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Volumn 28, Issue 25, 2012, Pages 9475-9486

On the molecular mechanism of stabilization of proteins by cosolvents: Role of Lifshitz electrodynamic forces

Author keywords

[No Author keywords available]

Indexed keywords

BOVINE SERUM ALBUMINS; COSOLVENTS; DIELECTRIC SUSCEPTIBILITY; ELECTRODYNAMIC FORCES; ELECTRODYNAMIC INTERACTION; EXPERIMENTAL OBSERVATION; FAR ULTRAVIOLET; HYDRATION SHELL; HYDROGEN-BONDED STRUCTURES; MOLECULAR MECHANISM; NONIONIC; PROTEIN SURFACE; ROLE OF WATER; SEPARATION DISTANCES; STRUCTURAL STABILITIES; THERMAL DENATURATIONS; THREE-BODY INTERACTION; WATER STRUCTURE;

EID: 84862881149     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la300953n     Document Type: Article
Times cited : (16)

References (66)
  • 1
    • 0023505188 scopus 로고
    • Thermal stability of proteins in the presence of poly(ethylene glycols)
    • Lee, L.L.-Y.; Lee, L. C. Thermal stability of proteins in the presence of poly(ethylene glycols) Biochemistry 1987, 26, 7813-7819
    • (1987) Biochemistry , vol.26 , pp. 7813-7819
    • Lee, L.L.-Y.1    Lee, L.C.2
  • 2
    • 0018789680 scopus 로고
    • Increased thermal stability of proteins in the presence of sugars and polyols
    • Beck, J. F.; Oakenfull, D.; Smith, M. B. Increased thermal stability of proteins in the presence of sugars and polyols Biochemistry 1979, 23, 5191-5196
    • (1979) Biochemistry , vol.23 , pp. 5191-5196
    • Beck, J.F.1    Oakenfull, D.2    Smith, M.B.3
  • 3
    • 0038374325 scopus 로고    scopus 로고
    • Why is trehalose an exceptional protein stabilizer
    • Kaoushik, J. K.; Bhat, R. Why is trehalose an exceptional protein stabilizer J. Biol. Chem. 2003, 278, 26458-26465
    • (2003) J. Biol. Chem. , vol.278 , pp. 26458-26465
    • Kaoushik, J.K.1    Bhat, R.2
  • 4
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa, T.; Timasheff, S. N. Stabilization of protein structure by sugars Biochemistry 1982, 21, 6536-6544
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 5
    • 0019872622 scopus 로고
    • Stabilization of protein structure by sugars
    • Gekko, K.; Timasheff, S. N. Stabilization of protein structure by sugars Biochemistry 1981, 20, 4667-4676
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 6
    • 0024613305 scopus 로고
    • Influence of protein conformation on its adaptability under chaotropic conditions
    • Damodaran, S. Influence of protein conformation on its adaptability under chaotropic conditions Intl. J. Biol. Macromol. 1989, 11, 2-8
    • (1989) Intl. J. Biol. Macromol. , vol.11 , pp. 2-8
    • Damodaran, S.1
  • 7
    • 0017623134 scopus 로고
    • Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series
    • DOI 10.1016/0003-9861(77)90434-9
    • Melander, W.; Horvath, C. Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic seris Arch. Biochem. Biophys. 1977, 183, 200-215 (Pubitemid 8200028)
    • (1977) Archives of Biochemistry and Biophysics , vol.183 , Issue.1 , pp. 200-215
    • Melander, W.1    Horvath, C.2
  • 8
    • 0019026145 scopus 로고
    • Protein solubility and the lyotropic series of ions
    • Bull, H. B.; Breeze, K. Protein solubility and the lyotropic series of ions Arch. Biochem. Biophys. 1980, 202, 116-120
    • (1980) Arch. Biochem. Biophys. , vol.202 , pp. 116-120
    • Bull, H.B.1    Breeze, K.2
  • 9
    • 0022032982 scopus 로고
    • The stabilization of proteins by osmolytes
    • Arakawa, T.; Timasheff, S. N. The stabilization of proteins by osmolytes Biophys. J. 1985, 47, 411-414
    • (1985) Biophys. J. , vol.47 , pp. 411-414
