메뉴 건너뛰기




Volumn 77, Issue 6, 1999, Pages 3120-3133

Membrane lysis by the antibacterial peptides cecropins B1 and B3: A spin-label electron spin resonance study on phospholipid bilayers

Author keywords

[No Author keywords available]

Indexed keywords

CECROPIN B; PHOSPHATIDIC ACID; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID;

EID: 0032806444     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77142-0     Document Type: Article
Times cited : (40)

References (53)
  • 1
    • 0025724956 scopus 로고
    • Interaction with phospholipid bilayers, ion channel formation, and antimicrobial activity of basic amphipathic alpha-helical model peptides of various chain lengths
    • Agawa, Y., S. Lee, S. Ono, H. Aoyagi, M. Ohno, T. Taniguchi, K. Anzai, and Y. Kirino. 1991. Interaction with phospholipid bilayers, ion channel formation, and antimicrobial activity of basic amphipathic alpha-helical model peptides of various chain lengths. J. Biol. Chem. 266: 20218-20222.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20218-20222
    • Agawa, Y.1    Lee, S.2    Ono, S.3    Aoyagi, H.4    Ohno, M.5    Taniguchi, T.6    Anzai, K.7    Kirino, Y.8
  • 2
    • 0024974071 scopus 로고
    • Structural studies on transmembrane proteins. 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines
    • Altenbach, C., S. L. Flitsch, H. G. Khorana, and W. L. Hubbell. 1989. Structural studies on transmembrane proteins. 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines. Biochemistry. 28: 7806-7812.
    • (1989) Biochemistry , vol.28 , pp. 7806-7812
    • Altenbach, C.1    Flitsch, S.L.2    Khorana, H.G.3    Hubbell, W.L.4
  • 3
    • 0025832273 scopus 로고
    • Dynamics and aggregation of the peptide ion channel alamethicin. Measurements using spin-labeled peptides
    • Archer, S. J., J. F. Ellena, and D. S. Cafiso. 1991. Dynamics and aggregation of the peptide ion channel alamethicin. Measurements using spin-labeled peptides. Biophys. J. 60:389-398.
    • (1991) Biophys. J. , vol.60 , pp. 389-398
    • Archer, S.J.1    Ellena, J.F.2    Cafiso, D.S.3
  • 4
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Barlett, G. R. 1959. Phosphorus assay in column chromatography. J. Biol. Chem. 234:466-468.
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Barlett, G.R.1
  • 5
    • 0029768644 scopus 로고    scopus 로고
    • Helix-helix interactions in lipid bilayers
    • Ben-Tal, N., and B. Honig. 1997. Helix-helix interactions in lipid bilayers. Biophys. J. 71:3046-3050.
    • (1997) Biophys. J. , vol.71 , pp. 3046-3050
    • Ben-Tal, N.1    Honig, B.2
  • 6
    • 0030754783 scopus 로고    scopus 로고
    • Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles
    • Ben-Tal, N., B. Honig, C. Miller, and S. Mclaughlin. 1997a. Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles. Biophys. J. 73:1717-1727.
    • (1997) Biophys. J. , vol.73 , pp. 1717-1727
    • Ben-Tal, N.1    Honig, B.2    Miller, C.3    McLaughlin, S.4
  • 7
    • 0029757155 scopus 로고    scopus 로고
    • Binding of small basic peptides to membranes containing acidic lipids: Theoretical models and experimental results
    • Ben-Tal, N., B. Honig, R. M. Peitzsch, G. Denisov, and S. McLaughlin. 1997b. Binding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental results. Biophys. J. 71: 561-575.
    • (1997) Biophys. J. , vol.71 , pp. 561-575
    • Ben-Tal, N.1    Honig, B.2    Peitzsch, R.M.3    Denisov, G.4    McLaughlin, S.5
  • 8
    • 0018783453 scopus 로고
    • Chromium oxalate: A new spin label broadening agent for use with thylakoids
    • Berg, S. P., and D. M. Nesbitt. 1979. Chromium oxalate: a new spin label broadening agent for use with thylakoids. Biochim. Biophys. Acta. 548:608-615.
    • (1979) Biochim. Biophys. Acta , vol.548 , pp. 608-615
    • Berg, S.P.1    Nesbitt, D.M.2
  • 9
    • 0025818448 scopus 로고
    • Antibacterial peptides: Key components needed in immunity
    • Boman, H. G. 1991. Antibacterial peptides: key components needed in immunity. Cell. 65:205-207.
