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Volumn 70, Issue 1, 1996, Pages 84-96

A Monte Carlo simulation study of protein-induced heat capacity changes and lipid-induced protein clustering

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BINDING AFFINITY; CALORIMETRY; LIPID MEMBRANE; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN LIPID INTERACTION; PROTEIN LOCALIZATION; SYSTEM ANALYSIS; THERMODYNAMICS;

EID: 0030071247     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79551-6     Document Type: Article
Times cited : (61)

References (69)
  • 1
    • 0027511498 scopus 로고
    • Percolation, and diffusion in three-component lipid bilayers: Effect of cholesterol on an equimolar mixture of two phosphatidylcholines
    • Almeida, P. F. F., W. L. C. Vaz, and T. E. Thompson. 1993. Percolation, and diffusion in three-component lipid bilayers: effect of cholesterol on an equimolar mixture of two phosphatidylcholines. Biophys. J. 64:399-412.
    • (1993) Biophys. J. , vol.64 , pp. 399-412
    • Almeida, P.F.F.1    Vaz, W.L.C.2    Thompson, T.E.3
  • 3
    • 0002566197 scopus 로고
    • A statistical-thermodynamic view of cooperative structural changes in phospholipid bilayer membranes: Their potential role in biological function
    • Biltonen, R. L. 1990. A statistical-thermodynamic view of cooperative structural changes in phospholipid bilayer membranes: their potential role in biological function. J. Chem. Thermodynamics. 22:1-19.
    • (1990) J. Chem. Thermodynamics , vol.22 , pp. 1-19
    • Biltonen, R.L.1
  • 4
    • 0019027499 scopus 로고
    • Lipid phase transition in planar bilayer membrane, and its effect on carrier-, and pore-mediated transport
    • Boheim, G., W. Hanke, and H. J. Eibl. 1980 Lipid phase transition in planar bilayer membrane, and its effect on carrier-, and pore-mediated transport. Proc. Natl Acad. Sci. USA. 77:3403-3407.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 3403-3407
    • Boheim, G.1    Hanke, W.2    Eibl, H.J.3
  • 5
    • 0024415946 scopus 로고
    • Effects of acyl chain length on the structure, and motion of gramicidin A in lipid bilayers
    • Cornell, B. A., F. Separovic, D. E. Thomas, A. R. Atkins, and R. Smith. 1989. Effects of acyl chain length on the structure, and motion of gramicidin A in lipid bilayers. Biochim. Biophys. Acta. 985:229-232.
    • (1989) Biochim. Biophys. Acta , vol.985 , pp. 229-232
    • Cornell, B.A.1    Separovic, F.2    Thomas, D.E.3    Atkins, A.R.4    Smith, R.5
  • 6
    • 0023664811 scopus 로고
    • Noncooperative vs. cooperative reactivation of D-β-hydroxybutyrate-dehydrogenase: Multiple equilibria for lecithin binding are determined by the physical state (soluble vs. bilayer) and composition of the phospholipid
    • Cortese, J. D., and S Fleischer. 1987. Noncooperative vs. cooperative reactivation of D-β-hydroxybutyrate-dehydrogenase: multiple equilibria for lecithin binding are determined by the physical state (soluble vs. bilayer) and composition of the phospholipid. Biochemistry. 26:5283-5293.
    • (1987) Biochemistry , vol.26 , pp. 5283-5293
    • Cortese, J.D.1    Fleischer, S.2
  • 7
    • 0000399355 scopus 로고
    • Application of finite-size scaling to the Pink model for lipid bilayers
    • Corvera, E., M. Laradij, and M. J. Zuckermann. 1993. Application of finite-size scaling to the Pink model for lipid bilayers. J. Phys. Rev E 47:696-703.