    • Arakawa, T.1    Timasheff, S.N.2
  • 10
    • 0028618410 scopus 로고
    • Contribution of the surface free energy perturbation to protein-solvent interactions
    • Kita, Y.; Arakawa, T.; Lin, T.-Y.; Timasheff, S. N. Contribution of the surface free energy perturbation to protein-solvent interactions Biochemistry 1994, 33, 15178-15189
    • (1994) Biochemistry , vol.33 , pp. 15178-15189
    • Kita, Y.1    Arakawa, T.2    Lin, T.-Y.3    Timasheff, S.N.4
  • 11
    • 0001440224 scopus 로고    scopus 로고
    • Effect of surface tension on the stability of heat-stressed proteins: A molecular thermodynamic interpretation
    • Cioci, F. Effect of surface tension on the stability of heat-stressed proteins: A molecular thermodynamic interpretation J. Phys. Chem. 1996, 100, 17400-17405 (Pubitemid 126790128)
    • (1996) Journal of Physical Chemistry , vol.100 , Issue.43 , pp. 17400-17405
    • Cioci, F.1
  • 13
    • 34249830163 scopus 로고    scopus 로고
    • Hofmeister salt effects on surface tension arise from partitioning of anions and cations between bulk water and the air-water interface
    • DOI 10.1021/jp070245z
    • Pegram, L. M.; Record, M. T. Hofmeister salt effects on surface tension arise from partitioning of anions and cations between bulk water and the air-water interface J. Phys. Chem. 2007, 111, 5411-5417 (Pubitemid 46854534)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.19 , pp. 5411-5417
    • Pegram, L.M.1    Record Jr., M.T.2
  • 14
    • 0013807126 scopus 로고
    • On the conformational stability of globular proteins. The effects of various electrolytes and nonelectrolytes on the thermal ribonuclease transition
    • Von Hippel, P. H.; Wong, K. Y. On the conformational stability of globular proteins. The effects of various electrolytes and nonelectrolytes on the thermal ribonuclease transition J. Biol. Chem. 1965, 240, 3909-3023
    • (1965) J. Biol. Chem. , vol.240 , pp. 3909-3023
    • Von Hippel, P.H.1    Wong, K.Y.2
  • 15
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin, R. L. How Hofmeister ion interactions affect protein stability Biophys. J. 1996, 71, 2056-2063 (Pubitemid 26325984)
    • (1996) Biophysical Journal , vol.71 , Issue.4 , pp. 2056-2063
    • Baldwin, R.L.1
  • 16
    • 0029037128 scopus 로고
    • Thermostabilization of erythrocyte carbonic anhydrase by polyhydric additives
    • Cioci, F. Thermostabilization of erythrocyte carbonic anhydrase by polyhydric additives Enzy. Microb. Technol. 1995, 17, 592-600
    • (1995) Enzy. Microb. Technol. , vol.17 , pp. 592-600
    • Cioci, F.1
  • 17
    • 84945064021 scopus 로고
    • Three-body dispersion forces
    • McLachlan, A. D. Three-body dispersion forces Mol. Phys. 1963, 6, 423-427
    • (1963) Mol. Phys. , vol.6 , pp. 423-427
    • McLachlan, A.D.1
  • 18
    • 33845451534 scopus 로고
    • Effect of the medium on dispersion forces in fluids
    • McLachlan, A. D. Effect of the medium on dispersion forces in fluids Faraday Soc. 1965, 40, 239-245
    • (1965) Faraday Soc. , vol.40 , pp. 239-245
    • McLachlan, A.D.1
  • 20
    • 0015709940 scopus 로고
    • Van der Waals forces in biological systems
    • Israelachvili, J. van der Waals forces in biological systems Q. Rev. Biophys. 1974, 6, 341-387
    • (1974) Q. Rev. Biophys. , vol.6 , pp. 341-387
    • Israelachvili, J.1
  • 21
    • 27744603532 scopus 로고
    • In; Lee, L. H. Gordon and Breach Science Publishers: London
    • Parsegian, V. A.; Gingell, D. In Recent Advances in Adhesion; Lee, L. H., Ed.; Gordon and Breach Science Publishers: London, 1973; pp 153-192.
