메뉴 건너뛰기




Volumn 92, Issue 11, 2007, Pages 3978-3987

Interaction of alamethicin pores in DMPC bilayers

Author keywords

[No Author keywords available]

Indexed keywords

ALAMETHICIN; DIMYRISTOYLPHOSPHATIDYLCHOLINE;

EID: 34250373778     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.101204     Document Type: Article
Times cited : (34)

References (66)
  • 1
    • 0033587719 scopus 로고    scopus 로고
    • Characterization of lipid bilayer phases by confocal microscopy and fluorescence correlation spectroscopy
    • Korlach, J., P. Schwille, W. Webb, and G. Feigenson. 1999. Characterization of lipid bilayer phases by confocal microscopy and fluorescence correlation spectroscopy. Proc. Natl. Acad. Sci. USA. 96:8461-8466.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8461-8466
    • Korlach, J.1    Schwille, P.2    Webb, W.3    Feigenson, G.4
  • 3
    • 0035498468 scopus 로고    scopus 로고
    • Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues
    • Duclohier, H., and H. Wróblewski. 2001. Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues. J. Membr. Biol. 184:1-12.
    • (2001) J. Membr. Biol , vol.184 , pp. 1-12
    • Duclohier, H.1    Wróblewski, H.2
  • 4
    • 36549093656 scopus 로고
    • Circular dichroism of oriented α helices. I. Proof of the exciton theory
    • Olah, G. A., and H. W. Huang. 1988. Circular dichroism of oriented α helices. I. Proof of the exciton theory. J. Chem. Phys. 89:2531-2538.
    • (1988) J. Chem. Phys , vol.89 , pp. 2531-2538
    • Olah, G.A.1    Huang, H.W.2
  • 5
    • 0036156880 scopus 로고    scopus 로고
    • Sigmoidal concentration dependence of antimicrobial peptide activities: A case study on alamethicin
    • Chen, F.-Y., M.-T. Lee, and H. W. Huang. 2002. Sigmoidal concentration dependence of antimicrobial peptide activities: a case study on alamethicin. Biophys. J. 82:908-914.
    • (2002) Biophys. J , vol.82 , pp. 908-914
    • Chen, F.-Y.1    Lee, M.-T.2    Huang, H.W.3
  • 6
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • Bechinger, B. 1999. The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim. Biophys. Acta. 1462:157-183.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 7
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin
    • Bechinger, B. 1997. Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 156:197-211.
    • (1997) J. Membr. Biol , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 8
    • 0017073034 scopus 로고
    • Voltage-induced formation of alamethicin pores in lecithin bilayer vesicles
    • Lau, A. L. Y., and S. I. Chan. 1976. Voltage-induced formation of alamethicin pores in lecithin bilayer vesicles. Biochemistry. 15:2551-2555.
    • (1976) Biochemistry , vol.15 , pp. 2551-2555
    • Lau, A.L.Y.1    Chan, S.I.2
  • 9
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai, Y. 1999. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta. 1462:55-70.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 10
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • Huang, H. 2000. Action of antimicrobial peptides: two-state model. Biochemistry. 39:8347-8352.
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.1
  • 11
    • 0028790410 scopus 로고
    • Antimicrobial peptide pores in membranes detected by neutron in-plane scattering
    • He, K., S. J. Ludtke, H. W. Huang, and D. L. Worcester. 1995. Antimicrobial peptide pores in membranes detected by neutron in-plane scattering. Biochemistry. 34:15614-15618.
    • (1995) Biochemistry , vol.34 , pp. 15614-15618
    • He, K.1    Ludtke, S.J.2    Huang, H.W.3    Worcester, D.L.4
  • 12
    • 0030028241 scopus 로고    scopus 로고
    • Neutron scattering in the plane of the membranes: Structure of alamethicin pores
    • He, K., S. J. Ludtke, D. L. Worcester, and H. W. Huang. 1996. Neutron scattering in the plane of the membranes: structure of alamethicin pores. Biophys. J. 70:2659-2666.