    • (1991) Cell , vol.65 , pp. 205-207
    • Boman, H.G.1
  • 10
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman, H. G. 1995. Peptide antibiotics and their role in innate immunity. Anna. Rev. Immunol. 13:61-92.
    • (1995) Anna. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 11
    • 0017182089 scopus 로고
    • Estimation of membrane surface potential and charge density from the phase equilibrium of a paramagnetic amphiphile
    • Castle, J. D., and W. L. Hubbell. 1976. Estimation of membrane surface potential and charge density from the phase equilibrium of a paramagnetic amphiphile. Biochemistry. 15:4818-4831.
    • (1976) Biochemistry , vol.15 , pp. 4818-4831
    • Castle, J.D.1    Hubbell, W.L.2
  • 12
    • 0030746525 scopus 로고    scopus 로고
    • Effects of the anti-bacterial peptide cecropin B and its analogs, cecropins B-1 and B-2, on liposomes, bacteria, and cancer cells
    • Chen, H. M., W. Wang, D. Smith, and S. C. Chan. 1997. Effects of the anti-bacterial peptide cecropin B and its analogs, cecropins B-1 and B-2, on liposomes, bacteria, and cancer cells. Biochim. Biophys. Acta. 1336: 171-179.
    • (1997) Biochim. Biophys. Acta , vol.1336 , pp. 171-179
    • Chen, H.M.1    Wang, W.2    Smith, D.3    Chan, S.C.4
  • 13
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • Christensen, B., J. Fink, R. B. Merrifield, and D. Mauzerall. 1988. Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc. Natl. Acad. Sci. USA. 85:5072-5076.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 14
    • 0027249384 scopus 로고
    • Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in micrococcus luteus
    • Cociancich, S., A. Ghazi, C. Hetru, J. A. Hoffmann, and L. Letellier. 1993. Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in micrococcus luteus. J. Biol. Chem. 268: 19239-19245.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19239-19245
    • Cociancich, S.1    Ghazi, A.2    Hetru, C.3    Hoffmann, J.A.4    Letellier, L.5
  • 15
    • 0025860280 scopus 로고
    • Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation
    • Cruciani, R. A., J. L. Barker, M. Zasloff, H.-C. Chen, and O. Colamonici. 1991. Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation. Proc. Natl. Acad. Sci. USA. 88: 3792-3796.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3792-3796
    • Cruciani, R.A.1    Barker, J.L.2    Zasloff, M.3    Chen, H.-C.4    Colamonici, O.5
  • 16
    • 0025238719 scopus 로고
    • ESR of spin-labeled bacteriophage M13 coat protein in mixed phospholipid bilayers
    • Dejongh, H. H., M. A. Hemminga, and D. Marsh. ESR of spin-labeled bacteriophage M13 coat protein in mixed phospholipid bilayers. 1990. Biochim. Biophys. Acta. 1024:82-88.
    • (1990) Biochim. Biophys. Acta , vol.1024 , pp. 82-88
    • Dejongh, H.H.1    Hemminga, M.A.2    Marsh, D.3
  • 18
    • 0029111532 scopus 로고
    • Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles
    • Gazit, E., A. Boman, H. G. Boman, and L. Shai. 1995. Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles. Biochemistry. 34:11470-11488.
    • (1995) Biochemistry , vol.34 , pp. 11470-11488
    • Gazit, E.1    Boman, A.2    Boman, H.G.3    Shai, L.4
  • 19
    • 0027488790 scopus 로고
    • An electron spin resonance study of interactions between gramicidin A' and phosphatidylcholine bilayers
    • Ge, M., and J. H. Freed. 1993. An electron spin resonance study of interactions between gramicidin A' and phosphatidylcholine bilayers. Biophys. J. 65:2106-2123.
    • (1993) Biophys. J. , vol.65 , pp. 2106-2123
    • Ge, M.1    Freed, J.H.2
  • 20
    • 0023712129 scopus 로고
    • The solution conformation of the antibacterial peptide cecropin A: A nuclear magnetic resonance and dynamical simulated annealing study
    • Holak, T. A., A. Engstrom, P. J. Kraulis, G. Lindeberg, H. Bennich, T. A. Jones, A. M. Gronenborn, and G. M. Clore. 1988. The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study. Biochemistry. 27: 7620-7629.
