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Volumn 10, Issue 8, 2009, Pages 3283-3315

Isothermal microcalorimetry to investigate non specific interactions in biophysical chemistry

Author keywords

Isothermal titration calorimetry; Non specific interactions

Indexed keywords

AMPHOPHILE; DNA; POLYELECTROLYTE;

EID: 69549116018     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms10083283     Document Type: Review
Times cited : (70)

References (161)
  • 1
    • 33645319676 scopus 로고    scopus 로고
    • Overcoming roadblocks in lead optimization: A thermodynamic perspective
    • DOI 10.1111/j.1747-0285.2005.00314.x
    • Ruben, A.J.; Kiso, Y.; Freire, E. Overcomming roadblocks in lead optimization:a thermodynamic perspective. Chem. Biol. Drug Des. 2006, 67, 2-4. (Pubitemid 43881382)
    • (2006) Chemical Biology and Drug Design , vol.67 , Issue.1 , pp. 2-4
    • Ruben, A.J.1    Kiso, Y.2    Freire, E.3
  • 3
    • 69549089294 scopus 로고    scopus 로고
    • Thermodynamic dissection of cooperativity in ligand recognition
    • Oxford University Press: New York, NY, USA, Chapter 2
    • Rose, T.; di Cera, E. Thermodynamic dissection of cooperativity in ligand recognition. In Thermodynamics in Biology. Oxford University Press: New York, NY, USA, 2000; Chapter 2.
    • (2000) Thermodynamics in Biology
    • Rose, T.1    Di Cera, E.2
  • 6
    • 60949096805 scopus 로고    scopus 로고
    • Quest for ion-ion correlations in electric double layers and overcharging phenomena
    • Lyklema, J. Quest for ion-ion correlations in electric double layers and overcharging phenomena. Adv. Colloid Interface Sci. 2009, 147-148, 205-213.
    • (2009) Adv. Colloid Interface Sci. , vol.147-148 , pp. 205-213
    • Lyklema, J.1
  • 7
    • 43849094337 scopus 로고    scopus 로고
    • Adsorption and polymerization of amino acids on mineral surfaces: A review
    • Lambert, J.-F. Adsorption and polymerization of amino acids on mineral surfaces: a review. Origins Life Evol. Biosphere 2008, 38, 211-242.
    • (2008) Origins Life Evol. Biosphere , vol.38 , pp. 211-242
    • Lambert, J.-F.1
  • 9
    • 0002443506 scopus 로고
    • Electrical double layer on silver iodide. Influence of temperature and application to sol stability
    • Lyklema, J. Electrical double layer on silver iodide. Influence of temperature and application to sol stability. Discuss. Faraday Soc. 1966, 42, 81-90.
    • (1966) Discuss. Faraday Soc. , vol.42 , pp. 81-90
    • Lyklema, J.1
  • 10
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • Manning, G.S.Q. The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Rev. Biophys. 1978, 11,179-246.
    • (1978) Rev. Biophys. , vol.11 , pp. 179-246
    • Manning, G.S.Q.1
  • 12
    • 0242386506 scopus 로고    scopus 로고
    • Binding Affinities of Host-Guest, Protein-Ligand, and Protein-Transition-State Complexes
    • DOI 10.1002/anie.200200565
    • Houk, K.N.; Leach, A.G.; Kim, S.P.; Zhang, X. Binding affinities of host-guest, protein-ligand, and protein-transition state complexes. Angew. Chem. Int. Ed. 2003, 42, 4872-4897. (Pubitemid 37345385)
    • (2003) Angewandte Chemie - International Edition , vol.42 , Issue.40 , pp. 4872-4897
    • Houk, K.N.1    Leach, A.G.2    Kim, S.P.3    Zhang, X.4
  • 13
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones, S.; Thornton, J.M. Principles of protein-protein interactions. Proc. Natl. Acad. Sci. 1996, 93, 13-20.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 15
    • 1642574267 scopus 로고    scopus 로고
    • 2-aqueous solution interface from low ionic strength solution
    • 2-aqueous solution interface from low ionic strength solution. Colloids Surf., B: Biointerfaces 2004, 33, 129-142.
    • (2004) Colloids Surf., B: Biointerfaces , vol.33 , pp. 129-142
    • Ball, V.1
  • 16
    • 66249119965 scopus 로고    scopus 로고
    • Molecular simulation of protein-surface interactions: Benefits, problems, solutions, and future directions
    • Latour, R.A. Molecular simulation of protein-surface interactions: Benefits, problems, solutions, and future directions. Biointerphases 2008, 3, FC2-FC12.
