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Volumn 92, Issue 9, 2007, Pages 3166-3177

Calorimetric, X-ray diffraction, and spectroscopic studies of the thermotropic phase behavior and organization of tetramyristoyl cardiolipin membranes

Author keywords

[No Author keywords available]

Indexed keywords

CARDIOLIPIN; TETRAMYRISTOYL CARDIOLIPIN; UNCLASSIFIED DRUG;

EID: 34247579683     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.094003     Document Type: Article
Times cited : (67)

References (69)
  • 1
    • 0021804591 scopus 로고
    • Lipids of mitochondria
    • Daum, G. 1985. Lipids of mitochondria. Biochim. Biophys. Acta. 822:1-42.
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 1-42
    • Daum, G.1
  • 2
    • 0002835914 scopus 로고
    • Fatty acids, related and derived lipids
    • C. Ratledge and S. G. Wilkinson, editors. Academic Press, London
    • Ratledge, C., and S. G. Wilkinson. 1988. Fatty acids, related and derived lipids. In Microbial Lipids. C. Ratledge and S. G. Wilkinson, editors. Academic Press, London.
    • (1988) Microbial Lipids
    • Ratledge, C.1    Wilkinson, S.G.2
  • 3
    • 0001176869 scopus 로고
    • Gram-positive bacteria
    • C. Ratledge and S. G. Wilkinson, editors. Academic Press, London
    • O'Leary, W. M., and S. G. Wilkinson. 1988. Gram-positive bacteria. In Microbial Lipids. C. Ratledge and S. G. Wilkinson, editors. Academic Press, London.
    • (1988) Microbial Lipids
    • O'Leary, W.M.1    Wilkinson, S.G.2
  • 4
    • 0000420475 scopus 로고
    • Gram-negative bacteria
    • C. Ratledge and S. G. Wilkinson, editors. Academic Press, London
    • Wilkinson, S. G. 1988. Gram-negative bacteria. In Microbial Lipids. C. Ratledge and S. G. Wilkinson, editors. Academic Press, London.
    • (1988) Microbial Lipids
    • Wilkinson, S.G.1
  • 5
    • 0026603840 scopus 로고
    • Cardiolipins and biomembrane function
    • Hoch, F. L. 1992. Cardiolipins and biomembrane function. Biochim. Biophys. Acta. 1113:71-133.
    • (1992) Biochim. Biophys. Acta , vol.1113 , pp. 71-133
    • Hoch, F.L.1
  • 6
    • 0015935065 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation. XXVI. Specificity of phospholipids required for energy transfer reactions
    • Kagawa, Y., A. Kandrach, and E. Racker. 1973. Partial resolution of the enzymes catalyzing oxidative phosphorylation. XXVI. Specificity of phospholipids required for energy transfer reactions. J. Biol. Chem. 248:676-684.
    • (1973) J. Biol. Chem , vol.248 , pp. 676-684
    • Kagawa, Y.1    Kandrach, A.2    Racker, E.3
  • 7
    • 0023807789 scopus 로고
    • Synthesis of cardiolipin derivatives with protection of the free hydroxyl: Its application to the study of cardiolipin stimulation of cytochrome-c oxidase
    • Dale, M. P., and N. C. Robinson. 1988. Synthesis of cardiolipin derivatives with protection of the free hydroxyl: its application to the study of cardiolipin stimulation of cytochrome-c oxidase. Biochemistry. 27:8270-8275.
    • (1988) Biochemistry , vol.27 , pp. 8270-8275
    • Dale, M.P.1    Robinson, N.C.2
  • 8
    • 0030848050 scopus 로고    scopus 로고
    • Cell respiration is controlled by ATP, an allosteric inhibitor of cytochrome c oxidase
    • Arnold, S., and B. Kadenbach. 1997. Cell respiration is controlled by ATP, an allosteric inhibitor of cytochrome c oxidase. Eur. J. Biochem. 249:350-354.
