메뉴 건너뛰기




Volumn 1667, Issue 1, 2004, Pages 26-37

Influence of the lipid composition on the kinetics of concerted insertion and folding of melittin in bilayers

Author keywords

Circular dichroism; Fluorescence; Folding; Kinetics; Lipid membrane; Melittin

Indexed keywords

BEE VENOM; BROMINE; CHOLESTEROL; GLYCEROPHOSPHOLIPID; LIPID; MELITTIN; PEPTIDE; PHOSPHORYLCHOLINE; TRYPTOPHAN;

EID: 7744240086     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2004.08.012     Document Type: Article
Times cited : (52)

References (71)
  • 1
    • 0015527253 scopus 로고
    • Bee and wasp venoms
    • E. Habermann Bee and wasp venoms Science 177 1972 314 322
    • (1972) Science , vol.177 , pp. 314-322
    • Habermann, E.1
  • 2
    • 0025217893 scopus 로고
    • The actions of melittin on membranes
    • C.E. Dempsey The actions of melittin on membranes Biochim. Biophys. Acta 1031 1990 143 161
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 143-161
    • Dempsey, C.E.1
  • 3
    • 0020025608 scopus 로고
    • Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue
    • W.F. DeGrado, G.F. Musso, M. Lieber, E.T. Kaiser, and F.J. Kézdy Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue Biophys. J. 37 1982 329 338
    • (1982) Biophys. J. , vol.37 , pp. 329-338
    • Degrado, W.F.1    Musso, G.F.2    Lieber, M.3    Kaiser, E.T.4    Kézdy, F.J.5
  • 5
    • 0030790179 scopus 로고    scopus 로고
    • Pore formation and translocation of melittin
    • K. Matsuzaki, S. Yoneyama, and K. Miyajima Pore formation and translocation of melittin Biophys. J. 73 1997 831 838
    • (1997) Biophys. J. , vol.73 , pp. 831-838
    • Matsuzaki, K.1    Yoneyama, S.2    Miyajima, K.3
  • 6
    • 0029042292 scopus 로고
    • Study of vesicle leakage induced by melittin
    • T. Benachir, and M. Lafleur Study of vesicle leakage induced by melittin Biochim. Biophys. Acta 1235 1995 452 460
    • (1995) Biochim. Biophys. Acta , vol.1235 , pp. 452-460
    • Benachir, T.1    Lafleur, M.2
  • 7
    • 0031027375 scopus 로고    scopus 로고
    • Melittin-induced leakage from phosphatidylcholine vesicles is modulated by cholesterol: A property used for membrane targeting
    • T. Benachir, M. Monette, J. Grenier, and M. Lafleur Melittin-induced leakage from phosphatidylcholine vesicles is modulated by cholesterol: a property used for membrane targeting Eur. Biophys. J. 25 1997 201 210
    • (1997) Eur. Biophys. J. , vol.25 , pp. 201-210
    • Benachir, T.1    Monette, M.2    Grenier, J.3    Lafleur, M.4
  • 8
    • 0037417761 scopus 로고    scopus 로고
    • Lipopolysaccharides in bacterial membranes act like cholesterol in eukaryotic plasma membranes in providing protection against melittin-induced bilayer lysis
    • D. Allende, and T.J. McIntosh Lipopolysaccharides in bacterial membranes act like cholesterol in eukaryotic plasma membranes in providing protection against melittin-induced bilayer lysis Biochemistry 42 2003 1101 1108
    • (2003) Biochemistry , vol.42 , pp. 1101-1108
    • Allende, D.1    McIntosh, T.J.2
  • 10
    • 0037687909 scopus 로고    scopus 로고
    • Effects of sphingomyelin on melittin pore formation
    • M.J. Gómara, S. Nir, and J.L. Nieva Effects of sphingomyelin on melittin pore formation Biochim. Biophys. Acta 1612 2003 83 89
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 83-89
    • Gómara, M.J.1    Nir, S.2    Nieva, J.L.3
  • 11
    • 0025243640 scopus 로고
    • Leakage of internal markers from erythrocytes and lipid vesicles induced by melittin, gramicidin S and alamethicin: A comparative study