    • (1988) Biochemistry , vol.27 , pp. 7620-7629
    • Holak, T.A.1    Engstrom, A.2    Kraulis, P.J.3    Lindeberg, G.4    Bennich, H.5    Jones, T.A.6    Gronenborn, A.M.7    Clore, G.M.8
  • 21
    • 0030827974 scopus 로고    scopus 로고
    • Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins
    • Hristova, K., M. E. Selsted, and S. H. White. 1997. Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins. J. Biol. Chem. 272:24224-24233.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24224-24233
    • Hristova, K.1    Selsted, M.E.2    White, S.H.3
  • 22
    • 0027318549 scopus 로고
    • Immune reactions in Drosophila and other insects: A model for innate immunity
    • Hultmark, D. 1993. Immune reactions in Drosophila and other insects: a model for innate immunity. Trends Genet. 9:78-183.
    • (1993) Trends Genet , vol.9 , pp. 78-183
    • Hultmark, D.1
  • 23
    • 0018820115 scopus 로고
    • Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia
    • Hultmark, D., H. Steiner, T. Rasmuson, and H. G. Boman. 1980. Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia. Eur. J. Biochem. 106:7-16.
    • (1980) Eur. J. Biochem. , vol.106 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmuson, T.3    Boman, H.G.4
  • 24
    • 0024619711 scopus 로고
    • In vitro cytocidal effect of lytic peptides on several transformed mammalian cell lines
    • Jaynes, J. M., G. R. Julian, G. W. Jeffers, K. L. White, and F. M. Enright. 1989. In vitro cytocidal effect of lytic peptides on several transformed mammalian cell lines. Pept. Res. 2:157-160.
    • (1989) Pept. Res. , vol.2 , pp. 157-160
    • Jaynes, J.M.1    Julian, G.R.2    Jeffers, G.W.3    White, K.L.4    Enright, F.M.5
  • 25
    • 0015223127 scopus 로고
    • Lipid spin labels in lecithin multilayers. A study of motion along fatty acid chains
    • Jost, P. C., L. J. Libertini, V. C. Hebert, and O. H. Griffith. 1971. Lipid spin labels in lecithin multilayers. A study of motion along fatty acid chains. J. Mol. Biol. 59:77-98.
    • (1971) J. Mol. Biol. , vol.59 , pp. 77-98
    • Jost, P.C.1    Libertini, L.J.2    Hebert, V.C.3    Griffith, O.H.4
  • 26
    • 0025021992 scopus 로고
    • Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes
    • Kagan, B. L., M. E. Selsted, T. Ganz., and R. I. Lehrer. 1990. Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes. Proc. Natl. Acad. Sci. USA. 87: 210-214.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 210-214
    • Kagan, B.L.1    Selsted, M.E.2    Ganz, T.3    Lehrer, R.I.4
  • 27
    • 0014822895 scopus 로고
    • Spin-labeled Neurospora mitochondria
    • Keith, A., G. Bulfield, and W. Snipes. 1970. Spin-labeled Neurospora mitochondria. Biophys. J. 10:618-629.
    • (1970) Biophys. J. , vol.10 , pp. 618-629
    • Keith, A.1    Bulfield, G.2    Snipes, W.3
  • 28
    • 0025914405 scopus 로고
    • Binding of peptides with basic residues to membranes containing acidic phospholipids
    • Kim, J., M. Mosior, L. A. Chung, H. Wu, and S. McLaughlin. 1991. Binding of peptides with basic residues to membranes containing acidic phospholipids. Biophys. J. 60:135-148.
    • (1991) Biophys. J. , vol.60 , pp. 135-148
    • Kim, J.1    Mosior, M.2    Chung, L.A.3    Wu, H.4    McLaughlin, S.5
  • 29
    • 0031030031 scopus 로고    scopus 로고
    • Interaction of bee venom melittin with zwitterionic and negatively charged phospholipid bilayers: A spin-label electron spin resonance study
    • Kleinschmidt, J. H., J. E. Mahaney, D. D. Thomas, and D. Marsh. 1997. Interaction of bee venom melittin with zwitterionic and negatively charged phospholipid bilayers: a spin-label electron spin resonance study. Biophys. J. 72:767-778.
