic matching and membrane-mediated interactions in lipid bilayers containing gramicidin. Biophys. J. 76 (1999) 3176-3185
    • (1999) Biophys. J. , vol.76 , pp. 3176-3185
    • Harroun, T.A.1    Heller, W.T.2    Weiss, T.M.3    Yang, L.4    Huang, H.W.5
  • 65
    • 84943997802 scopus 로고
    • Elastic properties of lipid bilayers: theory and possible experiments
    • Helfrich W. Elastic properties of lipid bilayers: theory and possible experiments. Z. Naturforsch. 28 (1973) 693-703
    • (1973) Z. Naturforsch. , vol.28 , pp. 693-703
    • Helfrich, W.1
  • 67
    • 2642533608 scopus 로고    scopus 로고
    • Lipid modulation of protein-induced membrane domains as a mechanism for controlling signal transduction
    • Hinderliter A., Biltonen R.L., and Almeida P.F. Lipid modulation of protein-induced membrane domains as a mechanism for controlling signal transduction. Biochemistry 43 (2004) 7102-7110
    • (2004) Biochemistry , vol.43 , pp. 7102-7110
    • Hinderliter, A.1    Biltonen, R.L.2    Almeida, P.F.3
  • 68
    • 0035799334 scopus 로고    scopus 로고
    • Domain formation in a fluid mixed lipid bilayer modulated through binding of the C2 protein motif
    • Hinderliter A., Almeida P.F., Creutz C.E., and Biltonen R.L. Domain formation in a fluid mixed lipid bilayer modulated through binding of the C2 protein motif. Biochemistry 40 (2001) 4181-4191
    • (2001) Biochemistry , vol.40 , pp. 4181-4191
    • Hinderliter, A.1    Almeida, P.F.2    Creutz, C.E.3    Biltonen, R.L.4
  • 69
    • 84950109965 scopus 로고
    • Simulating microscopic hydrodynamics phenomena with dissipative particle dynamics
    • Hoogerbrugge P.J., and Koelman J.M.V.A. Simulating microscopic hydrodynamics phenomena with dissipative particle dynamics. Europhys. Lett. 19 (1992) 155-160
    • (1992) Europhys. Lett. , vol.19 , pp. 155-160
    • Hoogerbrugge, P.J.1    Koelman, J.M.V.A.2
  • 70
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: two-state model
    • Huang H.W. Action of antimicrobial peptides: two-state model. Biochemistry 39 (2000) 8347-8352
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 71
    • 2942754299 scopus 로고    scopus 로고
    • Molecular mechanism of peptide-induced pores in membranes
    • Huang H.W., Chen F.Y., and Lee M.T. Molecular mechanism of peptide-induced pores in membranes. Phys. Rev. Lett. 92 (2004) 198304
    • (2004) Phys. Rev. Lett. , vol.92 , pp. 198304
    • Huang, H.W.1    Chen, F.Y.2    Lee, M.T.3
  • 72
    • 18744403982 scopus 로고    scopus 로고
    • Chemical theory and computation special feature: interfacial folding and membrane insertion of designed peptides studied by molecular dynamics simulations
    • Im W., and Brooks C.L. Chemical theory and computation special feature: interfacial folding and membrane insertion of designed peptides studied by molecular dynamics simulations. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 6771-6776
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 6771-6776
    • Im, W.1    Brooks, C.L.2
  • 73
    • 0025876658 scopus 로고
    • Hydrophobic membrane thickness and lipid-protein interactions of the leucine transport system of Lactococcus lactis
    • In't Veld G., Driessen A.J.M., Op den Kamp J.A.F., and Konings W.N. Hydrophobic membrane thickness and lipid-protein interactions of the leucine transport system of Lactococcus lactis. Biochim. Biophys. Acta 1065 (1991) 203-212
    • (1991) Biochim. Biophys. Acta , vol.1065 , pp. 203-212
    • In't Veld, G.1    Driessen, A.J.M.2    Op den Kamp, J.A.F.3    Konings, W.N.4
  • 74
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., and Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376 (1995) 660-669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 75
    • 0029737564 scopus 로고    scopus 로고
    • What is the surface tension of a lipid membrane?
    • Jähnig F. What is the surface tension of a lipid membrane?. Biophys. J. 71 (1996) 1348-1349
    • (1996) Biophys. J. , vol.71 , pp. 1348-1349
    • Jähnig, F.1
  • 76
    • 7244244196 scopus 로고    scopus 로고
    • Lipids do influence protein function-the hydrophobic matching hypothesis revised
    • Jensen M.Ø., and Mouritsen O.G. Lipids do influence protein function-the hydrophobic matching hypothesis revised. Biochim. Biophys. Acta Biomembranes 1666 (2004) 205-226
    • (2004) Biochim. Biophys. Acta Biomembranes , vol.1666 , pp. 205-226
    • Jensen, M.O.1    Mouritsen, O.G.2
  • 77
    • 0035183282 scopus 로고    scopus 로고
    • The mechanism of glycerol conduction in aquaglyceroporins
    • Jensen M.Ø., Tajkhorshid E., and Schulten K. The mechanism of glycerol conduction in aquaglyceroporins. Structure 9 (2001) 1083-1093
    • (2001) Structure , vol.9 , pp. 1083-1093
    • Jensen, M.O.1    Tajkhorshid, E.2    Schulten, K.3
  • 79
    • 0018814507 scopus 로고
    • The lipid-protein interface in biological membranes
    • Jost P.C., and Hayes Griffith O. The lipid-protein interface in biological membranes. Ann. NY Acad. Sci. U.S.A. 348 (1980) 391-405
    • (1980) Ann. NY Acad. Sci. U.S.A. , vol.348 , pp. 391-405
    • Jost, P.C.1    Hayes Griffith, O.2
  • 82
    • 7644222023 scopus 로고    scopus 로고