    • S.H. Portlock, M.J. Clague, and R.J. Cherry Leakage of internal markers from erythrocytes and lipid vesicles induced by melittin, gramicidin S and alamethicin: a comparative study Biochim. Biophys. Acta 1030 1990 1 10
    • (1990) Biochim. Biophys. Acta , vol.1030 , pp. 1-10
    • Portlock, S.H.1    Clague, M.J.2    Cherry, R.J.3
  • 12
    • 0030704248 scopus 로고    scopus 로고
    • Modulation of tryptophan environment in membrane-bound melittin by negatively charged phospholipids: Implications in membrane organization and function
    • A.K. Ghosh, R. Rukmini, and A. Chattopadhyay Modulation of tryptophan environment in membrane-bound melittin by negatively charged phospholipids: implications in membrane organization and function Biochemistry 36 1997 14291 14305
    • (1997) Biochemistry , vol.36 , pp. 14291-14305
    • Ghosh, A.K.1    Rukmini, R.2    Chattopadhyay, A.3
  • 13
    • 0025128695 scopus 로고
    • 2H nuclear magnetic resonance and differential scanning calorimetry
    • 2H nuclear magnetic resonance and differential scanning calorimetry Biochemistry 29 1990 451 464
    • (1990) Biochemistry , vol.29 , pp. 451-464
    • Vist, M.R.1    Davis, J.H.2
  • 14
    • 0026700004 scopus 로고
    • Phosphatidylcholine: Cholesterol phase diagrams
    • J.L. Thewalt, and M. Bloom Phosphatidylcholine: cholesterol phase diagrams Biophys. J. 63 1992 1176 1181
    • (1992) Biophys. J. , vol.63 , pp. 1176-1181
    • Thewalt, J.L.1    Bloom, M.2
  • 15
    • 0032922797 scopus 로고    scopus 로고
    • Calorimetric and spectroscopic studies of the effects of cholesterol on the thermotropic phase behavior and organization of a homologous series of linear saturated phosphatidylethanolamine bilayers
    • T.P.W. McMullen, R.N.A.H. Lewis, and R.N. McElhaney Calorimetric and spectroscopic studies of the effects of cholesterol on the thermotropic phase behavior and organization of a homologous series of linear saturated phosphatidylethanolamine bilayers Biochim. Biophys. Acta 1416 1999 119 134
    • (1999) Biochim. Biophys. Acta , vol.1416 , pp. 119-134
    • McMullen, T.P.W.1    Lewis, R.N.A.H.2    McElhaney, R.N.3
  • 16
    • 0037274943 scopus 로고    scopus 로고
    • Bilayer interfacial properties modulate the binding of amphipathic peptides
    • D. Allende, A. Vidal, S.A. Simon, and T.J. McIntosh Bilayer interfacial properties modulate the binding of amphipathic peptides Chem. Phys. Lipids 122 2003 65 76
    • (2003) Chem. Phys. Lipids , vol.122 , pp. 65-76
    • Allende, D.1    Vidal, A.2    Simon, S.A.3    McIntosh, T.J.4
  • 17
    • 0035479424 scopus 로고    scopus 로고
    • 'Detergent-like' permeabilization of anionic lipid vesicles by melittin
    • A.S. Ladokhin, and S.H. White 'Detergent-like' permeabilization of anionic lipid vesicles by melittin Biochim. Biophys. Acta 1514 2001 253 260
    • (2001) Biochim. Biophys. Acta , vol.1514 , pp. 253-260
    • Ladokhin, A.S.1    White, S.H.2
  • 18
    • 0020079526 scopus 로고
    • The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities
    • T.C. Terwilliger, L. Weissman, and D. Eisenberg The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities Biophys. J. 37 1982 353 361
    • (1982) Biophys. J. , vol.37 , pp. 353-361
    • Terwilliger, T.C.1    Weissman, L.2    Eisenberg, D.3
  • 19
    • 0033613815 scopus 로고    scopus 로고
    • Folding of amphipathic α-helices on membranes: Energetics of helix formation by melittin
    • A.S. Ladokhin, and S.H. White Folding of amphipathic α-helices on membranes: energetics of helix formation by melittin J. Mol. Biol. 285 1999 1363 1369