    • (1997) Biophys. J. , vol.72 , pp. 767-778
    • Kleinschmidt, J.H.1    Mahaney, J.E.2    Thomas, D.D.3    Marsh, D.4
  • 31
    • 0003765930 scopus 로고
    • P. C. Jost and O. H. Griffith, editors. John Wiley, New York
    • Marsh, D., and A. Watts. 1981. Lipid-Protein Interactions. 2. P. C. Jost and O. H. Griffith, editors. John Wiley, New York.
    • (1981) Lipid-protein Interactions , vol.2
    • Marsh, D.1    Watts, A.2
  • 33
    • 0027435124 scopus 로고
    • Aggregation state of spin-labeled cecropin AD in solution
    • Mchaourab, H. S., J. S. Hyde, and J. B. Feix. 1993. Aggregation state of spin-labeled cecropin AD in solution. Biochemistry. 32:11895-11902.
    • (1993) Biochemistry , vol.32 , pp. 11895-11902
    • McHaourab, H.S.1    Hyde, J.S.2    Feix, J.B.3
  • 34
    • 0028243155 scopus 로고
    • Binding and state of aggregation of spin-labeled cecropin AD in phospholipid bilayers: Effects of surface charge and fatty acyl chain length
    • Mchaourab, H. S., J. S. Hyde, and J. B. Feix. 1994. Binding and state of aggregation of spin-labeled cecropin AD in phospholipid bilayers: effects of surface charge and fatty acyl chain length. Biochemistry. 33: 6691-6699.
    • (1994) Biochemistry , vol.33 , pp. 6691-6699
    • McHaourab, H.S.1    Hyde, J.S.2    Feix, J.B.3
  • 36
    • 0026489966 scopus 로고
    • Selective placement of electron spin resonance spin labels: New structural methods for peptides and proteins
    • Millhauser, G. L. 1992. Selective placement of electron spin resonance spin labels: new structural methods for peptides and proteins. TIBS. 17:448-452.
    • (1992) TIBS , vol.17 , pp. 448-452
    • Millhauser, G.L.1
  • 38
    • 0029152911 scopus 로고
    • Insertion of diphtheria toxin in lipid bilayers studied by spin label ESR
    • Montich, G. G., C. Montecucco, E. Papini, and D. Marsh. 1995. Insertion of diphtheria toxin in lipid bilayers studied by spin label ESR. Biochemistry. 34:11561-11567.
    • (1995) Biochemistry , vol.34 , pp. 11561-11567
    • Montich, G.G.1    Montecucco, C.2    Papini, E.3    Marsh, D.4
  • 39
    • 0001350946 scopus 로고    scopus 로고
    • Organization of diphtheria toxin T domain in bilayers: A site-directed spin labeling study
    • Oh, K. J., H. Zhan, C. Cui, K. Hideg, R. J. Collier, and W. L. Hubbell. 1996. Organization of diphtheria toxin T domain in bilayers: a site-directed spin labeling study. Science. 273:810-812.
    • (1996) Science , vol.273 , pp. 810-812
    • Oh, K.J.1    Zhan, H.2    Cui, C.3    Hideg, K.4    Collier, R.J.5    Hubbell, W.L.6
  • 41
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • Pouny, Y., D. Rapaport, A. Mor. P. Nicolas, and Y. Shai. 1992. Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry, 31:12416-12423.
    • (1992) Biochemistry , vol.31 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 42
    • 0028339191 scopus 로고
    • Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: Facets of their conformational features, structure-function correlations and membrane-perturbing abilities
    • Saberwal, G., and R. Nagaraj. 1994. Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure-function correlations and membrane-perturbing abilities. Biochim. Biophys. Acta. 1197:109-131.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 109-131
    • Saberwal, G.1    Nagaraj, R.2
  • 43
    • 0023056958 scopus 로고
    • Thermodynamic analysis of incorporation and aggregation in a membrane: Application to the pore-forming peptide alamethicin
    • Schwarz, G., S. Stankowski, and V. Rizzo. 1986. Thermodynamic analysis of incorporation and aggregation in a membrane: application to the pore-forming peptide alamethicin. Biochim. Biophys. Acta. 861: 141-151.
    • (1986) Biochim. Biophys. Acta , vol.861 , pp. 141-151
    • Schwarz, G.1    Stankowski, S.2    Rizzo, V.3
  • 44
    • 0020039463 scopus 로고
    • Secondary structure of the cecropins: Antibacterial peptides from the moth Hyalophora cecropia
    • Steiner, H. 1982. Secondary structure of the cecropins: antibacterial peptides from the moth Hyalophora cecropia. FEBS. Lett. 137:283-287.