    • Binding and insertion of α-helical anti-microbial peptides in POPC bilayers studied by molecular dynamics simulations
    • Kandasamy S.K., and Larson R.G. Binding and insertion of α-helical anti-microbial peptides in POPC bilayers studied by molecular dynamics simulations. Chem. Phys. Lipids 132 (2004) 113-132
    • (2004) Chem. Phys. Lipids , vol.132 , pp. 113-132
    • Kandasamy, S.K.1    Larson, R.G.2
  • 83
    • 0034902235 scopus 로고    scopus 로고
    • Interactions of cholesterol with lipid bilayers: the preferred configuration and fluctuations
    • Kessel A., Ben-Tal N., and May S. Interactions of cholesterol with lipid bilayers: the preferred configuration and fluctuations. Biophys. J. 81 (2001) 643-658
    • (2001) Biophys. J. , vol.81 , pp. 643-658
    • Kessel, A.1    Ben-Tal, N.2    May, S.3
  • 84
    • 18844434621 scopus 로고    scopus 로고
    • Molecular modeling of lipid bilayers and the effect of protein-like inclusions
    • Kik R.A., Leermakers F.A.M., and Kleijn J.M. Molecular modeling of lipid bilayers and the effect of protein-like inclusions. Phys. Chem. Chem. Phys. 7 (2005) 1996-2005
    • (2005) Phys. Chem. Chem. Phys. , vol.7 , pp. 1996-2005
    • Kik, R.A.1    Leermakers, F.A.M.2    Kleijn, J.M.3
  • 85
    • 0026473040 scopus 로고
    • Gramicidin and gramicidin-lipid interactions
    • Killian J.A. Gramicidin and gramicidin-lipid interactions. Biochim. Biophys. Acta 1113 (1992) 391-425
    • (1992) Biochim. Biophys. Acta , vol.1113 , pp. 391-425
    • Killian, J.A.1
  • 86
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian J.A. Hydrophobic mismatch between proteins and lipids in membranes. Biochim. Biophys. Acta 1376 (1998) 401-416
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 401-416
    • Killian, J.A.1
  • 87
    • 4444343863 scopus 로고    scopus 로고
    • Lipid bilayer topology of the transmembrane α-helix of M13 major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy
    • Koehorst R.B.M., Spruijt R.B., Vergeldt F.J., and Hemminga M.A. Lipid bilayer topology of the transmembrane α-helix of M13 major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy. Biophys. J. 87 (2004) 1445-1455
    • (2004) Biophys. J. , vol.87 , pp. 1445-1455
    • Koehorst, R.B.M.1    Spruijt, R.B.2    Vergeldt, F.J.3    Hemminga, M.A.4
  • 88
    • 0033545957 scopus 로고    scopus 로고
    • Site-specific deuterium order parameters and membrane-bound behavior of a peptide fragment from the intracellular domain of HIV-1 gp41
    • Koenig B.W., Ferretti J.A., and Gawrisch K. Site-specific deuterium order parameters and membrane-bound behavior of a peptide fragment from the intracellular domain of HIV-1 gp41. Biochemistry 38 (1999) 6327-6334
    • (1999) Biochemistry , vol.38 , pp. 6327-6334
    • Koenig, B.W.1    Ferretti, J.A.2    Gawrisch, K.3
  • 89
    • 0041589300 scopus 로고    scopus 로고
    • Translocation of phospholipids is facilitated by a subset of membrane-spanning proteins of the bacterial cytoplasmic membrane
    • Kol M.A., van Delen A., de Kroon A.I.P.M., and de Kruijff B. Translocation of phospholipids is facilitated by a subset of membrane-spanning proteins of the bacterial cytoplasmic membrane. J. Biol. Chem. 278 (2003) 24586-24593
    • (2003) J. Biol. Chem. , vol.278 , pp. 24586-24593
    • Kol, M.A.1    van Delen, A.2    de Kroon, A.I.P.M.3    de Kruijff, B.4
  • 90
  • 91
    • 85037181125 scopus 로고    scopus 로고
    • Molecular simulations of mesoscopic bilayer phases
    • Kranenburg M., Venturoli M., and Smit B. Molecular simulations of mesoscopic bilayer phases. Phys. Rev. E 67 (2003) 060901R
    • (2003) Phys. Rev. E , vol.67
    • Kranenburg, M.1    Venturoli, M.2    Smit, B.3
  • 92
    • 0242302386 scopus 로고    scopus 로고
    • Phase behaviour and induced interdigitation in bilayer studied with dissipative particle dynamics
    • Kranenburg M., Venturoli M., and Smit B. Phase behaviour and induced interdigitation in bilayer studied with dissipative particle dynamics. J. Phys. Chem. B 107 (2003) 11491-11501
    • (2003) J. Phys. Chem. B , vol.107 , pp. 11491-11501
    • Kranenburg, M.1    Venturoli, M.2    Smit, B.3
  • 93
    • 2942538349 scopus 로고    scopus 로고
    • Simulating the effects of alcohol on the structure of a membrane
    • Kranenburg M., and Smit B. Simulating the effects of alcohol on the structure of a membrane. FEBS Lett. 568 (2004) 15-18
    • (2004) FEBS Lett. , vol.568 , pp. 15-18
    • Kranenburg, M.1    Smit, B.2
  • 95
    • 4444254356 scopus 로고    scopus 로고
    • Simulating induced interdigitation in membranes
    • Kranenburg M., Vlaar M., and Smit B. Simulating induced interdigitation in membranes. Biophys. J. 87 (2004) 1596-1605
    • (2004) Biophys. J. , vol.87 , pp. 1596-1605
    • Kranenburg, M.1    Vlaar, M.2    Smit, B.3
  • 96
    • 0031740283 scopus 로고    scopus 로고
    • How lipids interact with an intrinsic membrane protein: the case of the calcium pump
    • Lee A.G. How lipids interact with an intrinsic membrane protein: the case of the calcium pump. Biochim. Biophys. Acta 1376 (1998) 381-390
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 381-390