    • (2008) Biointerphases , vol.3
    • Latour, R.A.1
  • 17
    • 0000472045 scopus 로고    scopus 로고
    • From random sequential adsorption to ballistic deposition: A general view of irreversible deposition processes
    • Schaaf, P.; Voegel, J.-C.; Senger, B. From random sequential adsorption to ballistic deposition: a general view of irreversible deposition processes. J. Phys. Chem. B 2000, 104, 2204-2214.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 2204-2214
    • Schaaf, P.1    Voegel, J.-C.2    Senger, B.3
  • 18
    • 0001586373 scopus 로고
    • Hydrophobicity of long chain n-alkyl carboxylic acids, as measured by their distribution between heptane and aqueous solutions
    • Smith, R.; Tanford, C. Hydrophobicity of long chain n-alkyl carboxylic acids, as measured by their distribution between heptane and aqueous solutions. Proc. Natl. Acad. Sci. USA. 1973, 70, 289-293.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 289-293
    • Smith, R.1    Tanford, C.2
  • 19
    • 33644918294 scopus 로고    scopus 로고
    • Simple thermodynamics for unravelling sophisticated selfassembly processes
    • Hamacek, J.; Borkovec, M.; Piguet, C. Simple thermodynamics for unravelling sophisticated selfassembly processes. Dalton Trans. 2006, 12, 1473-1490.
    • (2006) Dalton Trans , vol.12 , pp. 1473-1490
    • Hamacek, J.1    Borkovec, M.2    Piguet, C.3
  • 20
    • 4243778369 scopus 로고    scopus 로고
    • Complexation thermodynamics of cyclodextrins
    • Rekharsky, M.V.; Inoue, Y. Complexation thermodynamics of cyclodextrins. Chem Rev. 1998, 98, 1875-1918. (Pubitemid 128633440)
    • (1998) Chemical Reviews , vol.98 , Issue.5 , pp. 1875-1917
    • Rekharsky, M.V.1    Inoue, Y.2
  • 21
    • 0032901515 scopus 로고    scopus 로고
    • Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition
    • Jelesarov, I.; Bosshard, H.R. Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J. Mol. Recognit. 1999, 12, 3-18.
    • (1999) J. Mol. Recognit. , vol.12 , pp. 3-18
    • Jelesarov, I.1    Bosshard, H.R.2
  • 25
    • 0030913948 scopus 로고    scopus 로고
    • Use of surface plasmon resonance to probe the equilibrium and dynamic aspects of interactions between biological macromolecules
    • DOI 10.1146/annurev.biophys.26.1.541
    • Schuck. P. Use of surface plasmon resonance to probe the equilibrium and dynamic aspects of interactions between biological macromolecules. Annu. Rev. Biophys. Biomol. Struct. 1997, 26, 541-566. (Pubitemid 27255383)
    • (1997) Annual Review of Biophysics and Biomolecular Structure , vol.26 , pp. 541-566
    • Schuck, P.1
  • 26
    • 33748953157 scopus 로고    scopus 로고
    • Interpretation of the temperature dependence of equilibrium and rate constants
    • DOI 10.1002/jmr.799
    • Winzor, D.J.; Jackson, C.M. Interpretation of the temperature dependence of equilibrium and rate constants. J. Mol. Recognit. 2006, 19, 389-407. (Pubitemid 44437530)
    • (2006) Journal of Molecular Recognition , vol.19 , Issue.5 , pp. 389-407
    • Winzor, D.J.1    Jackson, C.M.2
  • 27
    • 0028805495 scopus 로고
    • Significant discrepancies between van't Hoff and calorimetric enthalpies
    • Liu, Y.; Sturtevant, J.M. Significant discrepancies between van't Hoff and calorimetric enthalpies. Protein Sci. 1995, 4, 2559-2561.
    • (1995) Protein Sci , vol.4 , pp. 2559-2561
    • Liu, Y.1    Sturtevant, J.M.2
  • 28
    • 0017295455 scopus 로고
    • Thermodynamic investigations of proteins. II. Calorimetric study of lysozyme denatured by guanidinium hydrochmoride
    • Pfeil, W.; Privalov, P.L. Thermodynamic investigations of proteins. II. Calorimetric study of lysozyme denatured by guanidinium hydrochmoride. Biophys. Chem. 1976, 4, 33-40.