    • (1999) J. Mol. Biol. , vol.285 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 20
    • 0019934717 scopus 로고
    • The helical hydrophobic moment: A measure of the amphiphilicity of a helix
    • D. Eisenberg, R.M. Weiss, and T.C. Terwilliger The helical hydrophobic moment: a measure of the amphiphilicity of a helix Nature 299 1982 371 374
    • (1982) Nature , vol.299 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 21
    • 0024963567 scopus 로고
    • Signal sequences
    • L.M. Gierasch Signal sequences Biochemistry 28 1989 923 930
    • (1989) Biochemistry , vol.28 , pp. 923-930
    • Gierasch, L.M.1
  • 22
    • 0022835408 scopus 로고
    • Structural analysis and amphiphilic properties of a chemically synthesized mitochondrial signal peptide
    • R.M. Epand, S.-W. Hui, C. Argan, L.L. Gillespie, and G.C. Shore Structural analysis and amphiphilic properties of a chemically synthesized mitochondrial signal peptide J. Biol. Chem. 261 1986 10017 10020
    • (1986) J. Biol. Chem. , vol.261 , pp. 10017-10020
    • Epand, R.M.1    Hui, S.-W.2    Argan, C.3    Gillespie, L.L.4    Shore, G.C.5
  • 23
    • 0023030922 scopus 로고
    • Membrane damage by hemolytic viruses, toxins, complement, and other cytotoxic agents. A common mechanism blocked by divalent cations
    • C.L. Bashford, G.M. Alder, G. Menestrina, K.J. Micklem, J.J. Murphy, and C.A. Pasternak Membrane damage by hemolytic viruses, toxins, complement, and other cytotoxic agents. A common mechanism blocked by divalent cations J. Biol. Chem. 261 1986 9300 9308
    • (1986) J. Biol. Chem. , vol.261 , pp. 9300-9308
    • Bashford, C.L.1    Alder, G.M.2    Menestrina, G.3    Micklem, K.J.4    Murphy, J.J.5    Pasternak, C.A.6
  • 24
    • 0023762882 scopus 로고
    • Comparison between complement and melittin hemolysis: Anti-melittin antibodies inhibit complement lysis
    • R.O. Laine, B.P. Morgan, and A.F. Esser Comparison between complement and melittin hemolysis: anti-melittin antibodies inhibit complement lysis Biochemistry 27 1988 5308 5314
    • (1988) Biochemistry , vol.27 , pp. 5308-5314
    • Laine, R.O.1    Morgan, B.P.2    Esser, A.F.3
  • 25
    • 17644432782 scopus 로고    scopus 로고
    • An amphipathic α-helical synthetic peptide analogue of melittin inhibits herpes simplex virus-1 (HSV-1)-induced cell fusion and virus spread
    • A. Baghian, J. Jaynes, F. Enright, and K.G. Kousoulas An amphipathic α-helical synthetic peptide analogue of melittin inhibits herpes simplex virus-1 (HSV-1)-induced cell fusion and virus spread Peptides 18 1997 177 183
    • (1997) Peptides , vol.18 , pp. 177-183
    • Baghian, A.1    Jaynes, J.2    Enright, F.3    Kousoulas, K.G.4
  • 26
    • 0031024551 scopus 로고    scopus 로고
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: Structure-function study
    • Z. Oren, and Y. Shai Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study Biochemistry 36 1997 1826 1835
    • (1997) Biochemistry , vol.36 , pp. 1826-1835
    • Oren, Z.1    Shai, Y.2
  • 29
    • 0026737184 scopus 로고
    • Kinetics of melittin induced pore formation in the membrane of lipid vesicles
    • G. Schwarz, R. Zong, and T. Popescu Kinetics of melittin induced pore formation in the membrane of lipid vesicles Biochim. Biophys. Acta 1110 1992 97 104
    • (1992) Biochim. Biophys. Acta , vol.1110 , pp. 97-104
    • Schwarz, G.1    Zong, R.2    Popescu, T.3
  • 30
    • 0032562219 scopus 로고    scopus 로고
    • Quantitative studies on the melittin-induced leakage mechanism of lipid vesicles