    • (1996) Biophys. J , vol.70 , pp. 2659-2666
    • He, K.1    Ludtke, S.J.2    Worcester, D.L.3    Huang, H.W.4
  • 13
    • 0032725432 scopus 로고    scopus 로고
    • Supramolecular structures of peptide assemblies in membranes by neutron off-plane scattering: Method of analysis
    • Yang, L., T. Weiss, T. Harroun, W. Heller, and H. Huang. 1999. Supramolecular structures of peptide assemblies in membranes by neutron off-plane scattering: method of analysis. Biophys. J. 77:2648-2656.
    • (1999) Biophys. J , vol.77 , pp. 2648-2656
    • Yang, L.1    Weiss, T.2    Harroun, T.3    Heller, W.4    Huang, H.5
  • 14
    • 0033638788 scopus 로고    scopus 로고
    • Lipid-mediated interactions between intrinsic membrane proteins: A theoretical study based on integral equations
    • Lagüe, P., M. J. Zuckermann, and B. Roux. 2000. Lipid-mediated interactions between intrinsic membrane proteins: a theoretical study based on integral equations. Biophys. J. 79:2867-2879.
    • (2000) Biophys. J , vol.79 , pp. 2867-2879
    • Lagüe, P.1    Zuckermann, M.J.2    Roux, B.3
  • 15
    • 0034950310 scopus 로고    scopus 로고
    • Lipid-mediated interactions between intrinsic membrane proteins: Dependence on protein size and lipid composition
    • Lagüe, P., M. J. Zuckermann, and B. Roux. 2001. Lipid-mediated interactions between intrinsic membrane proteins: dependence on protein size and lipid composition. Biophys. J. 81:276-284.
    • (2001) Biophys. J , vol.81 , pp. 276-284
    • Lagüe, P.1    Zuckermann, M.J.2    Roux, B.3
  • 16
    • 0029594533 scopus 로고
    • Membrane thinning caused by magainin 2
    • Ludtke, S. J., K. He, and H. W. Huang. 1995. Membrane thinning caused by magainin 2. Biochemistry. 34:16764-16769.
    • (1995) Biochemistry , vol.34 , pp. 16764-16769
    • Ludtke, S.J.1    He, K.2    Huang, H.W.3
  • 17
    • 0033798839 scopus 로고    scopus 로고
    • Crystallization of antimicrobial pores in membranes: Magainin and protegrin
    • Yang, L., T. M. Weiss, R. I. Lehrer, and H. W. Huang. 2000. Crystallization of antimicrobial pores in membranes: magainin and protegrin. Biophys. J. 79:2002-2009.
    • (2000) Biophys. J , vol.79 , pp. 2002-2009
    • Yang, L.1    Weiss, T.M.2    Lehrer, R.I.3    Huang, H.W.4
  • 18
    • 3142768523 scopus 로고    scopus 로고
    • Biomimetic membranes of lipid-peptide model systems prepared on solid support
    • Li, C., D. Constantin, and T. Salditt. 2004. Biomimetic membranes of lipid-peptide model systems prepared on solid support. J. Phys. Cond. Matt. 16:S2439-S2453.
    • (2004) J. Phys. Cond. Matt , vol.16
    • Li, C.1    Constantin, D.2    Salditt, T.3
  • 23
    • 0033932837 scopus 로고    scopus 로고
    • Effect of chain length and unsaturation on elasticity of lipid bilayers
    • Rawicz, W., K. C. Olbrich, T. McIntosh, D. Needham, and E. Evans. 2000. Effect of chain length and unsaturation on elasticity of lipid bilayers. Biophys. J. 79:328-339.
    • (2000) Biophys. J , vol.79 , pp. 328-339
    • Rawicz, W.1    Olbrich, K.C.2    McIntosh, T.3    Needham, D.4    Evans, E.5
  • 24
    • 0029022547 scopus 로고
    • X-ray diffraction study of lipid bilayer membranes interacting with amphiphilic helical peptides: Diphytanoyl phosphatidylcholine with alamethicin at low concentration
    • Wu, Y., K. He, S. J. Ludtke, and H. W. Huang. 1995. X-ray diffraction study of lipid bilayer membranes interacting with amphiphilic helical peptides: diphytanoyl phosphatidylcholine with alamethicin at low concentration. Biophys. J. 68:2361-2369.