    • (1993) J. Phys. Rev E , vol.47 , pp. 696-703
    • Corvera, E.1    Laradij, M.2    Zuckermann, M.J.3
  • 8
    • 0019328329 scopus 로고
    • Cytochrome c specifically induces non-bilayer structures in cardiolipin-containing model membranes
    • de Kruijff, B., and P. R. Cullis. 1980. Cytochrome c specifically induces non-bilayer structures in cardiolipin-containing model membranes. Biochim. Biophys. Acta. 602:477-490.
    • (1980) Biochim. Biophys. Acta , vol.602 , pp. 477-490
    • De Kruijff, B.1    Cullis, P.R.2
  • 9
    • 36749107374 scopus 로고
    • Thermodynaimc fluctuations in phospholipid bilayers
    • Doniach, S. J. 1978. Thermodynaimc fluctuations in phospholipid bilayers. J. Chem. Phys. 68:4912-4915.
    • (1978) J. Chem. Phys. , vol.68 , pp. 4912-4915
    • Doniach, S.J.1
  • 10
    • 0021113445 scopus 로고
    • The effects of bilayer thickness and tension on gramicidin single-channel lifetime
    • Elliott, J. R., D. Needham, J. P. Dilger, and D. A. Haydon. 1983. The effects of bilayer thickness and tension on gramicidin single-channel lifetime. Biochim. Biophys. Acta. 735:95-103.
    • (1983) Biochim. Biophys. Acta , vol.735 , pp. 95-103
    • Elliott, J.R.1    Needham, D.2    Dilger, J.P.3    Haydon, D.A.4
  • 11
    • 0027362726 scopus 로고
    • A molecular model for lipid-protein interaction in membranes, the role of hydrophobic mismatch
    • Fattal, D. R., and A. Ben-Shaul 1993. A molecular model for lipid-protein interaction in membranes, the role of hydrophobic mismatch. Biophys. J. 65:1795-1809.
    • (1993) Biophys. J. , vol.65 , pp. 1795-1809
    • Fattal, D.R.1    Ben-Shaul, A.2
  • 12
    • 0001447096 scopus 로고
    • Theory and simulations for hard-disk models of binary mixtures of molecules with internal degrees of freedom
    • Fraser, D. P., M. J. Zuckermann, and O. G. Mouritsen. 1991. Theory and simulations for hard-disk models of binary mixtures of molecules with internal degrees of freedom. Phys. Rev. A 43:6642-6656.
    • (1991) Phys. Rev. A , vol.43 , pp. 6642-6656
    • Fraser, D.P.1    Zuckermann, M.J.2    Mouritsen, O.G.3
  • 15
    • 11644279337 scopus 로고
    • Time-dependent statistics of the Ising model
    • Glauber, R. J. 1963. Time-dependent statistics of the Ising model. J. Math. Phys. 4:294-306.
    • (1963) J. Math. Phys. , vol.4 , pp. 294-306
    • Glauber, R.J.1
  • 16
    • 0023053349 scopus 로고
    • Apocytochrome c binding to negatively charged lipid dispersions studied by spin-label electron spin resonance
    • Görrissen, H., and D. Marsh. 1986. Apocytochrome c binding to negatively charged lipid dispersions studied by spin-label electron spin resonance. Biochemistry. 25:2904-2910.
    • (1986) Biochemistry , vol.25 , pp. 2904-2910
    • Görrissen, H.1    Marsh, D.2
  • 18
    • 0025267451 scopus 로고
    • Hydrolytic action of phospholipase A2 in monolayers in the phase transition region: Direct observation of enzyme domain formation using fluorescence microscopy
    • Grainger, D. W., A. Reichert, H. Ringsdorf, and C. Salesse. 1990. Hydrolytic action of phospholipase A2 in monolayers in the phase transition region: direct observation of enzyme domain formation using fluorescence microscopy. Biochim. Biophys. Acta. 1023:365-379.
    • (1990) Biochim. Biophys. Acta , vol.1023 , pp. 365-379
    • Grainger, D.W.1    Reichert, A.2    Ringsdorf, H.3    Salesse, C.4
  • 19
    • 0019323459 scopus 로고
    • The lowest conductance state of the alamethicin pore
    • Hanke, W., and G. Boheim. 1980. The lowest conductance state of the alamethicin pore. Biochim. Biophys Acta. 596:456-462.