    • Lee, A.G.1
  • 97
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: a structural perspective
    • Lee A.G. Lipid-protein interactions in biological membranes: a structural perspective. Biochim. Biophys. Acta 1612 (2003) 1-40
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 98
    • 0031049676 scopus 로고    scopus 로고
    • Evidence for phospholipid microdomain formation in liquid crystalline liposomes reconstituted with Escherichia coli lactose permease
    • Lehtonen J.Y.A., and Kinnunen P.K.J. Evidence for phospholipid microdomain formation in liquid crystalline liposomes reconstituted with Escherichia coli lactose permease. Biophys. J. 72 (1997) 1247-1257
    • (1997) Biophys. J. , vol.72 , pp. 1247-1257
    • Lehtonen, J.Y.A.1    Kinnunen, P.K.J.2
  • 99
    • 0034068919 scopus 로고    scopus 로고
    • Stability of a melittin pore in a lipid bilayer: a molecular dynamics study
    • Lin J.H., and Baumgaertner A. Stability of a melittin pore in a lipid bilayer: a molecular dynamics study. Biophys. J. 78 (2000) 1714-1724
    • (2000) Biophys. J. , vol.78 , pp. 1714-1724
    • Lin, J.H.1    Baumgaertner, A.2
  • 100
    • 0025316971 scopus 로고
    • Role of specific acidic lipids on the reconstitution of sodium-dependent amino acid transport in proteoliposomes derived from Ehrlich cell plasma membranes
    • Lin G.R., McCormick J.I., Dhe-Paganon S., Silvius J.R., and Johnstone R.M. Role of specific acidic lipids on the reconstitution of sodium-dependent amino acid transport in proteoliposomes derived from Ehrlich cell plasma membranes. Biochemistry 29 (1990) 4575-4581
    • (1990) Biochemistry , vol.29 , pp. 4575-4581
    • Lin, G.R.1    McCormick, J.I.2    Dhe-Paganon, S.3    Silvius, J.R.4    Johnstone, R.M.5
  • 101
    • 33747439868 scopus 로고    scopus 로고
    • Lin, J.H., Baumgaertner, A., 2005. Extraction of a melittin pore from a lipid bilayer: a molecular dynamics study. J. Am. Chem. Soc., submitted for publication.
  • 103
    • 17844379740 scopus 로고    scopus 로고
    • Structure and dynamics of model pore insertion into a membrane
    • Lopez C.F., Nielsen S.O., Ensing B., Moore P.B., and Klein M.L. Structure and dynamics of model pore insertion into a membrane. Biophys. J. 88 (2005) 3083-3094
    • (2005) Biophys. J. , vol.88 , pp. 3083-3094
    • Lopez, C.F.1    Nielsen, S.O.2    Ensing, B.3    Moore, P.B.4    Klein, M.L.5
  • 104
    • 0029594533 scopus 로고
    • Membrane thinning caused by magainin 2
    • Ludtke S., He K., and Huang H. Membrane thinning caused by magainin 2. Biochemistry 34 (1995) 16764-16769
    • (1995) Biochemistry , vol.34 , pp. 16764-16769
    • Ludtke, S.1    He, K.2    Huang, H.3
  • 105
    • 0033027685 scopus 로고    scopus 로고
    • Spring constants for channel induced lipid bilayer deformations. Estimates using gramicidin channels
    • Lundbæk J.A., and Andersen O.S. Spring constants for channel induced lipid bilayer deformations. Estimates using gramicidin channels. Biophys. J. 76 (1999) 889-895
    • (1999) Biophys. J. , vol.76 , pp. 889-895
    • Lundbæk, J.A.1    Andersen, O.S.2
  • 106
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: structure and implications
    • MacKenzie K.R., Prestegard J.H., and Engelmann D.M. A transmembrane helix dimer: structure and implications. Science 276 (1997) 131-133
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelmann, D.M.3
  • 107
    • 0035899991 scopus 로고    scopus 로고
    • Self-association of model transmembrane helix is modulated by lipid structure
    • Mall S., Broadbridge R., Sharma R.P., East J.M., and Lee A.G. Self-association of model transmembrane helix is modulated by lipid structure. Biochemistry 40 (2001) 12379-12386
    • (2001) Biochemistry , vol.40 , pp. 12379-12386
    • Mall, S.1    Broadbridge, R.2    Sharma, R.P.3    East, J.M.4    Lee, A.G.5
  • 108
    • 0035812110 scopus 로고    scopus 로고
    • Effect of undulations on surface tension in simulated bilayers
    • Marrink S.J., and Mark A.E. Effect of undulations on surface tension in simulated bilayers. J. Phys. Chem. B. 105 (2001) 6122-6127
    • (2001) J. Phys. Chem. B. , vol.105 , pp. 6122-6127
    • Marrink, S.J.1    Mark, A.E.2
  • 109
    • 0344589334 scopus 로고    scopus 로고
    • Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling
    • Marsh D., and Horvath L.I. Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling. Biochim. Biophys. Acta 1376 (1998) 267-296
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 267-296
    • Marsh, D.1    Horvath, L.I.2
  • 110
    • 0033768029 scopus 로고    scopus 로고
    • Theories on structural perturbations of lipid bilayers
    • May S. Theories on structural perturbations of lipid bilayers. Curr. Opin. Colloid Interf. Sci. 5 (2000) 244-249
    • (2000) Curr. Opin. Colloid Interf. Sci. , vol.5 , pp. 244-249
    • May, S.1
  • 111
    • 0034667495 scopus 로고    scopus 로고
    • A molecular model for lipid-mediated interaction between proteins in membranes
    • May S., and Ben-Shaul A. A molecular model for lipid-mediated interaction between proteins in membranes. Phys. Chem. Chem. Phys. 2 (2000) 4494-4502