    • (1997) Eur. J. Biochem , vol.249 , pp. 350-354
    • Arnold, S.1    Kadenbach, B.2
  • 9
    • 0035803487 scopus 로고    scopus 로고
    • Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure
    • Lange, C., J. H. Nett, B. L. Trumpower, and C. Hunte. 2001. Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure. EMBO J. 20:6591-6600.
    • (2001) EMBO J , vol.20 , pp. 6591-6600
    • Lange, C.1    Nett, J.H.2    Trumpower, B.L.3    Hunte, C.4
  • 11
    • 0017128381 scopus 로고
    • Purification and properties of the proton-translocating adenosine triphosphatase complex of bovine heart mitochondria
    • Serrano, R., B. J. Banner, and E. Racker. 1976. Purification and properties of the proton-translocating adenosine triphosphatase complex of bovine heart mitochondria. J. Biol. Chem. 251:2453-2461.
    • (1976) J. Biol. Chem , vol.251 , pp. 2453-2461
    • Serrano, R.1    Banner, B.J.2    Racker, E.3
  • 12
    • 0032407654 scopus 로고    scopus 로고
    • Cardiolipins and mitochondrial proton-selective leakage
    • Hoch, F. L. 1998. Cardiolipins and mitochondrial proton-selective leakage. J. Bioenerg. Biomembr. 30:511-532.
    • (1998) J. Bioenerg. Biomembr , vol.30 , pp. 511-532
    • Hoch, F.L.1
  • 14
    • 0020133397 scopus 로고
    • Stimulation of luteal mitochondrial cholesterol side-chain cleavage by cardiolipin
    • Tanaka, T., and J. F. Strauss. 1982. Stimulation of luteal mitochondrial cholesterol side-chain cleavage by cardiolipin. Endocrinology. 110:1592-1598.
    • (1982) Endocrinology , vol.110 , pp. 1592-1598
    • Tanaka, T.1    Strauss, J.F.2
  • 15
    • 0027315471 scopus 로고
    • Catalytic properties of cytochrome P-450(SCC) purified from the human placenta - comparison to bovine cytochrome P-450(SCC)
    • Tuckey, R. C., and K. J. Cameron. 1993. Catalytic properties of cytochrome P-450(SCC) purified from the human placenta - comparison to bovine cytochrome P-450(SCC). Biochim. Biophys. Acta. 1163:185-194.
    • (1993) Biochim. Biophys. Acta , vol.1163 , pp. 185-194
    • Tuckey, R.C.1    Cameron, K.J.2
  • 16
    • 0033559224 scopus 로고    scopus 로고
    • Enzymatic properties of vesicle-reconstituted human cytochrome P450SCC (CYP11A1) - differences in functioning of the mitochondrial electron-transfer chain using human and bovine adrenodoxin and activation by cardiolipin
    • Kisselev, P., R. C. Tuckey, S. T. Woods, T. Triantopoulos, and D. Schwartz. 1999. Enzymatic properties of vesicle-reconstituted human cytochrome P450SCC (CYP11A1) - differences in functioning of the mitochondrial electron-transfer chain using human and bovine adrenodoxin and activation by cardiolipin. Eur. J. Biochem. 260:768-773.
    • (1999) Eur. J. Biochem , vol.260 , pp. 768-773
    • Kisselev, P.1    Tuckey, R.C.2    Woods, S.T.3    Triantopoulos, T.4    Schwartz, D.5
  • 17
    • 0035115358 scopus 로고    scopus 로고
    • Is there a conserved interaction between cardiolipin and the Type II bacterial reaction center?
    • Wakeham, M. C., R. B. Sessions, M. R. Jones, and P. K. Fyfe. 2001. Is there a conserved interaction between cardiolipin and the Type II bacterial reaction center? Biophys. J. 80:1395-1405.