    • (1980) Biochim. Biophys Acta , vol.596 , pp. 456-462
    • Hanke, W.1    Boheim, G.2
  • 20
    • 0027963594 scopus 로고
    • The thermotropic behavior of dimyristoyl phosphatidylglycerol and its interaction with cytochrome c
    • Heimburg, T., and R. L. Biltonen. 1994. The thermotropic behavior of dimyristoyl phosphatidylglycerol and its interaction with cytochrome c. Biochemistry. 33:9477-9488.
    • (1994) Biochemistry , vol.33 , pp. 9477-9488
    • Heimburg, T.1    Biltonen, R.L.2
  • 21
    • 0026012387 scopus 로고
    • 31P-NMR spectroscopy. Correlation between the conformational changes of the protein and the lipid bilayer
    • 31P-NMR spectroscopy. Correlation between the conformational changes of the protein and the lipid bilayer. Biochemistry. 30:9084-9089.
    • (1991) Biochemistry , vol.30 , pp. 9084-9089
    • Heimburg, T.1    Hildebrandt, P.2    Marsh, D.3
  • 22
    • 0027145627 scopus 로고
    • Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements: An FTIR study
    • Heimburg, T., and D. Marsh. 1993. Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements: an FTIR study. Biophys. J. 65:2408-2417.
    • (1993) Biophys. J. , vol.65 , pp. 2408-2417
    • Heimburg, T.1    Marsh, D.2
  • 23
    • 0025330596 scopus 로고
    • Quantitative conformational analysis of cytochrome c bound to phospholipid vesicles studied by resonance Raman spectroscopy
    • Hildebrandt, P., T Heimburg, and D. Marsh. 1990. Quantitative conformational analysis of cytochrome c bound to phospholipid vesicles studied by resonance Raman spectroscopy Eur. Biophys. J. 18:193-201.
    • (1990) Eur. Biophys. J. , vol.18 , pp. 193-201
    • Hildebrandt, P.1    Heimburg, T.2    Marsh, D.3
  • 25
    • 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
  • 26
    • 0025963179 scopus 로고
    • A general model for the interaction of foreign molecules with lipid membranes: Drugs and anesthetics
    • Jørgensen, K., J. H. Ipsen, O. G. Mouritsen, D. Bennet, and M. J. Zuckermann. 1991. A general model for the interaction of foreign molecules with lipid membranes: drugs and anesthetics. Biochim. Biophys. Acta. 1062:227-238.
    • (1991) Biochim. Biophys. Acta , vol.1062 , pp. 227-238
    • Jørgensen, K.1    Ipsen, J.H.2    Mouritsen, O.G.3    Bennet, D.4    Zuckermann, M.J.5
  • 27
    • 0027291942 scopus 로고
    • Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids
    • Keller, S. L., S. M. Bezrukov, S. M. Gruner, M. W. Tate, I. Vodyanoy, and V. A. Parsegian. 1994. Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids. Biophys. J. 65:23-27.
    • (1994) Biophys. J. , vol.65 , pp. 23-27
    • Keller, S.L.1    Bezrukov, S.M.2    Gruner, S.M.3    Tate, M.W.4    Vodyanoy, I.5    Parsegian, V.A.6
  • 28
    • 0025046582 scopus 로고
    • Reconstitution of transferrin receptor in mixed lipid vesicles. An example of the role of elastic and electrostatic forces for protein/lipid assembly
    • Kurrle, A., P. Rieber, and E Sackmann. 1990. Reconstitution of transferrin receptor in mixed lipid vesicles. An example of the role of elastic and electrostatic forces for protein/lipid assembly. Biochemistry. 29: 8274-8282.