    • (1973) Recent Advances in Adhesion , pp. 153-192
    • Parsegian, V.A.1    Gingell, D.2
  • 22
    • 0031190402 scopus 로고    scopus 로고
    • Hamaker constants of inorganic materials
    • PII S0001868697000031
    • Bergstrom, L. Hamaker constants of inorganic materials Advan. Colloid Interface Sci. 1997, 70, 125-169 (Pubitemid 127403555)
    • (1997) Advances in Colloid and Interface Science , vol.70 , Issue.1-3 , pp. 125-169
    • Bergstrom, L.1
  • 23
    • 0030031382 scopus 로고    scopus 로고
    • Van der Waals interactions involving proteins
    • Roth, C. M.; Neal, B. L.; Lenhoff, A. M. Van der Waals interactions involving proteins Biophys. J. 1996, 70, 977-987 (Pubitemid 26028312)
    • (1996) Biophysical Journal , vol.70 , Issue.2 , pp. 977-987
    • Roth, C.M.1    Neal, B.L.2    Lenhoff, A.M.3
  • 25
    • 0041957096 scopus 로고
    • Polarized vacuum ultraviolet spectra of crystalline urea
    • Campbell, B. F.; Clark, L. B. Polarized vacuum ultraviolet spectra of crystalline urea J. Am. Chem. Soc. 1989, 111, 8131-8136
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 8131-8136
    • Campbell, B.F.1    Clark, L.B.2
  • 26
    • 33646456769 scopus 로고
    • The absorption spectra of amino acids in the region two hundred to two hundred and thirty millimicrons
    • Saidel, L. J.; Goldfarb, R.; Waldman, S. The absorption spectra of amino acids in the region two hundred to two hundred and thirty millimicrons J. Biol. Chem. 1952, 197, 285-291
    • (1952) J. Biol. Chem. , vol.197 , pp. 285-291
    • Saidel, L.J.1    Goldfarb, R.2    Waldman, S.3
  • 27
    • 0039000616 scopus 로고
    • The infrared spectra of some amino acids
    • Leifer, A.; Lippincott, E. R. The infrared spectra of some amino acids J. Am. Chem. Soc. 1957, 79, 5098-5101
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 5098-5101
    • Leifer, A.1    Lippincott, E.R.2
  • 28
    • 77949426811 scopus 로고    scopus 로고
    • Vibrational circular dichroism and IR absorption spectra of amino acids: A density functional study
    • Ji, Z.; Santamaria, R.; Garizon, I. L. Vibrational circular dichroism and IR absorption spectra of amino acids: A density functional study J. Phys. Chem. A 2010, 114, 3591-3601
    • (2010) J. Phys. Chem. A , vol.114 , pp. 3591-3601
    • Ji, Z.1    Santamaria, R.2    Garizon, I.L.3
  • 30
    • 0012264316 scopus 로고    scopus 로고
    • Femtosecond photoionization of ion beam desorbed aliphatic and aromatic amino acids: Fragmentation via α-cleavage reactions
    • Vorsa, V.; Kono, T.; Willey, K. F.; Winograd, N. Femtosecond photoionization of ion beam desorbed aliphatic and aromatic amino acids: Fragmentation via α-cleavage reactions J. Phys. Chem. B 1999, 103, 7889-7895
    • (1999) J. Phys. Chem. B , vol.103 , pp. 7889-7895
    • Vorsa, V.1    Kono, T.2    Willey, K.F.3    Winograd, N.4
  • 31
    • 77951472750 scopus 로고    scopus 로고
    • Part 3: Theoretical study on some amino acids and their potential activity as corrosion inhibitors for mild steel in HCl
    • Eddy, N. O. Part 3: Theoretical study on some amino acids and their potential activity as corrosion inhibitors for mild steel in HCl Molec. Simul. 2010, 36, 354-363
    • (2010) Molec. Simul. , vol.36 , pp. 354-363
    • Eddy, N.O.1
  • 32
    • 80052139437 scopus 로고    scopus 로고
    • Effects of alkyl side chains on properties of aliphatic amino acids probed using quantum chemical calculations
    • Ganesan, A.; Wang, F.; Brunger, M.; Prince, K. Effects of alkyl side chains on properties of aliphatic amino acids probed using quantum chemical calculations J. Synchrotron Rad. 2011, 18, 733-742