    • S. Rex, and G. Schwarz Quantitative studies on the melittin-induced leakage mechanism of lipid vesicles Biochemistry 37 1998 2336 2345
    • (1998) Biochemistry , vol.37 , pp. 2336-2345
    • Rex, S.1    Schwarz, G.2
  • 31
    • 0026099161 scopus 로고
    • Kinetics of melittin binding to phospholipid small unilamellar vesicles
    • K.M. Sekharam, T.D. Badrick, and S. Georghiou Kinetics of melittin binding to phospholipid small unilamellar vesicles Biochim. Biophys. Acta 1063 1991 171 174
    • (1991) Biochim. Biophys. Acta , vol.1063 , pp. 171-174
    • Sekharam, K.M.1    Badrick, T.D.2    Georghiou, S.3
  • 32
    • 0028784395 scopus 로고
    • Stopped-flow fluorometric study of the interaction of melittin with phospholipid bilayers: Importance of the physical state of the bilayer and the acyl chain length
    • T.D. Badrick, A. Philippetis, and S. Georghiou Stopped-flow fluorometric study of the interaction of melittin with phospholipid bilayers: importance of the physical state of the bilayer and the acyl chain length Biophys. J. 69 1995 1999 2010
    • (1995) Biophys. J. , vol.69 , pp. 1999-2010
    • Badrick, T.D.1    Philippetis, A.2    Georghiou, S.3
  • 33
    • 0032467144 scopus 로고    scopus 로고
    • Amino acid sequences which promote and prevent the binding and membrane insertion of surface-active peptide: Comparison of melittin and promelittin
    • C. Wolfe, J. Cladera, and P. O'Shea Amino acid sequences which promote and prevent the binding and membrane insertion of surface-active peptide: comparison of melittin and promelittin Mol. Membr. Biol. 15 1998 221 227
    • (1998) Mol. Membr. Biol. , vol.15 , pp. 221-227
    • Wolfe, C.1    Cladera, J.2    O'Shea, P.3
  • 34
    • 0037457824 scopus 로고    scopus 로고
    • Exploring peptide membrane interaction using surface plasmon resonance: Differentiation between pore formation versus membrane disruption by lytic peptides
    • N. Papo, and Y. Shai Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides Biochemistry 42 2003 458 466
    • (2003) Biochemistry , vol.42 , pp. 458-466
    • Papo, N.1    Shai, Y.2
  • 35
    • 0018483723 scopus 로고
    • Conformational change and self association of monomeric melittin
    • J.C. Talbot, J. Dufourcq, J. DeBony, J.F. Faucon, and C. Lussan Conformational change and self association of monomeric melittin FEBS Lett. 102 1979 191 193
    • (1979) FEBS Lett. , vol.102 , pp. 191-193
    • Talbot, J.C.1    Dufourcq, J.2    Debony, J.3    Faucon, J.F.4    Lussan, C.5
  • 36
    • 0023192005 scopus 로고
    • Lipid specific penetration of melittin into phospholipid model membranes
    • A.M. Batenburg, J.C.L. Hibbeln, and B. de Kruijff Lipid specific penetration of melittin into phospholipid model membranes Biochim. Biophys. Acta 903 1987 155 165
    • (1987) Biochim. Biophys. Acta , vol.903 , pp. 155-165
    • Batenburg, A.M.1    Hibbeln, J.C.L.2    De Kruijff, B.3
  • 37
    • 0017377209 scopus 로고
    • Intrinsic fluorescence study of lipid-protein interactions in membrane models. Binding of melittin, an amphipathic peptide, to phospholipid vesicles
    • J. Dufourcq, and J.-F. Faucon Intrinsic fluorescence study of lipid-protein interactions in membrane models. Binding of melittin, an amphipathic peptide, to phospholipid vesicles Biochim. Biophys. Acta 467 1977 1 11
    • (1977) Biochim. Biophys. Acta , vol.467 , pp. 1-11
    • Dufourcq, J.1    Faucon, J.-F.2
  • 39
    • 0031005647 scopus 로고    scopus 로고