    • (1990) Biochemistry , vol.29 , pp. 8274-8282
    • Kurrle, A.1    Rieber, P.2    Sackmann, E.3
  • 29
    • 33744650461 scopus 로고
    • Finite-size scaling and Monte Carlo simulations of first-order phase transitions
    • Lee, J., and J. M. Kosterlitz. 1991. Finite-size scaling and Monte Carlo simulations of first-order phase transitions. Phys. Rev. B. 43:3265-3277.
    • (1991) Phys. Rev. B , vol.43 , pp. 3265-3277
    • Lee, J.1    Kosterlitz, J.M.2
  • 30
    • 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
  • 32
    • 0002316753 scopus 로고
    • Spin-labeling and lipid-protein interactions in membranes
    • P. C. Jost and O. H. Griffith, editors, Wiley-Interscience, New York
    • Marsh, D., and A. Watts. 1982. Spin-labeling and lipid-protein interactions in membranes. In Lipid-Protein Interactions, Vol. 2. P. C. Jost and O. H. Griffith, editors, Wiley-Interscience, New York. 53-126.
    • (1982) Lipid-Protein Interactions , vol.2 , pp. 53-126
    • Marsh, D.1    Watts, A.2
  • 33
    • 0017617743 scopus 로고
    • Cooperativity of the phase transition in single-and multibilayer lipid vesicles
    • Marsh, D., A. Watts, and P. F. Knowles. 1977. Cooperativity of the phase transition in single- and multibilayer lipid vesicles. Biochim. Biophys. Acta. 465:500-514.
    • (1977) Biochim. Biophys. Acta , vol.465 , pp. 500-514
    • Marsh, D.1    Watts, A.2    Knowles, P.F.3
  • 34
    • 0022454645 scopus 로고
    • Studies of the interaction of human erythrocyte band 3 with membrane lipids using deuterium nuclear magnetic resonance, and differential scanning calorimetry
    • Morrow, M. R., J. H. Davis, F. J. Sharom, and M P. Lamb. 1986. Studies of the interaction of human erythrocyte band 3 with membrane lipids using deuterium nuclear magnetic resonance, and differential scanning calorimetry. Biochim. Biophys. Acta. 858:13-20.
    • (1986) Biochim. Biophys. Acta , vol.858 , pp. 13-20
    • Morrow, M.R.1    Davis, J.H.2    Sharom, F.J.3    Lamb, M.P.4
  • 36
    • 0025978450 scopus 로고
    • Theoretical models of phospholipid phase transitions
    • Mouritsen, O. G. 1991. Theoretical models of phospholipid phase transitions. Chem. Phys. Lipids. 57:179-194.
    • (1991) Chem. Phys. Lipids , vol.57 , pp. 179-194
    • Mouritsen, O.G.1
  • 37
    • 0002231181 scopus 로고
    • Protein-Lipid Interactions and membrane heterogeneity
    • A. Watts, editor. Elsevier, New York
    • Mouritsen, O. G., and R. L. Biltonen. 1992. Protein-Lipid Interactions and membrane heterogeneity. In Protein-Lipid Interactions. A. Watts, editor. Elsevier, New York. 1-35.
    • (1992) Protein-Lipid Interactions , pp. 1-35
    • Mouritsen, O.G.1    Biltonen, R.L.2
  • 39
    • 0026811372 scopus 로고
    • Dynamic lipid-bilayer heterogeneity: A mesoscopic vehicle for membrane function?
    • Mouritsen, O. G., and K. Jørgensen. 1992. Dynamic lipid-bilayer heterogeneity: a mesoscopic vehicle for membrane function? BioEssays. 14:129-135.
    • (1992) BioEssays , vol.14 , pp. 129-135
    • Mouritsen, O.G.1    Jørgensen, K.2
  • 40
    • 0008642108 scopus 로고
    • Thermodynamics of lipid-protein interactions in lipid membranes: The hydrophobic matching condition
    • M. Jackson, editor CRC Press, Boca Raton. FL
    • Mouritsen, O. G., and M. M. Sperotto. 1992. Thermodynamics of lipid-protein interactions in lipid membranes: the hydrophobic matching condition. In Thermodynamics of cell surface receptors, M. Jackson, editor CRC Press, Boca Raton. FL. 127-181.