    • (2001) Biophys. J , vol.80 , pp. 1395-1405
    • Wakeham, M.C.1    Sessions, R.B.2    Jones, M.R.3    Fyfe, P.K.4
  • 18
    • 0021765004 scopus 로고
    • The role of lipoteichoic acid biosynthesis in membrane lipid metabolism of growing Staphylococcus aureus
    • Koch, H. U., R. Haas, and W. Fischer. 1984. The role of lipoteichoic acid biosynthesis in membrane lipid metabolism of growing Staphylococcus aureus. Eur. J. Biochem. 138:357-363.
    • (1984) Eur. J. Biochem , vol.138 , pp. 357-363
    • Koch, H.U.1    Haas, R.2    Fischer, W.3
  • 19
    • 0015137521 scopus 로고
    • Metabolism of phosphatidylglycerol, lysylphosphatidyl-glycerol and cardiolipin of Staphylococcus aureus
    • Short, S. A., and D. C. White. 1971. Metabolism of phosphatidylglycerol, lysylphosphatidyl-glycerol and cardiolipin of Staphylococcus aureus. J. Bacteriol. 108:219-226.
    • (1971) J. Bacteriol , vol.108 , pp. 219-226
    • Short, S.A.1    White, D.C.2
  • 20
    • 0015530073 scopus 로고
    • Alteration of the phospholipid composition of Staphylococcus aureus cultures in medium containing NaCl
    • Kanemasa, Y., T. Yioshioka, and H. Hayashi. 1972. Alteration of the phospholipid composition of Staphylococcus aureus cultures in medium containing NaCl. Biochim. Biophys. Acta. 280:444-450.
    • (1972) Biochim. Biophys. Acta , vol.280 , pp. 444-450
    • Kanemasa, Y.1    Yioshioka, T.2    Hayashi, H.3
  • 21
    • 0018890974 scopus 로고
    • Alteration in phospholipid composition of Staphylococcus aureus during formation of autoplast
    • Okabe, A., Y. Hirai, H. Hayashi, and Y. Kanemasa. 1980. Alteration in phospholipid composition of Staphylococcus aureus during formation of autoplast. Biochim. Biophys. Acta. 617:28-35.
    • (1980) Biochim. Biophys. Acta , vol.617 , pp. 28-35
    • Okabe, A.1    Hirai, Y.2    Hayashi, H.3    Kanemasa, Y.4
  • 22
    • 0033856291 scopus 로고    scopus 로고
    • Surface charge density markedly attenuates the nonlamellar phase-forming properties of lipid bilayer membranes
    • Lewis, R. N. A. H., and R. N. McElhaney. 2000. Surface charge density markedly attenuates the nonlamellar phase-forming properties of lipid bilayer membranes. Biophys. J. 79:1455-1464.
    • (2000) Biophys. J , vol.79 , pp. 1455-1464
    • Lewis, R.N.A.H.1    McElhaney, R.N.2
  • 24
    • 0024365895 scopus 로고
    • Effect of acyl chain composition on salt-induced lamellar to inverted hexagonal phase transitions in cardiolipin
    • Sankaram, M. B., G. L. Powell, and D. Marsh. 1989. Effect of acyl chain composition on salt-induced lamellar to inverted hexagonal phase transitions in cardiolipin. Biochim. Biophys. Acta. 980:389-392.
    • (1989) Biochim. Biophys. Acta , vol.980 , pp. 389-392
    • Sankaram, M.B.1    Powell, G.L.2    Marsh, D.3
  • 25
    • 0001632015 scopus 로고
    • Induction of lamellar-inverted hexagonal phase-transition in cardiolipin by protons and monovalent cations
    • Seddon, J. M., R. D. Kaye, and D. Marsh. 1983. Induction of lamellar-inverted hexagonal phase-transition in cardiolipin by protons and monovalent cations. Biochim. Biophys. Acta. 734:347-352.
    • (1983) Biochim. Biophys. Acta , vol.734 , pp. 347-352
    • Seddon, J.M.1    Kaye, R.D.2    Marsh, D.3
  • 27
    • 0026913153 scopus 로고
    • Nonlamellar phases formed by membrane-lipids
    • Lindblom, G., and L. Rilfors. 1992. Nonlamellar phases formed by membrane-lipids. Adv. Colloid Interface Sci. 41:101-125.