    • Distribution analysis of depth-dependent fluorescence quenching in membranes: A practical guide
    • A.S. Ladokhin Distribution analysis of depth-dependent fluorescence quenching in membranes: a practical guide Methods Enzymol. 278 1997 462 473
    • (1997) Methods Enzymol. , vol.278 , pp. 462-473
    • Ladokhin, A.S.1
  • 40
    • 0025051457 scopus 로고
    • Quenching of tryptophan fluorescence by brominated phospholipid
    • E.J. Bolen, and P.W. Holloway Quenching of tryptophan fluorescence by brominated phospholipid Biochemistry 29 1990 9638 9643
    • (1990) Biochemistry , vol.29 , pp. 9638-9643
    • Bolen, E.J.1    Holloway, P.W.2
  • 41
    • 0022798958 scopus 로고
    • The structure of melittin in membranes
    • H. Vogel, and F. Jähnig The structure of melittin in membranes Biophys. J. 50 1986 573 582
    • (1986) Biophys. J. , vol.50 , pp. 573-582
    • Vogel, H.1    Jähnig, F.2
  • 42
    • 0036467406 scopus 로고    scopus 로고
    • The presence of PEG-lipids in liposomes does not reduce melittin binding but decreases melittin-induced leakage
    • S. Rex, J. Bian, J.R. Silvius, and M. Lafleur The presence of PEG-lipids in liposomes does not reduce melittin binding but decreases melittin-induced leakage Biochim. Biophys. Acta 1558 2002 211 221
    • (2002) Biochim. Biophys. Acta , vol.1558 , pp. 211-221
    • Rex, S.1    Bian, J.2    Silvius, J.R.3    Lafleur, M.4
  • 43
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • C.H. Fiske, and Y. Subbarow The colorimetric determination of phosphorus J. Biol. Chem. 66 1925 375 400
    • (1925) J. Biol. Chem. , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 44
    • 0022516431 scopus 로고
    • Morphological changes of phosphatidylcholine bilayers induced by melittin: Vesicularization, fusion, discoidal particles
    • J. Dufourcq, J.-F. Faucon, G. Fourche, J.-L. Dasseux, M. Le Maire, and T. Gulik-Krzywicki Morphological changes of phosphatidylcholine bilayers induced by melittin: vesicularization, fusion, discoidal particles Biochim. Biophys. Acta 859 1986 33 48
    • (1986) Biochim. Biophys. Acta , vol.859 , pp. 33-48
    • Dufourcq, J.1    Faucon, J.-F.2    Fourche, G.3    Dasseux, J.-L.4    Le Maire, M.5    Gulik-Krzywicki, T.6
  • 45
    • 0034667871 scopus 로고    scopus 로고
    • How to measure and analyze tryptophan florescence in membranes properly, and why bother?
    • A.S. Ladokhin, S. Jayasinghe, and S.H. White How to measure and analyze tryptophan florescence in membranes properly, and why bother? Anal. Biochem. 285 2000 235 245
    • (2000) Anal. Biochem. , vol.285 , pp. 235-245
    • Ladokhin, A.S.1    Jayasinghe, S.2    White, S.H.3
  • 46
    • 0030874298 scopus 로고    scopus 로고
    • Comparison of NH exchange and circular dichroism as techniques for measuring the parameters of the helix-coil transition in peptides
    • C.A. Rohl, and R.L. Baldwin Comparison of NH exchange and circular dichroism as techniques for measuring the parameters of the helix-coil transition in peptides Biochemistry 36 1997 8435 8442
    • (1997) Biochemistry , vol.36 , pp. 8435-8442
    • Rohl, C.A.1    Baldwin, R.L.2
  • 47
    • 0023626564 scopus 로고
    • Interaction of melittin with negatively charged phospholipids: Consequences for lipid organisation
    • A.M. Batenburg, J.H. van Esch, J. Leunissen-Bijvelt, A.J. Verkleij, and B. de Kruijff Interaction of melittin with negatively charged phospholipids: consequences for lipid organisation FEBS Lett. 223 1987 148 154
    • (1987) FEBS Lett. , vol.223 , pp. 148-154
    • Batenburg, A.M.1    Van Esch, J.H.2    Leunissen-Bijvelt, J.3    Verkleij, A.J.4    De Kruijff, B.5