    • (1992) Thermodynamics of Cell Surface Receptors , pp. 127-181
    • Mouritsen, O.G.1    Sperotto, M.M.2
  • 41
    • 85031227125 scopus 로고
    • Lipid surface organization as factor in the regulation of lipolytic enzymes
    • Muderwha, J. M., and H. L. Brockman. 1992. Lipid surface organization as factor in the regulation of lipolytic enzymes. Biophys. J. 61:A367.
    • (1992) Biophys. J. , vol.61
    • Muderwha, J.M.1    Brockman, H.L.2
  • 42
    • 0021227676 scopus 로고
    • The role of protein kinase c in cell surface signal transduction and tumor promotion
    • Nishizuka, Y. 1984. The role of protein kinase c in cell surface signal transduction and tumor promotion. Nature. 308:693-698.
    • (1984) Nature , vol.308 , pp. 693-698
    • Nishizuka, Y.1
  • 43
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase c
    • Nishizuka, Y. 1986. Studies and perspectives of protein kinase c. Science. 233:305-312.
    • (1986) Science , vol.233 , pp. 305-312
    • Nishizuka, Y.1
  • 44
    • 0025667349 scopus 로고
    • Kinetics of gramicidin channel formation in lipid bilayers: Transmembrane monomer association
    • O'Connell, A. M., R. E. Koeppe, and O. S. Andersen. 1990. Kinetics of gramicidin channel formation in lipid bilayers: transmembrane monomer association. Science. 250:1256-1259.
    • (1990) Science , vol.250 , pp. 1256-1259
    • O'Connell, A.M.1    Koeppe, R.E.2    Andersen, O.S.3
  • 46
    • 0026682675 scopus 로고
    • Interaction of protein kinase c with phosphatidylserine 1 cooperativity in lipid binding
    • Orr, J. W., and A. C. Newton. 1992a. Interaction of protein kinase c with phosphatidylserine 1 cooperativity in lipid binding. Biochemistry. 31: 4661-4667.
    • (1992) Biochemistry , vol.31 , pp. 4661-4667
    • Orr, J.W.1    Newton, A.C.2
  • 47
    • 0026635971 scopus 로고
    • Interaction of protein kinase c with phosphatidylserine. Specificity and regulation
    • Orr, J. W., and A. C. Newton. 1992b. Interaction of protein kinase c with phosphatidylserine. Specificity and regulation. Biochemistry. 31: 4667-4673.
    • (1992) Biochemistry , vol.31 , pp. 4667-4673
    • Orr, J.W.1    Newton, A.C.2
  • 48
    • 0343525407 scopus 로고
    • Protein-lipid interactions in bilayer lipids: A lattice model
    • Pink, D. A., and D. Chapman. 1979. Protein-lipid interactions in bilayer lipids: a lattice model. Proc. Natl. Acad. Sci. USA. 76:1542-1546.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 1542-1546
    • Pink, D.A.1    Chapman, D.2
  • 49
    • 0019330568 scopus 로고
    • Raman scattering in bilayers of saturated phosphatidylcholines
    • Pink, D. A., T. J. Green, and D. Chapman. 1980. Raman scattering in bilayers of saturated phosphatidylcholines. Exp. Theor. Biochem. 19:349-356
    • (1980) Exp. Theor. Biochem. , vol.19 , pp. 349-356
    • Pink, D.A.1    Green, T.J.2    Chapman, D.3
  • 50
    • 33845375670 scopus 로고
    • Direct measurement of the energetics of association between myelin basic protein and phosphatidylserine vesicles
    • Ramsay, G., R. Prabhu, and E. Freire. 1986. Direct measurement of the energetics of association between myelin basic protein and phosphatidylserine vesicles. Biochemistry. 25:2265-2270.