    • (1976) Biophys. Chem. , vol.4 , pp. 33-40
    • Pfeil, W.1    Privalov, P.L.2
  • 30
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann, W. Some factors in the interpretation of protein denaturation. Adv. Protein Chem. 1959, 14, 1-63.
    • (1959) Adv. Protein Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 33
    • 33749238188 scopus 로고    scopus 로고
    • Contribution of ligand desolvation to binding thermodynamics in a ligand-protein interaction
    • Shimokhina, N.; Bronowska, A.; Homans, S.W. Contribution of ligand desolvation to binding thermodynamics in a ligand-protein interaction. Angew. Chem. Int. Ed. 2006, 45, 6374-6376.
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 6374-6376
    • Shimokhina, N.1    Bronowska, A.2    Homans, S.W.3
  • 35
    • 0141522976 scopus 로고    scopus 로고
    • Uses of enthalpy-entropy compensation in protein research
    • DOI 10.1016/S0301-4622(03)00065-6
    • Lumry, R. Uses of enthalpy-entropy compensation in protein research. Biophys. Chem. 2003, 105, 545-557. (Pubitemid 37123083)
    • (2003) Biophysical Chemistry , vol.105 , Issue.2-3 , pp. 545-557
    • Lumry, R.1
  • 36
    • 0034710405 scopus 로고    scopus 로고
    • A calorimetric study of phospholipid hydration. Simultaneous monitoring of enthalpy and free energy
    • Markova, N.; Sparr, E.; Wadsö, L.; Wennerström, H. A calorimetric study of phospholipid hydration. Simultaneous monitoring of enthalpy and free energy. J. Phys. Chem. B 2000, 104, 8053-8060.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 8053-8060
    • Markova, N.1    Sparr, E.2    Wadsö, L.3    Wennerström, H.4
  • 37
    • 0001541777 scopus 로고    scopus 로고
    • Flow adsorption microcalorimetry
    • Groszek, A.J. Flow adsorption microcalorimetry. Thermochim. Acta 1998, 312, 133-143.
    • (1998) Thermochim. Acta , vol.312 , pp. 133-143
    • Groszek, A.J.1
  • 38
    • 0002540421 scopus 로고
    • Adsorption calorimetry in surface chemistry
    • Fubini, B. Adsorption calorimetry in surface chemistry. Thermochim. Acta 1988, 135, 19-29.
    • (1988) Thermochim. Acta , vol.135 , pp. 19-29
    • Fubini, B.1
  • 39
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T.; Williston, S.; Brandts, J.-F.; Lin, L.-N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 1989, 179, 131-137.
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.-F.3    Lin, L.-N.4
  • 40
    • 0026052762 scopus 로고
    • Direct calorimetric analysis of the enzymic activity of yeast cytochrome c oxydase
    • Morin, P.E.; Freire, E. Direct calorimetric analysis of the enzymic activity of yeast cytochrome c oxydase. Biochemistry 1991, 30, 8494-8500.
    • (1991) Biochemistry , vol.30 , pp. 8494-8500
    • Morin, P.E.1    Freire, E.2
  • 41
    • 0035884687 scopus 로고    scopus 로고
    • Enzyme kinetics determined using calorimetry: A general assay for enzyme activity?
    • DOI 10.1006/abio.2001.5218
    • Todd, M.J.; Gomez, J. Enzyme kinetics determined using calorimetry: a general assay for enzyme activity? Anal. Biochem. 2001, 296, 179-187. (Pubitemid 32868499)
    • (2001) Analytical Biochemistry , vol.296 , Issue.2 , pp. 179-187
    • Todd, M.J.1    Gomez, J.2
  • 42
    • 44649201020 scopus 로고    scopus 로고
    • Enzymatic activity of immobilized enzyme determined by isothermal titration calorimetry
    • Henzler, K.; Haupt, B.; Ballauff, M. Enzymatic activity of immobilized enzyme determined by isothermal titration calorimetry. Anal. Biochem. 2008, 378, 184-189.
    • (2008) Anal. Biochem. , vol.378 , pp. 184-189
    • Henzler, K.1    Haupt, B.2    Ballauff, M.3
  • 43
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov, P.L.; Potekhin, S.A. Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods Enzymol. 1986, 131, 4-51.