  • 49
    • 0034635171 scopus 로고    scopus 로고
    • Determining the membrane topology of peptides by fluorescence quenching
    • W.C. Wimley, and S.H. White Determining the membrane topology of peptides by fluorescence quenching Biochemistry 39 2000 161 170
    • (2000) Biochemistry , vol.39 , pp. 161-170
    • Wimley, W.C.1    White, S.H.2
  • 50
    • 0018487558 scopus 로고
    • The self-association of melittin and its binding to lipids-an intrinsic fluorescence polarization study
    • J.F. Faucon, J. Dufourcq, and C. Lussan The self-association of melittin and its binding to lipids-an intrinsic fluorescence polarization study FEBS Lett. 102 1979 187 190
    • (1979) FEBS Lett. , vol.102 , pp. 187-190
    • Faucon, J.F.1    Dufourcq, J.2    Lussan, C.3
  • 51
    • 0024591992 scopus 로고
    • Thermodynamic and kinetic studies on the association of melittin with a phospholipid bilayer
    • G. Schwartz, and G. Beschiaschvili Thermodynamic and kinetic studies on the association of melittin with a phospholipid bilayer Biochim. Biophys. Acta 979 1989 82 90
    • (1989) Biochim. Biophys. Acta , vol.979 , pp. 82-90
    • Schwartz, G.1    Beschiaschvili, G.2
  • 52
    • 0026470007 scopus 로고
    • Charge repulsion in the conformational stability of melittin
    • Y. Hagihara, M. Kataoka, S. Aimoto, and Y. Goto Charge repulsion in the conformational stability of melittin Biochemistry 31 1992 11908 11914
    • (1992) Biochemistry , vol.31 , pp. 11908-11914
    • Hagihara, Y.1    Kataoka, M.2    Aimoto, S.3    Goto, Y.4
  • 53
    • 0019871670 scopus 로고
    • Incorporation of melittin into phosphatidylcholine bilayers
    • H. Vogel Incorporation of melittin into phosphatidylcholine bilayers FEBS Lett. 134 1981 37 42
    • (1981) FEBS Lett. , vol.134 , pp. 37-42
    • Vogel, H.1
  • 54
    • 0018784022 scopus 로고
    • The structure of melittin in lipid bilayer membranes
    • A.F. Drake, and R.C. Hider The structure of melittin in lipid bilayer membranes Biochim. Biophys. Acta 555 1979 371 373
    • (1979) Biochim. Biophys. Acta , vol.555 , pp. 371-373
    • Drake, A.F.1    Hider, R.C.2
  • 55
    • 0023111150 scopus 로고
    • Determination of depth of bromine atoms in bilayers formed from bromolipid probes
    • T.J. McIntosh, and P.W. Holloway Determination of depth of bromine atoms in bilayers formed from bromolipid probes Biochemistry 26 1987 1783 1788
    • (1987) Biochemistry , vol.26 , pp. 1783-1788
    • McIntosh, T.J.1    Holloway, P.W.2
  • 56
    • 0033032331 scopus 로고    scopus 로고
    • Analysis of protein and peptide penetration into membranes by depth-dependent fluorescence quenching: Theoretical considerations
    • A.S. Ladokhin Analysis of protein and peptide penetration into membranes by depth-dependent fluorescence quenching: theoretical considerations Biophys. J. 76 1999 946 955
    • (1999) Biophys. J. , vol.76 , pp. 946-955
    • Ladokhin, A.S.1
  • 57
    • 0024328774 scopus 로고
    • Interaction of melittin with phosphatidylcholine membranes. Binding isotherm and lipid head-group conformation
    • E. Kuchinka, and J. Seelig Interaction of melittin with phosphatidylcholine membranes. Binding isotherm and lipid head-group conformation Biochemistry 28 1989 4216 4221
    • (1989) Biochemistry , vol.28 , pp. 4216-4221
    • Kuchinka, E.1    Seelig, J.2
  • 58
    • 1642359643 scopus 로고    scopus 로고
    • Energetics of pore formation induced by membrane active peptides