    • (1995) Biophys. J , vol.68 , pp. 2361-2369
    • Wu, Y.1    He, K.2    Ludtke, S.J.3    Huang, H.W.4
  • 25
    • 0036226098 scopus 로고    scopus 로고
    • Size distribution of barrel-stave aggregates of membrane peptides: Influence of the bilayer lateral pressure profile
    • Cantor, R. S. 2002. Size distribution of barrel-stave aggregates of membrane peptides: influence of the bilayer lateral pressure profile. Biophys. J. 82:2520-2525.
    • (2002) Biophys. J , vol.82 , pp. 2520-2525
    • Cantor, R.S.1
  • 26
    • 0036841855 scopus 로고    scopus 로고
    • Analysis and evaluation of channel models: Simulations of alamethicin
    • Tieleman, D. P., B. Hess, and M. S. P. Sansom. 2002. Analysis and evaluation of channel models: simulations of alamethicin. Biophys. J. 83:2393-2407.
    • (2002) Biophys. J , vol.83 , pp. 2393-2407
    • Tieleman, D.P.1    Hess, B.2    Sansom, M.S.P.3
  • 27
    • 13844318618 scopus 로고    scopus 로고
    • Surface-sensitive x-ray and neutron scattering characterization of planar lipid model membranes and lipid/peptide interactions
    • Lösche, M. 2002. Surface-sensitive x-ray and neutron scattering characterization of planar lipid model membranes and lipid/peptide interactions. Curr. Topics Membr. 52:117-161.
    • (2002) Curr. Topics Membr , vol.52 , pp. 117-161
    • Lösche, M.1
  • 28
    • 0036488567 scopus 로고    scopus 로고
    • X-ray reflectivity of solid-supported multilamellar membranes
    • Salditt, T., C. Li, A. Spaar, and U. Mennicke. 2002. X-ray reflectivity of solid-supported multilamellar membranes. Eur. Phys. J. E. 7:105-116.
    • (2002) Eur. Phys. J. E , vol.7 , pp. 105-116
    • Salditt, T.1    Li, C.2    Spaar, A.3    Mennicke, U.4
  • 29
    • 21244470784 scopus 로고    scopus 로고
    • Biomolecular and amphiphilic films probed by surface sensitive x-ray and neutron scattering
    • Salditt, T., and G. Brotons. 2004. Biomolecular and amphiphilic films probed by surface sensitive x-ray and neutron scattering. Anal. Bioanal. Chem. 379:960-973.
    • (2004) Anal. Bioanal. Chem , vol.379 , pp. 960-973
    • Salditt, T.1    Brotons, G.2
  • 30
    • 14544273244 scopus 로고    scopus 로고
    • Thermal fluctuations and stability of solid-supported lipid membranes
    • Salditt, T. 2005. Thermal fluctuations and stability of solid-supported lipid membranes. J. Phys. Cond. Matt. 17:R287-R314.
    • (2005) J. Phys. Cond. Matt , vol.17
    • Salditt, T.1
  • 31
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand, R., and H. Vogel. 1999. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta. 1462:11-28.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.1    Vogel, H.2
  • 32
    • 0033035249 scopus 로고    scopus 로고
    • An alamethicin channel in a lipid bilayer: Molecular dynamics simulations
    • Tieleman, D. P., H. J. C. Berendsen, and M. S. P. Sansom. 1999. An alamethicin channel in a lipid bilayer: molecular dynamics simulations. Biophys. J. 76:1757-1769.
    • (1999) Biophys. J , vol.76 , pp. 1757-1769
    • Tieleman, D.P.1    Berendsen, H.J.C.2    Sansom, M.S.P.3
  • 33
    • 5544257743 scopus 로고
    • Free-energy model for the inhomogeneous hardsphere fluid in D dimensions: Structure factors for the hard-disk (D = 2) mixtures in simple explicit form
    • Rosenfeld, Y. 1990. Free-energy model for the inhomogeneous hardsphere fluid in D dimensions: structure factors for the hard-disk (D = 2) mixtures in simple explicit form. Phys. Rev. A. 42:5978-5988.