    • (1986) Methods Enzymol , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 44
    • 0029198941 scopus 로고
    • Differential scanning calorimetry
    • Freire, E. Differential scanning calorimetry. Methods Mol. Biol. 1995, 40, 191-218.
    • (1995) Methods Mol. Biol. , vol.40 , pp. 191-218
    • Freire, E.1
  • 46
    • 0036498720 scopus 로고    scopus 로고
    • Determination of the volumetric properties of proteins and other solutes using pressure perturbation calorimetry
    • DOI 10.1006/abio.2001.5524
    • Lin, L.N.; Brandts, J.F.; Brandts, J.M.; Plotnikov, V. Determination of the volumetric properties of proteins and other solutes using pressure perturbation calorimetry. Anal. Biochem. 2002, 302, 144-160. (Pubitemid 34174621)
    • (2002) Analytical Biochemistry , vol.302 , Issue.1 , pp. 144-160
    • Lin, L.-N.1    Brandts, J.F.2    Brandts, J.M.3    Plotnikov, V.4
  • 47
    • 0017238490 scopus 로고
    • Compact form of DNA induced by spermidine
    • Gosule, L.C.; Schellman, J.A. Compact form of DNA induced by spermidine. Nature 1976, 259, 333-335.
    • (1976) Nature , vol.259 , pp. 333-335
    • Gosule, L.C.1    Schellman, J.A.2
  • 48
    • 0018803816 scopus 로고
    • Counterion-induced condensation of desoxyribonucleic acid: A light scattering study
    • Wilson, R.W.; Bloomfield, V.A. Counterion-induced condensation of desoxyribonucleic acid: a light scattering study. Biochemistry 1978, 18, 2192-2196.
    • (1978) Biochemistry , vol.18 , pp. 2192-2196
    • Wilson, R.W.1    Bloomfield, V.A.2
  • 49
    • 0031447208 scopus 로고    scopus 로고
    • DNA condensation by multivalent cations
    • Bloomfield, V.A. DNA condensation by multivalent cations. Biopolymers 1998, 44, 269-282.
    • (1998) Biopolymers , vol.44 , pp. 269-282
    • Bloomfield, V.A.1
  • 51
    • 0034607160 scopus 로고    scopus 로고
    • Vector unpacking as a potential barrier for receptor-mediated polyplex gene delivery
    • Schaffer, D.V.; Fidelman, N.A.; Dan, N.; Lauffenburger, D.A. Vector unpacking as a potential barrier for receptor-mediated polyplex gene delivery. Biotechnol. Bioeng. 2000, 67, 598-606.
    • (2000) Biotechnol. Bioeng. , vol.67 , pp. 598-606
    • Schaffer, D.V.1    Fidelman, N.A.2    Dan, N.3    Lauffenburger, D.A.4
  • 53
    • 0026763402 scopus 로고
    • Heparin-poly(ethylene glycol)-poly(vinyl alcohol) hydrogel: Preparation and assessment of thrombogenicity
    • Llanos, G.R.; Sefton, M.V. Heparin-poly(ethylene glycol)-poly(vinyl alcohol) hydrogel: preparation and assessment of thrombogenicity. Biomaterials 1992, 13, 421-424.
    • (1992) Biomaterials , vol.13 , pp. 421-424
    • Llanos, G.R.1    Sefton, M.V.2
  • 54
    • 0029251458 scopus 로고
    • Structures and stabilities of adsorbed proteins
    • Haynes, C.A.; Norde, W. Structures and stabilities of adsorbed proteins. J. Colloid Interface Sci. 1995, 169, 313-328.
    • (1995) J. Colloid Interface Sci. , vol.169 , pp. 313-328
    • Haynes, C.A.1    Norde, W.2
  • 55
    • 50049125588 scopus 로고    scopus 로고
    • Misfolding of the prion protein: Linking biophysical and biological approaches
    • Noinville, S.; Chich, J.F.; Rezaei, H. Misfolding of the prion protein: linking biophysical and biological approaches. Vet. Res. 2008, 39, 48.
    • (2008) Vet. Res. , vol.39 , pp. 48
    • Noinville, S.1    Chich, J.F.2    Rezaei, H.3
  • 56
    • 58149216444 scopus 로고    scopus 로고
    • Prorein Folding and misfolding on surfaces
    • Stefani, M. Prorein Folding and misfolding on surfaces. Int. J. Mol. Sci. 2008, 9, 2515-2542.