    • (2000) Phys. Chem. Chem. Phys. , vol.2 , pp. 4494-4502
    • May, S.1    Ben-Shaul, A.2
  • 112
    • 0033807597 scopus 로고    scopus 로고
    • Lipid demixing and protein-protein interactions in the adsorption of charged proteins on mixed membranes
    • May S., Harries D., and Ben-Shaul A. Lipid demixing and protein-protein interactions in the adsorption of charged proteins on mixed membranes. Biophys. J. 79 (2000) 1747-1760
    • (2000) Biophys. J. , vol.79 , pp. 1747-1760
    • May, S.1    Harries, D.2    Ben-Shaul, A.3
  • 113
    • 18744365208 scopus 로고    scopus 로고
    • Macroion-induced compositional instability of binary fluid membranes
    • May S., Harries D., and Ben-Shaul A. Macroion-induced compositional instability of binary fluid membranes. Phys. Rev. Lett. 89 (2002) 268102-268105
    • (2002) Phys. Rev. Lett. , vol.89 , pp. 268102-268105
    • May, S.1    Harries, D.2    Ben-Shaul, A.3
  • 114
    • 0037031440 scopus 로고    scopus 로고
    • Membrane perturbations induced by integral proteins: role of conformational restrictions of the lipid chains
    • May S. Membrane perturbations induced by integral proteins: role of conformational restrictions of the lipid chains. Langmuir 18 (2002) 6356-6364
    • (2002) Langmuir , vol.18 , pp. 6356-6364
    • May, S.1
  • 116
    • 21244448091 scopus 로고    scopus 로고
    • Domain formation induced by the adsorption of charged proteins on mixed lipid membranes
    • Mbamala E.C., Ben-Shaul A., and May S. Domain formation induced by the adsorption of charged proteins on mixed lipid membranes. Biophys. J. 88 (2005) 1702-1714
    • (2005) Biophys. J. , vol.88 , pp. 1702-1714
    • Mbamala, E.C.1    Ben-Shaul, A.2    May, S.3
  • 118
    • 0041821501 scopus 로고    scopus 로고
    • Sorting of lipids and transmembrane peptides between detergent-soluble bilayers and detergent-resistant rafts
    • McIntosh T.J., Vidal A., and Simon S.A. Sorting of lipids and transmembrane peptides between detergent-soluble bilayers and detergent-resistant rafts. Biophys. J. 85 (2003) 1656-1666
    • (2003) Biophys. J. , vol.85 , pp. 1656-1666
    • McIntosh, T.J.1    Vidal, A.2    Simon, S.A.3
  • 119
    • 0029099311 scopus 로고
    • A Monte Carlo model of fd Pf1 proteins in lipid membranes
    • Milik M., and Skolnick J. A Monte Carlo model of fd Pf1 proteins in lipid membranes. Biophys. J. 69 (1995) 1382-1386
    • (1995) Biophys. J. , vol.69 , pp. 1382-1386
    • Milik, M.1    Skolnick, J.2
  • 120
    • 0020486964 scopus 로고
    • Bilayer thickness and enzymatic activity in the mitochondrial cytochrome c oxidase and ATPase complex
    • Montecucco C., Smith G.A., Dabbeni-Sala F., Johansson A., Galante Y.M., and Bisson R. Bilayer thickness and enzymatic activity in the mitochondrial cytochrome c oxidase and ATPase complex. FEBS Lett. 144 (1982) 145-148
    • (1982) FEBS Lett. , vol.144 , pp. 145-148
    • Montecucco, C.1    Smith, G.A.2    Dabbeni-Sala, F.3    Johansson, A.4    Galante, Y.M.5    Bisson, R.6
  • 121
    • 0036199831 scopus 로고    scopus 로고
    • Characterization of the thermotropic behaviour and lateral organization of lipid-peptide mixtures by a combined experimental and theoretical approach: effects of hydrophobic mismatch and role of flanking residues
    • Morein S., Killian J.A., and Sperotto M.M. Characterization of the thermotropic behaviour and lateral organization of lipid-peptide mixtures by a combined experimental and theoretical approach: effects of hydrophobic mismatch and role of flanking residues. Biophys. J. 82 (2002) 1405-1417
    • (2002) Biophys. J. , vol.82 , pp. 1405-1417
    • Morein, S.1    Killian, J.A.2    Sperotto, M.M.3
  • 122
    • 0031914886 scopus 로고    scopus 로고
    • Self-assembly and organization of lipid-protein membranes
    • Mouritsen M.M. Self-assembly and organization of lipid-protein membranes. Curr. Opin. Colloid Interf. Sci. 3 (1998) 78-87
    • (1998) Curr. Opin. Colloid Interf. Sci. , vol.3 , pp. 78-87
    • Mouritsen, M.M.1
  • 123
    • 0021474573 scopus 로고
    • Mattress model of lipid-protein interactions in membranes
    • Mouritsen O.G., and Blom M. Mattress model of lipid-protein interactions in membranes. Biophys. J. 46 (1984) 141-153
    • (1984) Biophys. J. , vol.46 , pp. 141-153
    • Mouritsen, O.G.1    Blom, M.2
  • 124
    • 0008642108 scopus 로고
    • Thermodynamics of lipid-protein interactions in lipid membranes
    • Jackson M. (Ed), CRC Press, Inc, Boca Raton, FL
    • Mouritsen O.G., and Sperotto M.M. Thermodynamics of lipid-protein interactions in lipid membranes. In: Jackson M. (Ed). Thermodynamics of Membrane Receptors and Channels (1993), CRC Press, Inc, Boca Raton, FL 127-181
    • (1993) Thermodynamics of Membrane Receptors and Channels , pp. 127-181
    • Mouritsen, O.G.1    Sperotto, M.M.2
  • 126
    • 0029165107 scopus 로고
    • An investigation of the role of transmembrane domain in Golgi protein retention
    • Munro S. An investigation of the role of transmembrane domain in Golgi protein retention. EMBO J. 14 (1995) 4695-4704
    • (1995) EMBO J. , vol.14 , pp. 4695-4704
    • Munro, S.1
  • 127
    • 0031976015 scopus 로고    scopus 로고