    • (1986) Biochemistry , vol.25 , pp. 2265-2270
    • Ramsay, G.1    Prabhu, R.2    Freire, E.3
  • 51
    • 33751385662 scopus 로고
    • Distribution of proteins and lipids in the erythrocyte membrane
    • Rodgers, W., and M. Glaser. 1993. Distribution of proteins and lipids in the erythrocyte membrane. Biochemistry. 32:12591-12598.
    • (1993) Biochemistry , vol.32 , pp. 12591-12598
    • Rodgers, W.1    Glaser, M.2
  • 52
    • 0023230264 scopus 로고
    • 2 by dipalmitoylphosphatidylcholine large unilamellar vesicles
    • 2 by dipalmitoylphosphatidylcholine large unilamellar vesicles. J. Biol. Chem. 262:13476-13482.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13476-13482
    • Romero, G.1    Thompson, K.2    Biltonen, R.L.3
  • 53
    • 0024400738 scopus 로고
    • Theory of protein-induced lateral phase separation in lipid membranes
    • Sperotto, M. M, J. H. Ipsen, and O. G. Mouritsen. 1989. Theory of protein-induced lateral phase separation in lipid membranes. Cell Biophys. 14:79-95.
    • (1989) Cell Biophys. , vol.14 , pp. 79-95
    • Sperotto, M.M.1    Ipsen, J.H.2    Mouritsen, O.G.3
  • 54
    • 0026071516 scopus 로고
    • Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins
    • Sperotto, M. M., and O. G. Mouritsen. 1991. Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins. Biophys. J. 59:261-270.
    • (1991) Biophys. J. , vol.59 , pp. 261-270
    • Sperotto, M.M.1    Mouritsen, O.G.2
  • 55
    • 0027438092 scopus 로고
    • Lipid enrichment and selectivity of integral membrane proteins in two component lipid bilayers
    • Sperotto, M., and O. G. Mouritsen. 1993. Lipid enrichment and selectivity of integral membrane proteins in two component lipid bilayers. Eur. Biophys. J. 22:323-328
    • (1993) Eur. Biophys. J. , vol.22 , pp. 323-328
    • Sperotto, M.1    Mouritsen, O.G.2
  • 56
    • 0028672837 scopus 로고
    • Monte Carlo simulations of membranes: The phase transition of small unilamellar DPPC vesicles
    • Sugar, I. P., R. L. Biltonen, and N. Mitchard. 1994. Monte Carlo simulations of membranes: the phase transition of small unilamellar DPPC vesicles. Methods Enzymol. 240:569-593.
    • (1994) Methods Enzymol. , vol.240 , pp. 569-593
    • Sugar, I.P.1    Biltonen, R.L.2    Mitchard, N.3
  • 57
    • 84920302715 scopus 로고
    • Two-state model of the gel-liquid crystalline transition of small unilamellar vesicles of dipalmitoyl phosphatidylcholine
    • Sugar, I., N. Mitchard, and R. L. Biltonen. 1992. Two-state model of the gel-liquid crystalline transition of small unilamellar vesicles of dipalmitoyl phosphatidylcholine. Biophys. J. 63:A238.
    • (1992) Biophys. J. , vol.63
    • Sugar, I.1    Mitchard, N.2    Biltonen, R.L.3
  • 58
    • 85031233785 scopus 로고
    • Biological membrane domains: Possible functional significance
    • Thompson, T. E , M. B. Sankaram, and R. L. Biltonen. 1992. Biological membrane domains: possible functional significance. FASEB J. 6:A90.
    • (1992) FASEB J. , vol.6
    • Thompson, T.E.1    Sankaram, M.B.2    Biltonen, R.L.3
  • 60
    • 0024759776 scopus 로고
    • Translational diffusion and fluid domain connectivity in a two-component, two-phase phospholipid bilayer
    • Vaz, W. L. C., E. C. C. Melo, and T. E. Thompson. 1989. Translational diffusion and fluid domain connectivity in a two-component, two-phase phospholipid bilayer. Biophys. J. 56:869-876.