    • (2008) Int. J. Mol. Sci. , vol.9 , pp. 2515-2542
    • Stefani, M.1
  • 57
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C.M. Protein folding and misfolding. Nature 2003, 426, 884-891.
    • (2003) Nature , vol.426 , pp. 884-891
    • Dobson, C.M.1
  • 58
    • 0037040541 scopus 로고    scopus 로고
    • Protein folding. Molecular chaperones in the cytosol: From nascent chain to folded protein
    • DOI 10.1126/science.1068408
    • Hartl, F.U.; Hayer-Hartl, M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 2002, 295, 1852-1858. (Pubitemid 34214115)
    • (2002) Science , vol.295 , Issue.5561 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 59
    • 0018492276 scopus 로고
    • The variation of the critical micelle concentration of sodium dodecyl sulphate with ionic strength monitored by selective-ion membrane electrodes
    • Newbery, J.E. The variation of the critical micelle concentration of sodium dodecyl sulphate with ionic strength monitored by selective-ion membrane electrodes. Colloid Polym. Sci. 1979, 257, 773-775.
    • (1979) Colloid Polym. Sci. , vol.257 , pp. 773-775
    • Newbery, J.E.1
  • 60
    • 0020497371 scopus 로고
    • Calorimetric determination of the enthalpy of micelle formation in aqueous media
    • Birdi, K.S. Calorimetric determination of the enthalpy of micelle formation in aqueous media. Colloid Polym. Sci. 1983, 261, 45-48.
    • (1983) Colloid Polym. Sci. , vol.261 , pp. 45-48
    • Birdi, K.S.1
  • 61
    • 0030715273 scopus 로고    scopus 로고
    • Thermodynamics of the binding of a cationic lipid to DNA
    • DOI 10.1021/ja964324s
    • Spink, C.H.; Chaires J.B. Thermodynamics of the binding of a cationic lipid to DNA. J. Am. Chem. Soc. 1997, 119, 10920-10928. (Pubitemid 27528837)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.45 , pp. 10920-10928
    • Spink, C.H.1    Chaires, J.B.2
  • 64
    • 0025894585 scopus 로고
    • The effect of chemical structure upon the thermodynamics of micellization of model alkylarenesulfonates: III. Determination of the critical micelle concentration and the enthalpy of demicellization by means of microcalorimetry and a comparison with the phase separation model
    • van Os, N.; Daane, G.J.; Haandrikman, G. The effect of chemical structure upon the thermodynamics of micellization of model alkylarenesulfonates: III. Determination of the critical micelle concentration and the enthalpy of demicellization by means of microcalorimetry and a comparison with the phase separation model. J. Colloid Interface Sci. 1991, 141, 199-217.
    • (1991) J. Colloid Interface Sci. , vol.141 , pp. 199-217
    • Van Os, N.1    Daane, G.J.2    Haandrikman, G.3
  • 65
    • 0034176071 scopus 로고    scopus 로고
    • A titration microcalorimetric study of the effects of halide counterions on vesicle-forming aggregation in aqueous solution of branched chain alkylpyridinium surfactants
    • de Gooijer, J.M.; Engberts, J.B.F.N.; Blandamer, M.J. A titration microcalorimetric study of the effects of halide counterions on vesicle-forming aggregation in aqueous solution of branched chain alkylpyridinium surfactants. J. Colloid Interface Sci. 2000, 224, 4-10.
    • (2000) J. Colloid Interface Sci. , vol.224 , pp. 4-10
    • De Gooijer, J.M.1    Engberts, J.B.F.N.2    Blandamer, M.J.3
  • 66
    • 0035838779 scopus 로고    scopus 로고
    • A look at the thermodynamics of the association of amphiphilic polyelectrolytes in aqueous solutions: Strenghts and limitations of isothermal titration calorimetry
    • Bangar Raju, B.; Winnik, F.M.; Morishima,Y. A look at the thermodynamics of the association of amphiphilic polyelectrolytes in aqueous solutions: strenghts and limitations of isothermal titration calorimetry. Langmuir 2001, 17, 4416-4421.
    • (2001) Langmuir , vol.17 , pp. 4416-4421
    • Bangar Raju, B.1    Winnik, F.M.2    Morishima, Y.3
  • 67
    • 6444227409 scopus 로고    scopus 로고
    • 6: An equilibrium and structural study using a SDS selective electrode, isothermal titration calorimetry, and small angle neutron scattering
    • 6: An equilibrium and structural study using a SDS selective electrode, isothermal titration calorimetry, and small angle neutron scattering. Langmuir 2004, 20, 9320-9328.