    • (2011) J. Synchrotron Rad. , vol.18 , pp. 733-742
    • Ganesan, A.1    Wang, F.2    Brunger, M.3    Prince, K.4
  • 33
    • 0015418232 scopus 로고
    • Optical properties of liquid glycerol in the vacuum ultraviolet
    • Heller, J. M.; Brikhoff, R. D.; Williams, M. W.; Painter, L. R. Optical properties of liquid glycerol in the vacuum ultraviolet Radiat. Res. 1972, 52, 25-31
    • (1972) Radiat. Res. , vol.52 , pp. 25-31
    • Heller, J.M.1    Brikhoff, R.D.2    Williams, M.W.3    Painter, L.R.4
  • 34
    • 0042992138 scopus 로고
    • The internal energy of sputtered glycerol molecules, determined by photoionization mass spectrometry
    • Hoogerbrugge, R.; Bobeldijk, M.; Kistemaker, P. G.; Los, J. The internal energy of sputtered glycerol molecules, determined by photoionization mass spectrometry J. Phys. Chem. 1988, 88, 5314-5322
    • (1988) J. Phys. Chem. , vol.88 , pp. 5314-5322
    • Hoogerbrugge, R.1    Bobeldijk, M.2    Kistemaker, P.G.3    Los, J.4
  • 35
    • 0014685923 scopus 로고
    • Application of the Lifshitz theory to the calculation of van der Waals forces across thin lipid films
    • Parsegian, V. A.; Ninham, B. W. Application of the Lifshitz theory to the calculation of van der Waals forces across thin lipid films Nature 1969, 224, 1197-1198
    • (1969) Nature , vol.224 , pp. 1197-1198
    • Parsegian, V.A.1    Ninham, B.W.2
  • 36
    • 0019172574 scopus 로고
    • The calculation of Hamaker constants from Lifshitz theory with applications to wetting phenomena
    • Hough, D. B.; White, L. R. The calculation of Hamaker constants from Lifshitz theory with applications to wetting phenomena Adv. Colloid Interface Sci. 1980, 14, 3-41
    • (1980) Adv. Colloid Interface Sci. , vol.14 , pp. 3-41
    • Hough, D.B.1    White, L.R.2
  • 39
    • 26544476885 scopus 로고
    • Interfacial Lifshitz-van der Waals and polar interactions in macroscopic systems
    • Van Oss, C. J.; Chaudhury, M. K.; Good, R. J. Interfacial Lifshitz-van der Waals and polar interactions in macroscopic systems Chem. Rev. 1988, 88, 927-941
    • (1988) Chem. Rev. , vol.88 , pp. 927-941
    • Van Oss, C.J.1    Chaudhury, M.K.2    Good, R.J.3
  • 40
    • 0032180018 scopus 로고    scopus 로고
    • Role of dispersion interactions in the adsorption of proteins at oil-water and air-water interfaces
    • Sengupta, T.; Damodaran, S. Role of dispersion interactions in the adsorption of proteins at oil-water and air-water interfaces Langmuir 1998, 14, 6457-6469 (Pubitemid 128633883)
    • (1998) Langmuir , vol.14 , Issue.22 , pp. 6457-6469
    • Sengupta, T.1    Damodaran, S.2
  • 43
    • 0012406543 scopus 로고
    • Studies of the dielectric properties of protein solutions. II. The water-soluble proteins of normal horse serum
    • Ferry, J. D.; Oncley, J. L. Studies of the dielectric properties of protein solutions. II. The water-soluble proteins of normal horse serum J. Am. Chem. Soc. 1938, 60, 1123-1132
    • (1938) J. Am. Chem. Soc. , vol.60 , pp. 1123-1132
    • Ferry, J.D.1    Oncley, J.L.2
  • 45
    • 0000825079 scopus 로고
    • Dielectric increments and the conformations of amino acids and betaines in water
    • Kirchnerova, J.; Farrell, P. G.; Edward, J. T. Dielectric increments and the conformations of amino acids and betaines in water J. Phys. Chem. 1976, 80, 1974-1980
    • (1976) J. Phys. Chem. , vol.80 , pp. 1974-1980
    • Kirchnerova, J.1    Farrell, P.G.2    Edward, J.T.3
  • 46
    • 0020477047 scopus 로고
    • Preferential interactions of proteins with salts in concentrated solutions