    • (1992) Adv. Colloid Interface Sci , vol.41 , pp. 101-125
    • Lindblom, G.1    Rilfors, L.2
  • 28
    • 20444421221 scopus 로고    scopus 로고
    • Effects of lipid composition on the membrane activity and lipid phase behavior of Vibrio sp DSM14379 cells grown at various NaCl concentrations
    • Davevcic, T., L. Rilfors, J. Strancar, G. Lindblom, and D. Stopar. 2005. Effects of lipid composition on the membrane activity and lipid phase behavior of Vibrio sp DSM14379 cells grown at various NaCl concentrations. Biochim. Biophys. Acta. 1712:1-8.
    • (2005) Biochim. Biophys. Acta , vol.1712 , pp. 1-8
    • Davevcic, T.1    Rilfors, L.2    Strancar, J.3    Lindblom, G.4    Stopar, D.5
  • 29
    • 0018781585 scopus 로고
    • Phase transition characteristics of diphosphatidylglycerol (cardiolipin) and stereoisomeric phosphatidyldiacylglycerol bilayers. mono-valent and divalent metal-ion effects
    • Rainer, S., M. K. Jain, F. Ramirez, P. V. Ioannou, J. F. Marecek, and R. Wagner. 1979. Phase transition characteristics of diphosphatidylglycerol (cardiolipin) and stereoisomeric phosphatidyldiacylglycerol bilayers. mono-valent and divalent metal-ion effects. Biochim. Biophys. Acta. 558:187-198.
    • (1979) Biochim. Biophys. Acta , vol.558 , pp. 187-198
    • Rainer, S.1    Jain, M.K.2    Ramirez, F.3    Ioannou, P.V.4    Marecek, J.F.5    Wagner, R.6
  • 30
    • 0022296479 scopus 로고
    • The effect of headgroup structure on phase transition of phospholipids membranes as determined by differential scanning calorimetry
    • Nagamachi, E., R. Kariyama, and Y. Kanemasa. 1985. The effect of headgroup structure on phase transition of phospholipids membranes as determined by differential scanning calorimetry. Physiol. Chem. Phys. Med. NMR. 17:255-260.
    • (1985) Physiol. Chem. Phys. Med. NMR , vol.17 , pp. 255-260
    • Nagamachi, E.1    Kariyama, R.2    Kanemasa, Y.3
  • 31
    • 0025773380 scopus 로고
    • Intramolecular hydrogen-bonding in cardiolipin
    • Hubner, W., H. H. Mantsch, and M. Kates. 1991. Intramolecular hydrogen-bonding in cardiolipin. Biochim. Biophys. Acta. 1066:166-174.
    • (1991) Biochim. Biophys. Acta , vol.1066 , pp. 166-174
    • Hubner, W.1    Mantsch, H.H.2    Kates, M.3
  • 36
    • 34247562641 scopus 로고    scopus 로고
    • Global properties of biomimetic membranes: Perspectives on molecular features
    • Pabst, G. 2006. Global properties of biomimetic membranes: perspectives on molecular features. Biophys. Rev. Lett. 1:57-84.
    • (2006) Biophys. Rev. Lett , vol.1 , pp. 57-84
    • Pabst, G.1
  • 37
    • 0037418501 scopus 로고    scopus 로고
    • Structure and interactions in the anomalous swelling regime of phospholipid bilayers
    • Pabst, G., J. Katsaras, V. A. Raghunathan, and M. Rappolt. 2003. Structure and interactions in the anomalous swelling regime of phospholipid bilayers. Langmuir. 19:1716-1722.