    • (2004) Langmuir , vol.20 , pp. 9320-9328
    • Sidhu, J.1    Bloor, D.M.2    Couderc-Azouani, S.3    Penfold, J.4    Holzwarth, J.F.5    Wyn-Jones, E.6
  • 69
    • 0014645670 scopus 로고
    • Thermal analysis of lipids, proteins, and biological membranes: A review ans summary of some recent studies
    • Ladbrooke, B.D.; Chapman, D. Thermal analysis of lipids, proteins, and biological membranes: A review ans summary of some recent studies. Chem. Phys. Lipids 1969, 3, 304-356.
    • (1969) Chem. Phys. Lipids , vol.3 , pp. 304-356
    • Ladbrooke, B.D.1    Chapman, D.2
  • 70
    • 0016192567 scopus 로고
    • Biomembrane phase transitions. Studies of lipid-water systems using differential scanning calorimetry
    • Chapman, D.; Urbina, J. Biomembrane phase transitions. Studies of lipid-water systems using differential scanning calorimetry. J. Biol. Chem. 1974, 249, 2512-2521.
    • (1974) J. Biol. Chem. , vol.249 , pp. 2512-2521
    • Chapman, D.1    Urbina, J.2
  • 71
    • 0036197878 scopus 로고    scopus 로고
    • Application of pressure perturbation calorimetry to lipid bilayers
    • Heerklotz, H.; Seelig, J. Application of Pressure Perturbation Calorimetry to Lipid Bilayers. Biophys. J. 2002, 82, 1445-1452. (Pubitemid 34204764)
    • (2002) Biophysical Journal , vol.82 , Issue.3 , pp. 1445-1452
    • Heerklotz, H.1    Seelig, J.2
  • 72
    • 0036841874 scopus 로고    scopus 로고
    • Triton promotes domain formation in lipid raft mixtures
    • Heerklotz, H. Triton promotes domain formation in Lipid raft mixtures. Biophys. J. 2002, 83, 2693-2701. (Pubitemid 35265761)
    • (2002) Biophysical Journal , vol.83 , Issue.5 , pp. 2693-2701
    • Heerklotz, H.1
  • 73
    • 0030888260 scopus 로고    scopus 로고
    • Heat changes in lipid membranes under sudden osmotic stress
    • DOI 10.1021/bi961839n
    • Nebel, S.; Ganz, P.; Seelig, J. Heat changes in lipid membranes under sudden osmotic stress. Biochemistry 1997, 36, 2853-2859. (Pubitemid 27138568)
    • (1997) Biochemistry , vol.36 , Issue.10 , pp. 2853-2859
    • Nebel, S.1    Ganz, P.2    Seelig, J.3
  • 74
    • 11644276439 scopus 로고
    • Limiting laws and counterion condensation in polyelectrolyte solutions. I Colligative properties
    • Manning G.S. Limiting laws and counterion condensation in polyelectrolyte solutions. I Colligative properties. J. Chem.Phys. 1969, 51, 924-933.
    • (1969) J. Chem.Phys. , vol.51 , pp. 924-933
    • Manning, G.S.1
  • 75
    • 0030151599 scopus 로고    scopus 로고
    • Studies on the interaction of poly(4-vinylpyridiniumchloride) with poly(sodiumphosphate) in an aqueous solution by conductometry
    • Acar, N.; Tulun, T. Studies on the interaction of poly(4-vinypyridinium chloride) with poly(sodium phosphate) in an aqueous solution by conductometry. J. Polym. Sci. A. Polym.Chem. 1996, 34, 1251-1260. (Pubitemid 126553501)
    • (1996) Journal of Polymer Science, Part A: Polymer Chemistry , vol.34 , Issue.7 , pp. 1251-1260
    • Acar, N.1    Tulun, T.2
  • 76
    • 0031099559 scopus 로고    scopus 로고
    • Complex formation between polyelectrolytes in dilute aqueous solution
    • PII S0032386196006507
    • Webster, L.; Huglin, M.B.; Robb, I.D. Complex formation between polyelectrolytes in dilute aqueous solution. Polymer 1997, 38, 1373-1380. (Pubitemid 127409677)
    • (1997) Polymer , vol.38 , Issue.6 , pp. 1373-1380
    • Webster, L.1    Huglin, M.B.2    Robb, I.D.3
  • 77
    • 0034246134 scopus 로고    scopus 로고
    • Macroions in salty water with multivalent ions: Giant inversion of charge
    • Nguyen, T.T.; Grosberg, A.Y.; Shklovskii, B.I. Macroions in salty water with multivalent ions: giant inversion of charge. Phys. Rev. Lett. 2000, 85, 1568-1571.