    • Arakawa, T.; Timasheff, S. N. Preferential interactions of proteins with salts in concentrated solutions Biochemistry 1982, 21, 6545-6552
    • (1982) Biochemistry , vol.21 , pp. 6545-6552
    • Arakawa, T.1    Timasheff, S.N.2
  • 48
    • 0028150954 scopus 로고
    • Why do some organisms use a urea-methylamine mixture as osmolyte? Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein
    • DOI 10.1021/bi00208a021
    • Lin, T.-Y.; Timasheff, S. N. Why do some organisms use a urea-methylamine mixture as osmolyte? Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein Biochemistry 1994, 33, 12695-12701 (Pubitemid 24345902)
    • (1994) Biochemistry , vol.33 , Issue.42 , pp. 12695-12701
    • Lin, T.-Y.1    Timasheff, S.N.2
  • 49
    • 51149214905 scopus 로고
    • Raman spectral studies of the effects of urea and sucrose on water structure
    • Walrafen, G. E. Raman spectral studies of the effects of urea and sucrose on water structure J. Chem. Phys. 1966, 44, 3726-3727
    • (1966) J. Chem. Phys. , vol.44 , pp. 3726-3727
    • Walrafen, G.E.1
  • 50
    • 73349101519 scopus 로고    scopus 로고
    • Osmolyte-induced perturbations of hydrogen bonding between hydration layer waters: Correlation with protein conformational changes
    • Guo, F.; Friedman, J. M. Osmolyte-induced perturbations of hydrogen bonding between hydration layer waters: Correlation with protein conformational changes J. Phys. Chem. B 2009, 113, 16632-16642
    • (2009) J. Phys. Chem. B , vol.113 , pp. 16632-16642
    • Guo, F.1    Friedman, J.M.2
  • 52
    • 0141560450 scopus 로고    scopus 로고
    • Impact of urea on water structure: A clue to its properties as a denaturant?
    • DOI 10.1016/S0301-4622(03)00095-4
    • Soper, A. K.; Castner, E. W.; Luzar, A. Impact of urea on water structure: a clue to its properties as a denaturant? Biophys. Chem. 2003, 105, 649-666 (Pubitemid 37123089)
    • (2003) Biophysical Chemistry , vol.105 , Issue.2-3 , pp. 649-666
    • Soper, A.K.1    Castner, E.W.2    Luzar, A.3
  • 53
    • 0014354873 scopus 로고
    • Fluorescence spectroscopy of proteins
    • Stryer, L. Fluorescence spectroscopy of proteins Science 1968, 162, 526-533
    • (1968) Science , vol.162 , pp. 526-533
    • Stryer, L.1
  • 54
    • 0017661379 scopus 로고
    • Conjugated polyene fatty acids as fluorescent probes: Binding to bovine serum albumin
    • Sklar, L. A.; Hudson, B. S.; Simoni, R. D. Conjugated polyene fatty acids as fluorescent probes: Binging to bovine serum albumin Biochemistry 1977, 5100-5108 (Pubitemid 8222204)
    • (1977) Biochemistry , vol.16 , Issue.23 , pp. 5100-5108
    • Sklar, L.A.1    Hudson, B.S.2    Simoni, R.D.3
  • 55
    • 84985668665 scopus 로고
    • Effect of poly(ethylene glycol) on protein denaturation and model compound pKa's
    • Knoll, D; Hermans, J. Effect of poly(ethylene glycol) on protein denaturation and model compound pKa's Biopolymers 1981, 20, 1747-1750
    • (1981) Biopolymers , vol.20 , pp. 1747-1750
    • Knoll, D.1    Hermans, J.2
  • 56
    • 0022381773 scopus 로고
    • Mechanism of poly(ethylene glycol) interaction with proteins
    • DOI 10.1021/bi00345a005
    • Arakawa, T.; Timasheff, S. N. Mechanism of poly(ethylene glycol) interaction of proteins Biochemistry 1985, 24, 6756-6762 (Pubitemid 16170203)
    • (1985) Biochemistry , vol.24 , Issue.24 , pp. 6756-6762
    • Arakawa, T.1    Timasheff, S.N.2
  • 57
    • 0030932504 scopus 로고    scopus 로고
    • Destabilization of human serum albumin by polyethylene glycols studied by thermodynamical equilibrium and kinetic approaches
    • DOI 10.1016/S0141-8130(96)01150-6, PII S0141813096011506