    • (2003) Langmuir , vol.19 , pp. 1716-1722
    • Pabst, G.1    Katsaras, J.2    Raghunathan, V.A.3    Rappolt, M.4
  • 39
    • 0029758886 scopus 로고    scopus 로고
    • Structure of gel phase saturated lecithin bilayers; temperature and chain length dependence
    • Sun, W.-J., S. Tristram-Nagle, and J. F. Nagle. 1996. Structure of gel phase saturated lecithin bilayers; temperature and chain length dependence. Biophys. J. 71:885-891.
    • (1996) Biophys. J , vol.71 , pp. 885-891
    • Sun, W.-J.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 40
    • 0000130647 scopus 로고
    • Theory of the structure factor of lipid bilayers
    • Zhang, R. T., R. M. Suter, and J. F. Nagle. 1994. Theory of the structure factor of lipid bilayers. Phys. Rev. E. 50:5047-5060.
    • (1994) Phys. Rev. E , vol.50 , pp. 5047-5060
    • Zhang, R.T.1    Suter, R.M.2    Nagle, J.F.3
  • 42
    • 0028123788 scopus 로고
    • Enigmatic thermotropic phase behavior of highly asymmetric mixed-chain phosphatidylcholines which form mixed-interdigitated gel phases
    • Lewis, R. N. A. H., R. N. McElhaney, F. Osterberg, and S. M. Gruner. 1994. Enigmatic thermotropic phase behavior of highly asymmetric mixed-chain phosphatidylcholines which form mixed-interdigitated gel phases. Biophys. J. 66:207-216.
    • (1994) Biophys. J , vol.66 , pp. 207-216
    • Lewis, R.N.A.H.1    McElhaney, R.N.2    Osterberg, F.3    Gruner, S.M.4
  • 43
    • 0035118798 scopus 로고    scopus 로고
    • Studies of the structure and organization of cationic lipid bilayer membranes: Calorimetric, spectroscopic and x-ray diffraction studies of linear saturated P-O-ethyl phosphatidylcholines
    • Lewis, R. N. A. H., I. Winter, M. Kriechbaum, K. Lohner, and R. N. McElhaney. 2001. Studies of the structure and organization of cationic lipid bilayer membranes: calorimetric, spectroscopic and x-ray diffraction studies of linear saturated P-O-ethyl phosphatidylcholines. Biophys. J. 80:1329-1342.
    • (2001) Biophys. J , vol.80 , pp. 1329-1342
    • Lewis, R.N.A.H.1    Winter, I.2    Kriechbaum, M.3    Lohner, K.4    McElhaney, R.N.5
  • 44
    • 0029014673 scopus 로고
    • Lamellar phase polymorphism in interdigitated bilayer assemblies
    • Mason, J. T., R. E. Cunningham, and T. J. O'Leary. 1995. Lamellar phase polymorphism in interdigitated bilayer assemblies. Biochim. Biophys. Acta. 1236:67-72.
    • (1995) Biochim. Biophys. Acta , vol.1236 , pp. 67-72
    • Mason, J.T.1    Cunningham, R.E.2    O'Leary, T.J.3
  • 45
    • 24044489734 scopus 로고    scopus 로고
    • α phase: A comparison of phosphatidylcholine and phosphatidylethanolamine membranes
    • S. G. Pandalai, editor. Transworld Research Network, Kerala
    • α phase: a comparison of phosphatidylcholine and phosphatidylethanolamine membranes. In Recent Research Developments in Biophysics, Vol. 3. S. G. Pandalai, editor. Transworld Research Network, Kerala.
    • (2004) Recent Research Developments in Biophysics , vol.3
    • Rappolt, M.1    Laggner, P.2    Pabst, G.3
  • 46
    • 0015935391 scopus 로고
    • Structure and polymorphism of the hydrocarbon chains of lipids: A study of lecithin-water phases
    • Tardieu, A., V. Luzzatti, and F. C. Reman. 1973. Structure and polymorphism of the hydrocarbon chains of lipids: a study of lecithin-water phases. J. Mol. Biol. 75:711-733.