    • (2000) Phys. Rev. Lett. , vol.85 , pp. 1568-1571
    • Nguyen, T.T.1    Grosberg, A.Y.2    Shklovskii, B.I.3
  • 78
    • 17444422886 scopus 로고    scopus 로고
    • Super stoechiometric neutralization in particle - Polyelectrolyte systems
    • Kleimann, J.; Gehin-Deval C.; Auweter, H.; Borkovec, M. Super stoechiometric neutralization in particle - polyelectrolyte systems. Langmuir 2005, 21, 3688-3698.
    • (2005) Langmuir , vol.21 , pp. 3688-3698
    • Kleimann, J.1    Gehin-Deval, C.2    Auweter, H.3    Borkovec, M.4
  • 80
    • 0000340035 scopus 로고    scopus 로고
    • Effect of pH on the binding of β-lactoglobulin to sodium polystyrenesulfonate
    • Hallberg, R.K.; Dubin, P.L. Effect of pH on the binding of β-Lactoglobulin to sodium polystyrene sulfonate. J. Phys. Chem. B 1998, 102, 8629-8633. (Pubitemid 128611813)
    • (1998) Journal of Physical Chemistry B , vol.102 , Issue.43 , pp. 8629-8633
    • Hallberg, R.K.1    Dubin, P.L.2
  • 81
    • 0037131648 scopus 로고    scopus 로고
    • Effect of charge density on the formation and salt stability of polyelectrolyte complexes
    • Dautzenberg, H.; Jaeger, W. Effect of charge density on the formation and salt stability of polyelectrolyte complexes. Macromol. Rapid Commun. 2002, 203, 2095-2102.
    • (2002) Macromol. Rapid Commun. , vol.203 , pp. 2095-2102
    • Dautzenberg, H.1    Jaeger, W.2
  • 82
  • 83
    • 0032492820 scopus 로고    scopus 로고
    • Complex formation between bovine serum albumin and strong polyelectrolytes: Effect of polymer charge density
    • Mattison, K.W.; Dubin, P.L.; Brittain, I.J. Complex formation between bovine serum albumin and strong polyelectrolytes: effect of polymer charge density. J. Phys. Chem. B 1998, 102, 3830-3836.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3830-3836
    • Mattison, K.W.1    Dubin, P.L.2    Brittain, I.J.3
  • 84
    • 28844486089 scopus 로고    scopus 로고
    • Influence of chitosan structure on the formation and stability of DNA-chitosan polyelectrolyte complexes
    • Strand, S.P.; Danielsen, S.; Christensen, B.E.; Vårum, K.M. Influence of chitosan structure on the formation and stability of DNA-chitosan polyelectrolyte complexes. Biomacromolecules 2005, 6, 3357-3366.
    • (2005) Biomacromolecules , vol.6 , pp. 3357-3366
    • Strand, S.P.1    Danielsen, S.2    Christensen, B.E.3    Vårum, K.M.4
  • 85
    • 0031335459 scopus 로고    scopus 로고
    • Polyelectrolyte complex formation in highly aggregating systems. 1. Effect of salt: Polyelectrolyte complex formation in the presence of NaCl
    • Dautzenberg, H. Polyelectrolyte complex formation in highly aggregating systems. 1. Effect of salt: polyelectrolyte complex formation in the presence of NaCl. Macromolecules 1997, 30, 7810-7815. (Pubitemid 127561603)
    • (1997) Macromolecules , vol.30 , Issue.25 , pp. 7810-7815
    • Dautzenberg, H.1
  • 86
    • 27144551289 scopus 로고    scopus 로고
    • Polyelectrolyte-protein complexes: Structure and conformation of each specie revealed by SANS
    • DOI 10.1021/la0510174
    • Cousin, F.; Gummel, J.; Ung, D.; Boué, F. Polyelectrolyte-protein complexes: structure and conformation of each specie revealed by SANS. Langmuir 2005, 21, 9675-9688. (Pubitemid 41509378)
    • (2005) Langmuir , vol.21 , Issue.21 , pp. 9675-9688
    • Cousin, F.1    Gummel, J.2    Ung, D.3    Boue, F.4
  • 87
    • 33846961487 scopus 로고    scopus 로고
    • Microstructure of β-lactoglobulin/pectin coacervates studied by small-angle neutron scattering
    • DOI 10.1021/jp0632891
    • Wang, X.; Li, Y.; Wang, Y.-W.; Lal, J.; Huang, Q. Microstructure of β-Lactoglobulin/pectin coacervates studied by small angle neutron scattering. J. Phys. Chem. B 2007, 111, 515-520. (Pubitemid 46256247)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.3 , pp. 515-520
    • Wang, X.1    Li, Y.2    Wang, Y.-W.3    Lal, J.4    Huang, Q.5
  • 88
    • 33644560028 scopus 로고    scopus 로고
    • Interpolyelectrolyte complexes: A single-molecule insight
    • Kiriy, A.; Yu, J.; Stamm, M. Interpolyelectrolyte complexes: a single-molecule insight. Langmuir 2006, 22, 1800-1803.