    • M.-T. Lee, F.-Y. Chen, and H.W. Huang Energetics of pore formation induced by membrane active peptides Biochemistry 43 2004 3590 3599
    • (2004) Biochemistry , vol.43 , pp. 3590-3599
    • Lee, M.-T.1    Chen, F.-Y.2    Huang, H.W.3
  • 59
    • 0038778549 scopus 로고    scopus 로고
    • Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
    • F.-Y. Chen, M.-T. Lee, and H.W. Huang Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation Biophys. J. 84 2003 3751 3758
    • (2003) Biophys. J. , vol.84 , pp. 3751-3758
    • Chen, F.-Y.1    Lee, M.-T.2    Huang, H.W.3
  • 60
    • 0029764221 scopus 로고    scopus 로고
    • Time resolution of binding and membrane insertion of a mitochondrial signal peptide: Correlation with structural changes and evidence for cooperativity
    • C. Golding, S. Senior, M.T. Wilson, and P. O'Shea Time resolution of binding and membrane insertion of a mitochondrial signal peptide: correlation with structural changes and evidence for cooperativity Biochemistry 35 1996 10931 10937
    • (1996) Biochemistry , vol.35 , pp. 10931-10937
    • Golding, C.1    Senior, S.2    Wilson, M.T.3    O'Shea, P.4
  • 61
    • 0023657247 scopus 로고
    • Attenuated total reflectance Fourier transform infrared studies of the interaction of melittin, two fragments of melittin, and δ-hemolysin with phosphatidylcholines
    • J.W. Brauner, R. Mendelsohn, and F.G. Prendergast Attenuated total reflectance Fourier transform infrared studies of the interaction of melittin, two fragments of melittin, and δ-hemolysin with phosphatidylcholines Biochemistry 26 1987 8151 8158
    • (1987) Biochemistry , vol.26 , pp. 8151-8158
    • Brauner, J.W.1    Mendelsohn, R.2    Prendergast, F.G.3
  • 65
    • 0027240889 scopus 로고
    • Effect of cholesterol on the polymorphism of dipalmitoylphosphatidylcholine/melittin complexes: An NMR study
    • M. Monette, M.-R. Van Calsteren, and M. Lafleur Effect of cholesterol on the polymorphism of dipalmitoylphosphatidylcholine/melittin complexes: an NMR study Biochim. Biophys. Acta 1149 1993 319 328
    • (1993) Biochim. Biophys. Acta , vol.1149 , pp. 319-328
    • Monette, M.1    Van Calsteren, M.-R.2    Lafleur, M.3
  • 67
    • 0032796076 scopus 로고    scopus 로고
    • Characterization of permeability and morphological perturbations induced by nisin on phosphatidylcholine membranes
    • R. El Jastimi, K. Edwards, and M. Lafleur Characterization of permeability and morphological perturbations induced by nisin on phosphatidylcholine membranes Biophys. J. 77 1999 842 852
    • (1999) Biophys. J. , vol.77 , pp. 842-852
    • El Jastimi, R.1    Edwards, K.2    Lafleur, M.3
  • 68
    • 0027313673 scopus 로고
    • Pathways of protein folding
    • C.R. Matthews Pathways of protein folding Ann. Rev. Biochem. 62 1993 653 683
    • (1993) Ann. Rev. Biochem. , vol.62 , pp. 653-683
    • Matthews, C.R.1
  • 70
    • 0031012140 scopus 로고    scopus 로고
    • Slow α helix formation during folding of a membrane protein
    • M.L. Riley, B.A. Wallace, S.L. Flitsch, and P.J. Booth Slow α helix formation during folding of a membrane protein Biochemistry 36 1997 192 196
    • (1997) Biochemistry , vol.36 , pp. 192-196
    • Riley, M.L.1    Wallace, B.A.2    Flitsch, S.L.3    Booth, P.J.4
  • 71
    • 0030942644 scopus 로고    scopus 로고
    • Multiple-domain fluorescence lifetime data analysis
    • M.L. Johnson Multiple-domain fluorescence lifetime data analysis Methods Enzymol. 278 1997 570 583
    • (1997) Methods Enzymol. , vol.278 , pp. 570-583
    • Johnson, M.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.