    • (1973) J. Mol. Biol , vol.75 , pp. 711-733
    • Tardieu, A.1    Luzzatti, V.2    Reman, F.C.3
  • 47
    • 0025652577 scopus 로고
    • Hydrocarbon chain packing modes in lipids: Effect of altered subcell dimensions and chain rotation
    • Maulik, P. R., M. J. Ruocco, and G. G. Shipley. 1990. Hydrocarbon chain packing modes in lipids: effect of altered subcell dimensions and chain rotation. Chem. Phys. Lipids. 56:123-133.
    • (1990) Chem. Phys. Lipids , vol.56 , pp. 123-133
    • Maulik, P.R.1    Ruocco, M.J.2    Shipley, G.G.3
  • 48
    • 0024291333 scopus 로고
    • Structure and mechanical properties of giant lipid (DMPC) vesicle bilayers from 20°C below to 10°C above the liquid crystal-crystalline phase transition at 24°C
    • Needham, D., and E. Evans. 1988. Structure and mechanical properties of giant lipid (DMPC) vesicle bilayers from 20°C below to 10°C above the liquid crystal-crystalline phase transition at 24°C. Biochemistry. 27:8261-8269.
    • (1988) Biochemistry , vol.27 , pp. 8261-8269
    • Needham, D.1    Evans, E.2
  • 49
    • 14544295414 scopus 로고    scopus 로고
    • Vibrational spectroscopy of lipids
    • Spectroscopy. J. M. Chalmers and P. R. Griffiths, editors. John Wiley & Sons, New York
    • Lewis, R. N. A. H., and R. N. McElhaney. 2002. Vibrational spectroscopy of lipids. In The Handbook of Vibrational Spectroscopy. J. M. Chalmers and P. R. Griffiths, editors. John Wiley & Sons, New York. 5:3447-3464.
    • (2002) The Handbook of Vibrational , vol.5 , pp. 3447-3464
    • Lewis, R.N.A.H.1    McElhaney, R.N.2
  • 50
    • 0001774382 scopus 로고    scopus 로고
    • FTIR spectroscopy in the study of hydrated lipids and lipid bilayer membranes
    • H. H. Mantsch and D. Chapman, editors. John Wiley & Sons, New York
    • Lewis, R. N. A. H., and R. N. McElhaney. 1996. FTIR spectroscopy in the study of hydrated lipids and lipid bilayer membranes. In Infrared Spectroscopy of Biomolecules. H. H. Mantsch and D. Chapman, editors. John Wiley & Sons, New York.
    • (1996) Infrared Spectroscopy of Biomolecules
    • Lewis, R.N.A.H.1    McElhaney, R.N.2
  • 51
    • 0024291319 scopus 로고
    • 13C=O labeled phospholipids. Hydrogen bonding to carbonyl groups
    • 13C=O labeled phospholipids. Hydrogen bonding to carbonyl groups. Biochemistry. 27:8239-8249.
    • (1988) Biochemistry , vol.27 , pp. 8239-8249
    • Blume, A.1    Hübner, W.2    Messner, G.3
  • 52
    • 0027987329 scopus 로고
    • The components of the carbonyl stretching band in the infrared spectra of hydrated 1,2-diacylglycerolipid bilayers: A reevaluation
    • Lewis, R. N. A. H., R. N. McElhaney, W. Pohle, and H. H. Mantsch. 1994. The components of the carbonyl stretching band in the infrared spectra of hydrated 1,2-diacylglycerolipid bilayers: a reevaluation. Biophys. J. 67:2367-2375.
    • (1994) Biophys. J , vol.67 , pp. 2367-2375
    • Lewis, R.N.A.H.1    McElhaney, R.N.2    Pohle, W.3    Mantsch, H.H.4
  • 53
    • 0000648231 scopus 로고
    • Slow motional line NMR line shapes for very anisotropic rotational diffusion phosphorous-31 NMR of phospholipids
    • Campbell, R. F., F. E. Meirovitch, and J. H. Freed. 1979. Slow motional line NMR line shapes for very anisotropic rotational diffusion phosphorous-31 NMR of phospholipids. J. Phys. Chem. 83:525-533.