    • Farrugia, B.; Garcia, G.; D'Angelo, S.; Pico, G. Destabilization of human serum albumin by polyethylene glycols as studied by thermodynamic equilibrium and kinetic approaches Int. J. Biol. Maacromol. 1997, 20, 43-51 (Pubitemid 27168657)
    • (1997) International Journal of Biological Macromolecules , vol.20 , Issue.1 , pp. 43-51
    • Farruggia, B.1    Garcia, G.2    D'Angelo, C.3    Pico, G.4
  • 59
    • 0019877808 scopus 로고
    • Mechanism of precipitation of proteins by polyethylene glycols: Analysis in terms of excluded volume
    • Atha, D. H.; Ingham, K. C. Mechanism of precipitation of proteins by polyethylene glycols: Analysis in terms of excluded volume J. Biol. Chem. 1981, 256, 12108-12117
    • (1981) J. Biol. Chem. , vol.256 , pp. 12108-12117
    • Atha, D.H.1    Ingham, K.C.2
  • 60
    • 0022286246 scopus 로고
    • Use of polyethylene glocol in the crystallization of macromolecules
    • McPherson, A. Use of polyethylene glocol in the crystallization of macromolecules Methods Enzymol. 1985, 114, 120-124
    • (1985) Methods Enzymol. , vol.114 , pp. 120-124
    • McPherson, A.1
  • 61
    • 0347994108 scopus 로고    scopus 로고
    • Protein folding by the effects of macromolecular crowding
    • DOI 10.1110/ps.03288104
    • Tokuriki, N.; Kinjo, M.; Negi, S.; Hoshino, M.; Goto, Y.; Urabe, I.; Yomo, T. Protein folding by the effects of macromolecular crowding Protein Sci. 2004, 13, 125-133 (Pubitemid 38021147)
    • (2004) Protein Science , vol.13 , Issue.1 , pp. 125-133
    • Tokuriki, N.1    Kinjo, M.2    Negi, S.3    Hoshino, M.4    Goto, Y.5    Urabe, I.6    Yomo, T.7
  • 62
    • 0000557280 scopus 로고
    • Indirect evidence for hydration forces in the deposition of polystyrene latex colloids on glass surfaces
    • Ellmelech, M. Indirect evidence for hydration forces in the deposition of polystyrene latex colloids on glass surfaces J. Chem. Soc. Faraday Trans. 1990, 86, 1623-1624
    • (1990) J. Chem. Soc. Faraday Trans. , vol.86 , pp. 1623-1624
    • Ellmelech, M.1
  • 63
    • 84855877079 scopus 로고    scopus 로고
    • Hydration energy or hydration force? Origin of ion-specificity in ion selective electrodes
    • Wojciechowski, K. Hydration energy or hydration force? Origin of ion-specificity in ion selective electrodes Curr. Opin. Colliod Interface Sci. 2011, 16, 601-606
    • (2011) Curr. Opin. Colliod Interface Sci. , vol.16 , pp. 601-606
    • Wojciechowski, K.1
  • 64
    • 0019634384 scopus 로고
    • The concept of negative Hamaker coefficients. 1. History and present status
    • DOI 10.1016/0001-8686(81)80007-3
    • Visser, J. The concept of negative Hamaker coefficients. 1. History and present status Adv. Colloid Interface Sci. 1981, 15, 157-169 (Pubitemid 12465993)
    • (1981) Advances in Colloid and Interface Science , vol.15 , Issue.2 , pp. 157-169
    • Visser, J.1
  • 65
    • 0002639386 scopus 로고
    • Interactions in aqueous solution
    • Scheraga, H. A. Interactions in aqueous solution Acc. Chem. Res. 1979, 12, 7-14
    • (1979) Acc. Chem. Res. , vol.12 , pp. 7-14
    • Scheraga, H.A.1
  • 66
    • 1442288296 scopus 로고    scopus 로고
    • Osmotic coefficients and surface tension of aqueous electrolyte solutions: Role of dispersion forces
    • Kunz, W.; Belloni, L.; Bernard, O.; Ninham, B. W. Osmotic coefficients and surface tension of aqueous electrolyte solutions: Role of dispersion forces J. Phys. Chem. B 2004, 108, 2398-2404
    • (2004) J. Phys. Chem. B , vol.108 , pp. 2398-2404
    • Kunz, W.1    Belloni, L.2    Bernard, O.3    Ninham, B.W.4


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