    • (1990) Phys. Rev. A , vol.42 , pp. 5978-5988
    • Rosenfeld, Y.1
  • 34
    • 0021104115 scopus 로고
    • Bacteriorhodopsin remains dispersed in fluid phospholipid bilayers over a wide range of bilayer thicknesses
    • Lewis, B. A., and D. M. Engelman. 1983. Bacteriorhodopsin remains dispersed in fluid phospholipid bilayers over a wide range of bilayer thicknesses. J. Mol. Biol. 166:203-210.
    • (1983) J. Mol. Biol , vol.166 , pp. 203-210
    • Lewis, B.A.1    Engelman, D.M.2
  • 35
    • 0015737614 scopus 로고
    • Temperature- and light-dependent structural changes in rhodopsin-lipid membranes
    • Chen, Y. S., and W. L. Hubbell. 1973. Temperature- and light-dependent structural changes in rhodopsin-lipid membranes. Exp. Eye Res. 17:517-532.
    • (1973) Exp. Eye Res , vol.17 , pp. 517-532
    • Chen, Y.S.1    Hubbell, W.L.2
  • 36
    • 0015853935 scopus 로고
    • Lipid- and temperature-dependent structural changes in Acholeplasma laidlawii cell membranes
    • James, R., and D. Branton. 1973. Lipid- and temperature-dependent structural changes in Acholeplasma laidlawii cell membranes. Biochim. Biophys. Acta. 323:378-390.
    • (1973) Biochim. Biophys. Acta , vol.323 , pp. 378-390
    • James, R.1    Branton, D.2
  • 37
    • 0023413394 scopus 로고
    • Lateral interactions among membrane proteins: Implications for the organization of gap junctions
    • Abney, J. R., J. Braun, and J. C. Owicki. 1987. Lateral interactions among membrane proteins: implications for the organization of gap junctions. Biophys. J. 52:441-454.
    • (1987) Biophys. J , vol.52 , pp. 441-454
    • Abney, J.R.1    Braun, J.2    Owicki, J.C.3
  • 38
    • 0020589093 scopus 로고
    • Pair distribution functions of bacteriorhodopsin and rhodopsin in model bilayers
    • Pearson, L. T., B. A. Lewis, D. M. Engelman, and S. I. Chan. 1983. Pair distribution functions of bacteriorhodopsin and rhodopsin in model bilayers. Biophys. J. 43:167-174.
    • (1983) Biophys. J , vol.43 , pp. 167-174
    • Pearson, L.T.1    Lewis, B.A.2    Engelman, D.M.3    Chan, S.I.4
  • 39
    • 0021239203 scopus 로고
    • Statistical mechanics of lipid membranes, protein correlation functions and lipid ordering
    • Pearson, L. T., J. Edelman, and S. I. Chan. 1984. Statistical mechanics of lipid membranes, protein correlation functions and lipid ordering. Biophys. J. 45:863-871.
    • (1984) Biophys. J , vol.45 , pp. 863-871
    • Pearson, L.T.1    Edelman, J.2    Chan, S.I.3
  • 40
    • 0023409222 scopus 로고
    • Lateral interactions among membrane proteins: Valid estimates based on freeze-fracture electron microscopy
    • Braun, J., J. R. Abney, and J. C. Owicki. 1987. Lateral interactions among membrane proteins: valid estimates based on freeze-fracture electron microscopy. Biophys. J. 52:427-439.
    • (1987) Biophys. J , vol.52 , pp. 427-439
    • Braun, J.1    Abney, J.R.2    Owicki, J.C.3
  • 41
    • 0017304621 scopus 로고
    • Lipid-mediated protein interaction in membranes
    • Marčelja, S. 1976. Lipid-mediated protein interaction in membranes. Biochim. Biophys. Acta. 455:1-7.