    • Localization of proteins to the Golgi apparatus
    • Munro S. Localization of proteins to the Golgi apparatus. Trends Cell Biol. 8 (1998) 11-15
    • (1998) Trends Cell Biol. , vol.8 , pp. 11-15
    • Munro, S.1
  • 128
    • 22244472946 scopus 로고    scopus 로고
    • Lipid bilayer perturbations around a transmembrane nanotube: a coarse grain molecular dynamics study
    • Nielsen S.O., Ensing B., Ortiz V., Moore P.B., and Klein M.L. Lipid bilayer perturbations around a transmembrane nanotube: a coarse grain molecular dynamics study. Biophys. J. 88 (2005) 3822-3828
    • (2005) Biophys. J. , vol.88 , pp. 3822-3828
    • Nielsen, S.O.1    Ensing, B.2    Ortiz, V.3    Moore, P.B.4    Klein, M.L.5
  • 130
    • 0031895461 scopus 로고    scopus 로고
    • Energetics of inclusion-induced bilayer deformations
    • Nielsen C., Goulian M., and Andersen O.S. Energetics of inclusion-induced bilayer deformations. Biophys. J. 74 (1998) 1966-1983
    • (1998) Biophys. J. , vol.74 , pp. 1966-1983
    • Nielsen, C.1    Goulian, M.2    Andersen, O.S.3
  • 131
    • 22244472946 scopus 로고    scopus 로고
    • Lipid bilayer perturbations around a transmembrane nanotube: a coarse grain molecular dynamics study
    • Nielsen S.O., Ensing B., Ortiz V., Moore P.M., and Klein M.L. Lipid bilayer perturbations around a transmembrane nanotube: a coarse grain molecular dynamics study. Biophys. J. 88 (2005) 3822-3828
    • (2005) Biophys. J. , vol.88 , pp. 3822-3828
    • Nielsen, S.O.1    Ensing, B.2    Ortiz, V.3    Moore, P.M.4    Klein, M.L.5
  • 132
    • 1642546396 scopus 로고    scopus 로고
    • Atomic simulations of protein folding, using the replica exchange algorithm
    • Nymeyer H., Gnanakaran S., and Garcia A.E. Atomic simulations of protein folding, using the replica exchange algorithm. Meth. Enzymol. 383 (2004) 119-149
    • (2004) Meth. Enzymol. , vol.383 , pp. 119-149
    • Nymeyer, H.1    Gnanakaran, S.2    Garcia, A.E.3
  • 133
    • 18844362955 scopus 로고    scopus 로고
    • Folding is not required for bilayer insertion: replica exchange simulations of an α-helical peptide with an explicit lipid bilayer
    • Nymeyer H., Woolf T.B., and Garcia A.E. Folding is not required for bilayer insertion: replica exchange simulations of an α-helical peptide with an explicit lipid bilayer. Proteins 59 (2005) 783-790
    • (2005) Proteins , vol.59 , pp. 783-790
    • Nymeyer, H.1    Woolf, T.B.2    Garcia, A.E.3
  • 135
    • 0027489133 scopus 로고
    • Sorting of membrane-proteins in the secretory pathway
    • Pelham H.R.B., and Munro S. Sorting of membrane-proteins in the secretory pathway. Cell 75 (1993) 603-605
    • (1993) Cell , vol.75 , pp. 603-605
    • Pelham, H.R.B.1    Munro, S.2
  • 136
    • 0041929590 scopus 로고    scopus 로고
    • Structure and mechanism in prokaryotic mechanosensitive channels
    • Perozo E., and Rees D.C. Structure and mechanism in prokaryotic mechanosensitive channels. Curr. Opin. Struct. Biol. 13 (2003) 432-442
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 432-442
    • Perozo, E.1    Rees, D.C.2
  • 137
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • Perozo E., Kloda A., Cortes D., and Martinac B. Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating. Nat. Struct. Biol. 9 (2002) 696-703
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.3    Martinac, B.4
  • 139
    • 0034703270 scopus 로고    scopus 로고
    • Modulation of glycophorin A transmembrane helix interactions by lipid bilayers: molecular dynamics calculations
    • Petrache H.I., Grossfield A., MacKenzie K.R., Engelman D.M., and Woolf T. Modulation of glycophorin A transmembrane helix interactions by lipid bilayers: molecular dynamics calculations. J. Mol. Biol. 302 (2000) 727-746
    • (2000) J. Mol. Biol. , vol.302 , pp. 727-746
    • Petrache, H.I.1    Grossfield, A.2    MacKenzie, K.R.3    Engelman, D.M.4    Woolf, T.5
  • 141
    • 0027135397 scopus 로고
    • Hydrophobic mismatch and long-range protein/lipid interactions in bacteriorhodopsin/phosphatidylcholine vesicles
    • Piknová B., Pérochon E., and Tocanne J.-F. Hydrophobic mismatch and long-range protein/lipid interactions in bacteriorhodopsin/phosphatidylcholine vesicles. Eur. J. Biochem. 218 (1993) 385-396
    • (1993) Eur. J. Biochem. , vol.218 , pp. 385-396
    • Piknová, B.1    Pérochon, E.2    Tocanne, J.-F.3
  • 142
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • Popot J.-L., and Engelman D.M. Helical membrane protein folding, stability, and evolution. Ann. Rev. Biochem. 69 (2000) 881-922
    • (2000) Ann. Rev. Biochem. , vol.69 , pp. 881-922
    • Popot, J.-L.1    Engelman, D.M.2
  • 143
    • 14644398554 scopus 로고    scopus 로고
    • Orientation of β-barrel protein OmpA and PhuA in lipid membranes. Chain length dependence from infrared dichroism
    • Ramakrishnan M., Qu J., Pocanschi C.L., Kleinschmidt J.H., and Marsh D. Orientation of β-barrel protein OmpA and PhuA in lipid membranes. Chain length dependence from infrared dichroism. Biochemistry 44 (2005) 3515-3523
    • (2005) Biochemistry , vol.44 , pp. 3515-3523
    • Ramakrishnan, M.1    Qu, J.2    Pocanschi, C.L.3    Kleinschmidt, J.H.4    Marsh, D.5