    • (1989) Biophys. J. , vol.56 , pp. 869-876
    • Vaz, W.L.C.1    Melo, E.C.C.2    Thompson, T.E.3
  • 61
    • 0025368549 scopus 로고
    • Fluid-phase connectivity in an isomorphous. two-component-two phase phosphatidylcholine bilayer
    • Vaz, W. L. C., E. C. C., Melo, and T. E. Thompson. 1990. Fluid-phase connectivity in an isomorphous. two-component-two phase phosphatidylcholine bilayer. Biophys J. 58:273-275.
    • (1990) Biophys J. , vol.58 , pp. 273-275
    • Vaz, W.L.C.1    Melo, E.C.C.2    Thompson, T.E.3
  • 62
    • 0027517413 scopus 로고
    • Probing alamethicin channels with water-soluble polymers: Size modulated osmotic action
    • Vodyanoy, I., S. M. Bezrukov, and V. A. Parsegian. 1993. Probing alamethicin channels with water-soluble polymers: size modulated osmotic action. Biophys. J. 65:2097-2105.
    • (1993) Biophys. J. , vol.65 , pp. 2097-2105
    • Vodyanoy, I.1    Bezrukov, S.M.2    Parsegian, V.A.3
  • 63
    • 0002109391 scopus 로고
    • Magnetic resonance studies of phospholipid-protein interactions in bilayers
    • G. Cevc, editor. Marcel Dekker, New York
    • Watts, A. 1993. Magnetic resonance studies of phospholipid-protein interactions in bilayers. In Phospholipid Handbook. G. Cevc, editor. Marcel Dekker, New York. 687-741.
    • (1993) Phospholipid Handbook , pp. 687-741
    • Watts, A.1
  • 64
  • 65
    • 0028952293 scopus 로고
    • Membrane domains containing phosphatidylserine and substrate can be important for the activation of protein kinase C
    • Yang, L., and M. Glaser. 1994. Membrane domains containing phosphatidylserine and substrate can be important for the activation of protein kinase C. Biochemistry. 34:1500-1506.
    • (1994) Biochemistry , vol.34 , pp. 1500-1506
    • Yang, L.1    Glaser, M.2
  • 66
    • 0028950310 scopus 로고
    • Peptide models of helical hydrophobic transmembrane segments of membrane proteins. 2. Differential scanning calorimetry and FTIR spectroscopic studies of the interaction of Ac-K2-(LA)12-K2-amide with phosphatidylcholine membranes
    • Zhang, Y.-P., R. N. A. H. Lewis, R. S. Hodges, and R. N. McElhaney. 1995. Peptide models of helical hydrophobic transmembrane segments of membrane proteins. 2. Differential scanning calorimetry and FTIR spectroscopic studies of the interaction of Ac-K2-(LA)12-K2-amide with phosphatidylcholine membranes. Biochemistry. 34:2362-2371
    • (1995) Biochemistry , vol.34 , pp. 2362-2371
    • Zhang, Y.-P.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4
  • 68
    • 0010804078 scopus 로고
    • Effect of intermonolayer coupling on the phase behavior of lipid bilayers
    • Zhang, Z., M. J. Zuckermann, and O. G. Mouritsen. 1992. Effect of intermonolayer coupling on the phase behavior of lipid bilayers. Phys. Rev. A. 46:6707-6713.
    • (1992) Phys. Rev. A , vol.46 , pp. 6707-6713
    • Zhang, Z.1    Zuckermann, M.J.2    Mouritsen, O.G.3
  • 69
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • Zimm, B. H., and J. K. Bragg. 1959. Theory of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31:526-535.
    • (1959) J. Chem. Phys. , vol.31 , pp. 526-535
    • Zimm, B.H.1    Bragg, J.K.2


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