    • (1979) J. Phys. Chem , vol.83 , pp. 525-533
    • Campbell, R.F.1    Meirovitch, F.E.2    Freed, J.H.3
  • 54
    • 0017902280 scopus 로고
    • 31P Nuclear magnetic resonance and the headgroup structure of phospholipid membranes
    • 31P Nuclear magnetic resonance and the headgroup structure of phospholipid membranes. Biochim. Biophys. Acta. 515:105-140.
    • (1978) Biochim. Biophys. Acta , vol.515 , pp. 105-140
    • Seelig, J.1
  • 55
    • 0031012862 scopus 로고    scopus 로고
    • Calorimetric and spectroscopic studies of the thermotropic phase behavior of the n-saturated 1,2-diacyl-phosphatidylglycerols
    • Zhang, Y.-P., R. N. A. H. Lewis, and R. N. McElhaney. 1997. Calorimetric and spectroscopic studies of the thermotropic phase behavior of the n-saturated 1,2-diacyl-phosphatidylglycerols. Biophys. J. 72:779-793.
    • (1997) Biophys. J , vol.72 , pp. 779-793
    • Zhang, Y.-P.1    Lewis, R.N.A.H.2    McElhaney, R.N.3
  • 56
    • 0027292860 scopus 로고
    • Calorimetric and spectroscopic studies of the polymorphic phase behavior of a homologous series of n-saturated 1,2-diacyl phosphatidylethanolamines
    • Lewis, R. N. A. H., and R. N. McElhaney. 1993. Calorimetric and spectroscopic studies of the polymorphic phase behavior of a homologous series of n-saturated 1,2-diacyl phosphatidylethanolamines. Biophys. J. 64:1081-1096.
    • (1993) Biophys. J , vol.64 , pp. 1081-1096
    • Lewis, R.N.A.H.1    McElhaney, R.N.2
  • 57
    • 0019883908 scopus 로고
    • Titration of the phase transition of phosphatidylserine bilayer membranes: Effects of pH, surface electrostatics, ion binding and headgroup hydration
    • Cevc, G., A. Watts, and D. Marsh. 1981. Titration of the phase transition of phosphatidylserine bilayer membranes: effects of pH, surface electrostatics, ion binding and headgroup hydration. Biochemistry. 20:4955-4965.
    • (1981) Biochemistry , vol.20 , pp. 4955-4965
    • Cevc, G.1    Watts, A.2    Marsh, D.3
  • 59
    • 0023646707 scopus 로고
    • How membrane chain-melting properties are regulated by the polar surface of lipid bilayers
    • Cevc, G. 1990. How membrane chain-melting properties are regulated by the polar surface of lipid bilayers. Biochemistry. 26:6305-6310.
    • (1990) Biochemistry , vol.26 , pp. 6305-6310
    • Cevc, G.1
  • 61
    • 0031012862 scopus 로고    scopus 로고
    • Calorimetric and spectroscopic studies of the thermotropic phase behavior of the n-saturated 1,2-diacylphosphatidylglycerols
    • Zhang, Y. P., R. N. A. H. Lewis, and R. N. McElhaney. 1997. Calorimetric and spectroscopic studies of the thermotropic phase behavior of the n-saturated 1,2-diacylphosphatidylglycerols. Biophys. J. 72:779-793.
    • (1997) Biophys. J , vol.72 , pp. 779-793
    • Zhang, Y.P.1    Lewis, R.N.A.H.2    McElhaney, R.N.3
  • 62
    • 0000598799 scopus 로고
    • Conformation and packing properties of phosphatidic acid: The crystal structure of monosodium dimyristoylphosphatidate
    • Harlos, K., H. Eibl, I. Pascher, and S. Sundell. 1984. Conformation and packing properties of phosphatidic acid: the crystal structure of monosodium dimyristoylphosphatidate. Chem. Phys. Lipids. 34:115-126.