  • 144
    • 0022405005 scopus 로고
    • Long-range lipid-protein interactions. Evidence from time-resolved fluorescence depolarization and energy-transfer experiments with bacteriorhodopsin-dimyristoylphosphatidylcholine vesicles
    • Rehorek M., Dencher N.A., and Heyn M.P. Long-range lipid-protein interactions. Evidence from time-resolved fluorescence depolarization and energy-transfer experiments with bacteriorhodopsin-dimyristoylphosphatidylcholine vesicles. Biochemistry 24 (1985) 5980-5988
    • (1985) Biochemistry , vol.24 , pp. 5980-5988
    • Rehorek, M.1    Dencher, N.A.2    Heyn, M.P.3
  • 146
    • 0028321565 scopus 로고
    • Molecular dynamics simulations of the gramicidin channel
    • Roux B., and 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
  • 147
    • 0000380033 scopus 로고
    • Physical basis of trigger processes and membrane structure
    • Chapman D. (Ed), Academic Press, London
    • Sackmann E. Physical basis of trigger processes and membrane structure. In: Chapman D. (Ed). Biological Membranes vol. 5 (1984), Academic Press, London 105-143
    • (1984) Biological Membranes , vol.5 , pp. 105-143
    • Sackmann, E.1
  • 148
    • 0001810937 scopus 로고
    • Biological membranes architecture and function
    • Lipowsky R., and Sackmann E. (Eds), Elsevier, Amsterdam
    • Sackmann E. Biological membranes architecture and function. In: Lipowsky R., and Sackmann E. (Eds). Structure and Dynamics of Membranes (1995), Elsevier, Amsterdam 1-65
    • (1995) Structure and Dynamics of Membranes , pp. 1-65
    • Sackmann, E.1
  • 149
    • 0026058626 scopus 로고
    • Conformation and aggregation of M13 coat protein studied by molecular dynamics
    • Sanders J.C., van Nuland N.A., Edholm O., and Hemminga M.A. Conformation and aggregation of M13 coat protein studied by molecular dynamics. Biophys. Chem. 41 (1991) 193-202
    • (1991) Biophys. Chem. , vol.41 , pp. 193-202
    • Sanders, J.C.1    van Nuland, N.A.2    Edholm, O.3    Hemminga, M.A.4
  • 150
    • 0033747203 scopus 로고    scopus 로고
    • MD simulations predict a tilted orientation for the helical region of dynorphon A(1-17) in DPPC bilayers
    • Sankararamakrishnnan R., and Weinstein H. MD simulations predict a tilted orientation for the helical region of dynorphon A(1-17) in DPPC bilayers. Biophys. J. 79 (2000) 2331-2344
    • (2000) Biophys. J. , vol.79 , pp. 2331-2344
    • Sankararamakrishnnan, R.1    Weinstein, H.2
  • 151
    • 0037459073 scopus 로고    scopus 로고
    • Protein translocons: multifunctional mediators of protein translocation across membranes
    • Schnell D.J., and Hebert D.N. Protein translocons: multifunctional mediators of protein translocation across membranes. Cell 112 (2003) 491-505
    • (2003) Cell , vol.112 , pp. 491-505
    • Schnell, D.J.1    Hebert, D.N.2
  • 152
    • 0041843693 scopus 로고    scopus 로고
    • Molecular dynamics simulation of dimeric and monomeric forms of human prion protein: insight into dynamics and properties
    • Sekijima M., Satoshi Yamasaki S., Kaneko K., and Akiyama Y. Molecular dynamics simulation of dimeric and monomeric forms of human prion protein: insight into dynamics and properties. Biophys. J. 85 (2003) 1176-1185
    • (2003) Biophys. J. , vol.85 , pp. 1176-1185
    • Sekijima, M.1    Satoshi Yamasaki, S.2    Kaneko, K.3    Akiyama, Y.4
  • 153
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462 (1999) 55-70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 154
    • 0036284109 scopus 로고    scopus 로고
    • Organization of model helical peptides in lipid bilayers: insight into the behaviour of single-span protein transmembrane domains
    • Sharpe S., Barber K.R., Grant C.W.M., Goodyear D., and Morrow M.R. Organization of model helical peptides in lipid bilayers: insight into the behaviour of single-span protein transmembrane domains. Biophys. J. 83 (2002) 345-358
    • (2002) Biophys. J. , vol.83 , pp. 345-358
    • Sharpe, S.1    Barber, K.R.2    Grant, C.W.M.3    Goodyear, D.4    Morrow, M.R.5
  • 155
    • 0030966534 scopus 로고    scopus 로고
    • Transmembrane helix structure, dynamics, and interactions: multi-nanoseconds molecular dynamics simulations
    • Shen L., Bassolino D., and Stouch T. Transmembrane helix structure, dynamics, and interactions: multi-nanoseconds molecular dynamics simulations. Biophys. J. 73 (1997) 3-20
    • (1997) Biophys. J. , vol.73 , pp. 3-20
    • Shen, L.1    Bassolino, D.2    Stouch, T.3
  • 158
    • 0037443086 scopus 로고    scopus 로고
    • Interaction of the designed antimicrobial peptide MB21 and truncated dermaseptin S3 with lipid bilayers: molecular dynamics simulations
    • Shepherd C.M., Vogel H.J., and Tieleman D.P. Interaction of the designed antimicrobial peptide MB21 and truncated dermaseptin S3 with lipid bilayers: molecular dynamics simulations. Biochem. J. 370 (2003) 233-243
    • (2003) Biochem. J. , vol.370 , pp. 233-243
    • Shepherd, C.M.1    Vogel, H.J.2    Tieleman, D.P.3
  • 159
    • 0037044173 scopus 로고    scopus 로고
    • Equilibrium structure and lateral stress distribution of amphiphilic bilayers from dissipative particle dynamics