    • (1976) Biochim. Biophys. Acta , vol.455 , pp. 1-7
    • Marčelja, S.1
  • 42
    • 0043090491 scopus 로고
    • Theoretical study of protein-lipid interactions in bilayer membranes
    • Owicki, J. C., M. W. Springgate, and H. M. McConnell. 1978. Theoretical study of protein-lipid interactions in bilayer membranes. Proc. Natl. Acad. Sci. USA. 75:1616-1619.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 1616-1619
    • Owicki, J.C.1    Springgate, M.W.2    McConnell, H.M.3
  • 43
    • 0001065811 scopus 로고
    • Theory of protein-lipid and protein-protein interactions in bilayer membranes
    • Owicki, J. C., and H. M. McConnell. 1979. Theory of protein-lipid and protein-protein interactions in bilayer membranes. Proc. Natl. Acad. Sci. USA. 76:4750-4754.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4750-4754
    • Owicki, J.C.1    McConnell, H.M.2
  • 44
    • 0030949158 scopus 로고    scopus 로고
    • Lateral forces acting between particles in liquid films or lipid membranes
    • Kralchevsky, P. A. 1997. Lateral forces acting between particles in liquid films or lipid membranes. Adv. Biophys. 34:25-39.
    • (1997) Adv. Biophys , vol.34 , pp. 25-39
    • Kralchevsky, P.A.1
  • 45
    • 0023018907 scopus 로고
    • Deformation free energy of bilayer membrane and its effect on gramicidin channel lifetime
    • Huang, H. W. 1986. Deformation free energy of bilayer membrane and its effect on gramicidin channel lifetime. Biophys. J. 50:1061-1070.
    • (1986) Biophys. J , vol.50 , pp. 1061-1070
    • Huang, H.W.1
  • 46
    • 0025231220 scopus 로고
    • Calculation of deformation energies and conformations in lipid membranes containing gramicidin channels
    • Helfrich, P., and E. Jakobsson. 1990. Calculation of deformation energies and conformations in lipid membranes containing gramicidin channels. Biophys. J. 57:1075-1084.
    • (1990) Biophys. J , vol.57 , pp. 1075-1084
    • Helfrich, P.1    Jakobsson, E.2
  • 47
    • 84956088383 scopus 로고
    • Long-range forces in heterogeneous fluid membranes
    • Goulian, M., R. Bruinsma, and P. Pincus. 1993. Long-range forces in heterogeneous fluid membranes. Europhys. Lett. 22:145-150.
    • (1993) Europhys. Lett , vol.22 , pp. 145-150
    • Goulian, M.1    Bruinsma, R.2    Pincus, P.3
  • 50
    • 0021474573 scopus 로고
    • Mattress model of lipid-protein interactions in membranes
    • Mouritsen, O. G., and M. Bloom. 1984. Mattress model of lipid-protein interactions in membranes. Biophys. J. 46:141-153.
    • (1984) Biophys. J , vol.46 , pp. 141-153
    • Mouritsen, O.G.1    Bloom, M.2
  • 51
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian, J. 1998. Hydrophobic mismatch between proteins and lipids in membranes. Biochim. Biophys. Acta. 1376:401-416.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 401-416
    • Killian, J.1
  • 52
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee, A. 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.1
  • 55
    • 0034118188 scopus 로고    scopus 로고
    • Continuum solvent model calculations of alamethicin-membrane interactions: Thermodynamic aspects
    • Kessel, A., D. S. Cafiso, and N. Ben-Tal. 2000. Continuum solvent model calculations of alamethicin-membrane interactions: thermodynamic aspects. Biophys. J. 78:571-583.
    • (2000) Biophys. J , vol.78 , pp. 571-583
    • Kessel, A.1    Cafiso, D.S.2    Ben-Tal, N.3
  • 56
    • 0020360086 scopus 로고
    • A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution
    • Fox, R. O., Jr., and F. M. Richards. 1982. A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution. Nature. 300:325-330.
    • (1982) Nature , vol.300 , pp. 325-330
    • Fox Jr., R.O.1    Richards, F.M.2
  • 57
    • 0031001316 scopus 로고    scopus 로고
    • Alamethicin channels - modeling via restrained molecular dynamics simulations
    • Breed, J., P. C. Biggin, I. D. Kerr, O. S. Smart, and M. S. P. Sansom. 1997. Alamethicin channels - modeling via restrained molecular dynamics simulations. Biochim. Biophys. Acta. 1325:235-249.