    • (1982) FEBS. Lett. , vol.137 , pp. 283-287
    • Steiner, H.1
  • 45
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner, H. H., D., A. Engstrom, H. Bennich, and H. G. Boman. 1981. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292:246-248.
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.H.1    Engstrom, D.A.2    Bennich, H.3    Boman, H.G.4
  • 46
    • 0023864293 scopus 로고
    • Binding and action of cecropin and cecropin analogues: Antibacterial peptides from insects
    • Steiner, H., D. Andreu, and R. B. Merrifield. 1988. Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects. Biochim. Biophys. Acta. 939:260-266.
    • (1988) Biochim. Biophys. Acta , vol.939 , pp. 260-266
    • Steiner, H.1    Andreu, D.2    Merrifield, R.B.3
  • 47
    • 0019874035 scopus 로고
    • The diffusion-concentration product of oxygen in lipid bilayers using the spin-label T1 method
    • Subczynski, W. K., and J. S. Hyde. 1981. The diffusion-concentration product of oxygen in lipid bilayers using the spin-label T1 method. Biochim. Biophys. Acta. 643:283-291.
    • (1981) Biochim. Biophys. Acta , vol.643 , pp. 283-291
    • Subczynski, W.K.1    Hyde, J.S.2
  • 48
    • 0002714883 scopus 로고
    • Electron spin resonance studies of lipid-gramicidin interactions utilizing oriented multibilayers
    • Tanaka, H., and J. H. Freed. 1985. Electron spin resonance studies of lipid-gramicidin interactions utilizing oriented multibilayers. J. Phys. Chem. 89:350-360.
    • (1985) J. Phys. Chem. , vol.89 , pp. 350-360
    • Tanaka, H.1    Freed, J.H.2
  • 49
    • 0020479123 scopus 로고
    • The structure of melittin. II. Interpretation of the structure
    • Terwilliger, T. C., and D. Eisenberg. 1982. The structure of melittin. II. Interpretation of the structure. J. Biol. Chem. 257:6016-6022.
    • (1982) J. Biol. Chem. , vol.257 , pp. 6016-6022
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 50
    • 0032538458 scopus 로고    scopus 로고
    • The dependence of membrane permeability by the antibacterial peptide cecropin B and its analogs. CB-1 and CB-3, on liposomes of different composition
    • Wang, W., D. K. Smith, K. Moulding, and H. M. Chen. 1998. The dependence of membrane permeability by the antibacterial peptide cecropin B and its analogs. CB-1 and CB-3, on liposomes of different composition. J. Biol. Chem. 273:27438-27448.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27438-27448
    • Wang, W.1    Smith, D.K.2    Moulding, K.3    Chen, H.M.4
  • 51
    • 0028061984 scopus 로고
    • Interactions between human defensins and lipid bilayers: Evidence for formation of multimeric pores
    • Wimley, W. C., M. E. Selsted, and S. H. White. 1994. Interactions between human defensins and lipid bilayers: evidence for formation of multimeric pores. Protein Sci. 3:1362-1373.
    • (1994) Protein Sci. , vol.3 , pp. 1362-1373
    • Wimley, W.C.1    Selsted, M.E.2    White, S.H.3
  • 52
    • 0010247602 scopus 로고
    • Metal-nitroxyl interactions. 12. Nitroxyl spin probes in the presence of tris(oxalato) chromate(III)
    • Yager, T. D., G. R. Eaton, and S. S. Eaton. 1979. Metal-nitroxyl interactions. 12. Nitroxyl spin probes in the presence of tris(oxalato) chromate(III). Inorg. Chem. 18:725-727.
    • (1979) Inorg. Chem. , vol.18 , pp. 725-727
    • Yager, T.D.1    Eaton, G.R.2    Eaton, S.S.3
  • 53
    • 0344717077 scopus 로고
    • Use of high observing power in electron spin resonance saturation-recovery experiments in spin-labeled membranes
    • Yin, J.-J., and Hyde, J. S. 1989. Use of high observing power in electron spin resonance saturation-recovery experiments in spin-labeled membranes. J. Chem. Phys. 91:6029-6035.
    • (1989) J. Chem. Phys. , vol.91 , pp. 6029-6035
    • Yin, J.-J.1    Hyde, J.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.