    • Shillcock J.C., and Lipowsky R. Equilibrium structure and lateral stress distribution of amphiphilic bilayers from dissipative particle dynamics. J. Phys. Chem. 117 (2002) 5048-5061
    • (2002) J. Phys. Chem. , vol.117 , pp. 5048-5061
    • Shillcock, J.C.1    Lipowsky, R.2
  • 160
    • 0032926928 scopus 로고    scopus 로고
    • The modified stalk mechanism of lamellar/inverted phase transitions and its implication for membrane fusion
    • Siegel D.P. The modified stalk mechanism of lamellar/inverted phase transitions and its implication for membrane fusion. Biophys. J. 76 (1999) 291-313
    • (1999) Biophys. J. , vol.76 , pp. 291-313
    • Siegel, D.P.1
  • 161
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 162
    • 0342601426 scopus 로고    scopus 로고
    • Protein attraction in membranes induced by lipid fluctuations
    • Sintes T., and Baumgärtner A. Protein attraction in membranes induced by lipid fluctuations. Biophys. J. 73 (1997) 2251-2259
    • (1997) Biophys. J. , vol.73 , pp. 2251-2259
    • Sintes, T.1    Baumgärtner, A.2
  • 163
    • 0031996814 scopus 로고    scopus 로고
    • Membrane mediated protein attraction. A Monte-Carlo study
    • Sintes T., and Baumgaertner A. Membrane mediated protein attraction. A Monte-Carlo study. Physica A 249 (1998) 571-575
    • (1998) Physica A , vol.249 , pp. 571-575
    • Sintes, T.1    Baumgaertner, A.2
  • 164
    • 13544256698 scopus 로고    scopus 로고
    • Molecular dynamics study of gating in the mechanosensitive channel of small conductance MscS
    • Sotomayor M., and Schulten K. Molecular dynamics study of gating in the mechanosensitive channel of small conductance MscS. Biophys. J. 87 (2004) 3050-3060
    • (2004) Biophys. J. , vol.87 , pp. 3050-3060
    • Sotomayor, M.1    Schulten, K.2
  • 165
    • 0030839366 scopus 로고    scopus 로고
    • A theoretical model for the association of amphiphilic transmembrane peptides in lipid bilayers
    • Sperotto M.M. A theoretical model for the association of amphiphilic transmembrane peptides in lipid bilayers. Eur. Biophys. J. 26 (1997) 405-416
    • (1997) Eur. Biophys. J. , vol.26 , pp. 405-416
    • Sperotto, M.M.1
  • 166
    • 0026071516 scopus 로고
    • Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins
    • Sperotto M.M., and Mouritsen. Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins. Biophys. J. 59 (1991) 261-270
    • (1991) Biophys. J. , vol.59 , pp. 261-270
    • Sperotto, M.M.1    Mouritsen2
  • 169
    • 3142652571 scopus 로고    scopus 로고
    • Bilayer-dependent inhibition of mechanosensitive channels by neuroactive peptide enantiomers
    • Suchyna T.M., Tape S.E., Koeppe R.E., Andersen O.S., Sachs F., and Gottlieb P.A. Bilayer-dependent inhibition of mechanosensitive channels by neuroactive peptide enantiomers. Nature 430 (2004) 235-240
    • (2004) Nature , vol.430 , pp. 235-240
    • Suchyna, T.M.1    Tape, S.E.2    Koeppe, R.E.3    Andersen, O.S.4    Sachs, F.5    Gottlieb, P.A.6
  • 170
    • 0001616080 scopus 로고    scopus 로고
    • Replica-exchange molecular dynamics method for protein folding
    • Sugita Y., and Okamoto Y. Replica-exchange molecular dynamics method for protein folding. Chem. Phys. Lett. 314 (1999) 141-151
    • (1999) Chem. Phys. Lett. , vol.314 , pp. 141-151
    • Sugita, Y.1    Okamoto, Y.2
  • 171
    • 0035825634 scopus 로고    scopus 로고
    • Gating mechanism of the large mechanosensitive channel MscL
    • Sukharov S., Betanzos M., Chiang C.S., and Guy H.R. Gating mechanism of the large mechanosensitive channel MscL. Nature 409 (2001) 720-724
    • (2001) Nature , vol.409 , pp. 720-724
    • Sukharov, S.1    Betanzos, M.2    Chiang, C.S.3    Guy, H.R.4
  • 172
    • 35949020425 scopus 로고
    • Replica Monte Carlo simulation of spin-glasses
    • Swendsen R., and Wang J. Replica Monte Carlo simulation of spin-glasses. Phys. Rev. Lett. 57 (1986) 2607-2609
    • (1986) Phys. Rev. Lett. , vol.57 , pp. 2607-2609
    • Swendsen, R.1    Wang, J.2
  • 174
    • 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. A computer perspective of membranes: molecular dynamics studies of lipid bilayer systems. Biophys. Biochim. Acta 1331 (1997) 235-270
    • (1997) Biophys. Biochim. Acta , vol.1331 , pp. 235-270
    • Tieleman, D.P.1    Marrink, S.J.2    Berendsen, H.J.C.3
  • 175
    • 0032951553 scopus 로고    scopus 로고
    • Alamethicin helices in a bilayer and in solution: molecular dynamics simulations
    • Tieleman D.P., Sansom M.S.P., and Berendsen H.J.C. Alamethicin helices in a bilayer and in solution: molecular dynamics simulations. Biophys. J. 76 (1999) 40-49
    • (1999) Biophys. J. , vol.76 , pp. 40-49
    • Tieleman, D.P.1    Sansom, M.S.P.2    Berendsen, H.J.C.3
  • 176
    • 0033035249 scopus 로고    scopus 로고
    • An alamethicin channel in a lipid bilayer: molecular dynamics simulations
    • Tieleman D.P., Berendsen H.J.C., and Sansom M.S.P. An alamethicin channel in a lipid bilayer: molecular dynamics simulations. Biophys. J. 76 (1999) 1757-1769
    • (1999) Biophys. J. , vol.76 , pp. 1757-1769
    • Tieleman, D.P.1    Berendsen, H.J.C.2    Sansom, M.S.P.3
  • 177