    • (1984) Chem. Phys. Lipids , vol.34 , pp. 115-126
    • Harlos, K.1    Eibl, H.2    Pascher, I.3    Sundell, S.4
  • 63
    • 0018788297 scopus 로고
    • The molecular structure of lecithin dehydrate
    • Pearson, R. H., and I. Pascher. 1979. The molecular structure of lecithin dehydrate. Nature. 281:499-501.
    • (1979) Nature , vol.281 , pp. 499-501
    • Pearson, R.H.1    Pascher, I.2
  • 64
    • 0000048078 scopus 로고
    • Structural chemistry of 1,2 dilauroyl-DL-phosphatidylethanolamine: Molecular conformation and intermolecular packing of phospholipids
    • Hitchcock, P. B., R. Mason, K. M. Thomas, and G. G. Shipley. 1974. Structural chemistry of 1,2 dilauroyl-DL-phosphatidylethanolamine: molecular conformation and intermolecular packing of phospholipids. Proc. Natl. Acad. Sci. USA. 71:3036-3040.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 3036-3040
    • Hitchcock, P.B.1    Mason, R.2    Thomas, K.M.3    Shipley, G.G.4
  • 65
    • 0023648635 scopus 로고
    • Conformation and packing of membrane phospholipids: The crystal structure of sodium dimyristoylphosphatidylglycerol
    • Pascher, I., S. Sundell, K. Harlos, and H. Eibl. 1987. Conformation and packing of membrane phospholipids: the crystal structure of sodium dimyristoylphosphatidylglycerol. Biochim. Biophys. Acta. 896:77-88.
    • (1987) Biochim. Biophys. Acta , vol.896 , pp. 77-88
    • Pascher, I.1    Sundell, S.2    Harlos, K.3    Eibl, H.4
  • 66
    • 0033576275 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic studies of the interaction of the antimicrobial peptide Gramicidin S with lipid micelles and with lipid monolayer and bilayer membranes
    • Lewis, R. N. A. H., E. J. Prenner, L. H. Kondejewski, C. R. Flach, R. Mendelsohn, R. S. Hodges, and R. N. McElhaney. 1999. Fourier transform infrared spectroscopic studies of the interaction of the antimicrobial peptide Gramicidin S with lipid micelles and with lipid monolayer and bilayer membranes. Biochemistry. 38:15193-15203.
    • (1999) Biochemistry , vol.38 , pp. 15193-15203
    • Lewis, R.N.A.H.1    Prenner, E.J.2    Kondejewski, L.H.3    Flach, C.R.4    Mendelsohn, R.5    Hodges, R.S.6    McElhaney, R.N.7
  • 67
    • 0029984783 scopus 로고    scopus 로고
    • Interaction of nisin with planar lipid bilayers monitored by fluorescence recovery after photobleaching
    • Giffard, C. J., S. Ladha, A. R. Mackie, D. C. Clark, and D. Sanders. 1996. Interaction of nisin with planar lipid bilayers monitored by fluorescence recovery after photobleaching. J. Membr. Biol. 151:293-300.
    • (1996) J. Membr. Biol , vol.151 , pp. 293-300
    • Giffard, C.J.1    Ladha, S.2    Mackie, A.R.3    Clark, D.C.4    Sanders, D.5
  • 68
    • 0030047564 scopus 로고    scopus 로고
    • Nisin Z, mutant nisin Z and lacticin 481 interactions with anionic lipid correlate with antimicrobial activity. A monolayer study
    • Demel, R. A., T. Peelen, R. J. Siezen, B. de Kruijff, and O. P. Kuipers. 1996. Nisin Z, mutant nisin Z and lacticin 481 interactions with anionic lipid correlate with antimicrobial activity. A monolayer study. Eur. J. Biochem. 235:267-274.
    • (1996) Eur. J. Biochem , vol.235 , pp. 267-274
    • Demel, R.A.1    Peelen, T.2    Siezen, R.J.3    de Kruijff, B.4    Kuipers, O.P.5


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