    • (1997) Biochim. Biophys. Acta , vol.1325 , pp. 235-249
    • Breed, J.1    Biggin, P.C.2    Kerr, I.D.3    Smart, O.S.4    Sansom, M.S.P.5
  • 58
    • 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., B. Smit, and M. M. Sperotto. 2005. Simulation studies of protein-induced bilayer deformations, and lipid-induced protein tilting, on a mesoscopic model for lipid bilayers with embedded proteins. Biophys. J. 88:1778-1798.
    • (2005) Biophys. J , vol.88 , pp. 1778-1798
    • Venturoli, M.1    Smit, B.2    Sperotto, M.M.3
  • 59
    • 0031895461 scopus 로고    scopus 로고
    • Energetics of inclusion-induced bilayer deformations
    • Nielsen, C., M. Goulian, and O. S. Andersen. 1998. Energetics of inclusion-induced bilayer deformations. Biophys. J. 74:1966-1983.
    • (1998) Biophys. J , vol.74 , pp. 1966-1983
    • Nielsen, C.1    Goulian, M.2    Andersen, O.S.3
  • 60
    • 0342601426 scopus 로고    scopus 로고
    • Protein attraction in membranes induced by lipid fluctuations
    • Sintes, T., and A. Baumgärtner. 1997. Protein attraction in membranes induced by lipid fluctuations. Biophys. J. 73:2251-2259.
    • (1997) Biophys. J , vol.73 , pp. 2251-2259
    • Sintes, T.1    Baumgärtner, A.2
  • 61
    • 0034667495 scopus 로고    scopus 로고
    • A molecular model for lipid-mediated interaction between proteins in membranes
    • May, S., and A. Ben-Shaul. 2000. A molecular model for lipid-mediated interaction between proteins in membranes. Phys. Chem. Chem. Phys. 2:4494-4502.
    • (2000) Phys. Chem. Chem. Phys , vol.2 , pp. 4494-4502
    • May, S.1    Ben-Shaul, A.2
  • 62
    • 0031268384 scopus 로고    scopus 로고
    • Computer simulation of a DPPC phospholipid bilayer: Structural changes as a function of molecular surface area
    • Feller, S. E., R. M. Venable, and R. W. Pastor. 1997. Computer simulation of a DPPC phospholipid bilayer: structural changes as a function of molecular surface area. Langmuir. 13:6555-6561.
    • (1997) Langmuir , vol.13 , pp. 6555-6561
    • Feller, S.E.1    Venable, R.M.2    Pastor, R.W.3
  • 63
    • 0033030953 scopus 로고    scopus 로고
    • Toward a realistic theory of the interaction of membrane inclusions
    • Marčelja, S. 1999. Toward a realistic theory of the interaction of membrane inclusions. Biophys. J. 76:593-594.
    • (1999) Biophys. J , vol.76 , pp. 593-594
    • Marčelja, S.1
  • 64
    • 0142211230 scopus 로고    scopus 로고
    • Interaction between two cylindrical inclusions in a symmetric lipid bilayer
    • Bohinc, K., V. Kralj-Igliè, and S. May. 2003. Interaction between two cylindrical inclusions in a symmetric lipid bilayer. J. Chem. Phys. 119:7435-7444.
    • (2003) J. Chem. Phys , vol.119 , pp. 7435-7444
    • Bohinc, K.1    Kralj-Igliè, V.2    May, S.3
  • 65
    • 0141427367 scopus 로고
    • Mode expansion in equilibrium statistical mechanics. I. General theory and application to the classical electron gas
    • Andersen, H. C., and D. Chandler. 1970. Mode expansion in equilibrium statistical mechanics. I. General theory and application to the classical electron gas. J. Chem. Phys. 53:547-554.
    • (1970) J. Chem. Phys , vol.53 , pp. 547-554
    • Andersen, H.C.1    Chandler, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.