    • 0035132984 scopus 로고    scopus 로고
    • Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces
    • Tieleman D.P., Berendsen H.J.C., and Sansom M.S.P. Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces. Biophys. J. 80 (2001) 331-346
    • (2001) Biophys. J. , vol.80 , pp. 331-346
    • Tieleman, D.P.1    Berendsen, H.J.C.2    Sansom, M.S.P.3
  • 178
    • 0001794260 scopus 로고
    • Detection of lipid domains in biological membranes
    • Tocanne J.-F. Detection of lipid domains in biological membranes. Comm. Mol. Cell. Biophys. 8 (1992) 53-72
    • (1992) Comm. Mol. Cell. Biophys. , vol.8 , pp. 53-72
    • Tocanne, J.-F.1
  • 180
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, alpha-helical antimicrobial peptides
    • Tossi A., Sandri L., and Giangaspero A. Amphipathic, alpha-helical antimicrobial peptides. Biopolymers 55 (2000) 4-30
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 185
    • 0024403443 scopus 로고
    • Influence of sterols and phospholipids on sarcolemmal and sarcoplasmic reticular cation transporters
    • Vemuri R., and Philipson K.D. Influence of sterols and phospholipids on sarcolemmal and sarcoplasmic reticular cation transporters. J. Biol. Chem. 264 (1989) 8680-8685
    • (1989) J. Biol. Chem. , vol.264 , pp. 8680-8685
    • Vemuri, R.1    Philipson, K.D.2
  • 186
    • 16244363029 scopus 로고    scopus 로고
    • Simulating the self-assembly of model membranes
    • Venturoli M., and Smit B. Simulating the self-assembly of model membranes. Phys. Chem. Comm. 10 (1999)
    • (1999) Phys. Chem. Comm. , vol.10
    • Venturoli, M.1    Smit, B.2
  • 187
    • 21244431672 scopus 로고    scopus 로고
    • Simulation studies of protein-induced bilayer deformations, and lipid-induced protein tilting, on a mesoscopic model for lipid bilayers with embedded proteins
    • Venturoli M., Smit B., and Sperotto M.M. Simulation studies of protein-induced bilayer deformations, and lipid-induced protein tilting, on a mesoscopic model for lipid bilayers with embedded proteins. Biophys. J. 88 (2005) 1778-1798
    • (2005) Biophys. J. , vol.88 , pp. 1778-1798
    • Venturoli, M.1    Smit, B.2    Sperotto, M.M.3
  • 188
    • 0025681503 scopus 로고
    • Membrane proteins: from sequence to structure
    • von Heijne G., and Manoil M. Membrane proteins: from sequence to structure. Protein Eng. 4 (1990) 109-112
    • (1990) Protein Eng. , vol.4 , pp. 109-112
    • von Heijne, G.1    Manoil, M.2
  • 189
    • 1942487766 scopus 로고    scopus 로고
    • A computational model for the electrostatic sequestration of PI(4,5)P-2 by membrane-adsorbed basic peptides
    • Wang J.Y., Gambhir A., McLaughlin S., and Murray D. A computational model for the electrostatic sequestration of PI(4,5)P-2 by membrane-adsorbed basic peptides. Biophys. J. 86 (2004) 1969-1986
    • (2004) Biophys. J. , vol.86 , pp. 1969-1986
    • Wang, J.Y.1    Gambhir, A.2    McLaughlin, S.3    Murray, D.4
  • 191
    • 0028013531 scopus 로고
    • Peptides in lipid bilayers: structural and thermodynamic basis for partitioning and folding
    • White S.H., and Wimley W.C. Peptides in lipid bilayers: structural and thermodynamic basis for partitioning and folding. Curr. Opin. Struct. Biol. 4 (1994) 79-86
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 79-86
    • White, S.H.1    Wimley, W.C.2
  • 192
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: physical principles
    • White S.H., and Wimley W.C. Membrane protein folding and stability: physical principles. Ann. Rev. Biophys. Biomol. Struct. 28 (1999) 319-365
    • (1999) Ann. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 193
  • 194
    • 0026729232 scopus 로고
    • Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of X-ray and neutron diffraction data. III. Complete structure
    • Wiener C.M., and White S.H. Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of
    • (1992) Biophys. J. , vol.61 , pp. 437-447
    • Wiener, C.M.1    White, S.H.2
  • 196
    • 0037379687 scopus 로고    scopus 로고
    • Energetics and self-assembly of amphipathic peptide pores in lipid membranes
    • Zemel A., Fattal D.R., and Ben-Shaul A. Energetics and self-assembly of amphipathic peptide pores in lipid membranes. Biophys. J. 84 (2003) 2242-2255
    • (2003) Biophys. J. , vol.84 , pp. 2242-2255
    • Zemel, A.1    Fattal, D.R.2    Ben-Shaul, A.3
  • 197
    • 2942692314 scopus 로고    scopus 로고
    • Membrane perturbation induced by interfacially adsorbed peptides
    • Zemel A., Ben-Shaul A., and May S. Membrane perturbation induced by interfacially adsorbed peptides. Biophys. J. 86 (2004) 3607-3619
    • (2004) Biophys. J. , vol.86 , pp. 3607-3619
    • Zemel, A.1    Ben-Shaul, A.2    May, S.3
  • 198
    • 18844409111 scopus 로고    scopus 로고
    • Perturbation of a lipid membrane by amphipathic peptides and its role in pore formation
    • Zemel A., Ben-Shaul A., and May S. Perturbation of a lipid membrane by amphipathic peptides and its role in pore formation. Eur. Biophys. J. 34 (2005) 230-243
    • (2005) Eur. Biophys. J. , vol.34 , pp. 230-243
    • Zemel, A.1    Ben-Shaul, A.2    May, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.