    • (2006) Langmuir , vol.22 , pp. 1800-1803
    • Kiriy, A.1    Yu, J.2    Stamm, M.3
  • 90
    • 1242310625 scopus 로고    scopus 로고
    • Strutural evolution of an interpolyelectrolyte complex of charged dendrimers with poly-L-glutamic acid
    • Leisner, D.; Imae, T. Strutural evolution of an interpolyelectrolyte complex of charged dendrimers with poly-L-glutamic acid. J. Phys. Chem. B 2004, 108, 1798-1804.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 1798-1804
    • Leisner, D.1    Imae, T.2
  • 91
    • 45549094400 scopus 로고    scopus 로고
    • Heterogeneity of polyelectrolyte diffusion in polyelectrolyte-protein coacervates: A 1H pulsed field gradient NMR study
    • Menjoge, A.R.; Kayitmazer, A.B. Dubin, P.L.; Jaeger, W.; Vasenkov, S. Heterogeneity of polyelectrolyte diffusion in polyelectrolyte-protein coacervates: a 1H pulsed field gradient NMR study. J. Phys.Chem. B. 2008, 112, 4961-4966.
    • (2008) J. Phys.Chem. B , vol.112 , pp. 4961-4966
    • Menjoge, A.R.1    Kayitmazer, A.B.2    Dubin, P.L.3    Jaeger, W.4    Vasenkov, S.5
  • 92
    • 66349110575 scopus 로고    scopus 로고
    • Reversibility and relaxation behavior of polyelectrolyte complex micelle formation
    • Lindhoud, S.; Norde, W.; Cohen Stuart, M.A. Reversibility and relaxation behavior of polyelectrolyte complex micelle formation. J. Phys. Chem. B 2009, 113, 5431-5439.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 5431-5439
    • Lindhoud, S.1    Norde, W.2    Cohen Stuart, M.A.3
  • 93
    • 0041908291 scopus 로고    scopus 로고
    • Controllable stability of DNA containing polyelectrolyte complexes in water salt solutions
    • Izumrudov, V.A.; Zhiryakova, M.V.; Kudaibergenov, S.E. Controllable stability of DNA containing polyelectrolyte complexes in water salt solutions. Biopolymers 1999, 52, 94-108.
    • (1999) Biopolymers , vol.52 , pp. 94-108
    • Izumrudov, V.A.1    Zhiryakova, M.V.2    Kudaibergenov, S.E.3
  • 94
    • 0000422363 scopus 로고    scopus 로고
    • Stability of DNA containing interpolyelectrolyte complexes in water salt solutions
    • Izumrudov, V.A.; Zhiryakova, M.V. Stability of DNA containing interpolyelectrolyte complexes in water salt solutions. Macromol. Chem. Phys. 1999, 200, 2533-2540.
    • (1999) Macromol. Chem. Phys. , vol.200 , pp. 2533-2540
    • Izumrudov, V.A.1    Zhiryakova, M.V.2
  • 95
    • 0242490633 scopus 로고    scopus 로고
    • Competitive reactions in solution of Poly-L-histidine, Calf thymus DNA, and synthetic polyanions: Determining the binding constants of polyelectrolytes
    • Zelikin, A.; Trukhanova, E.S.; Putnam, D.; Izumrudov, V.A.; Litmanovich, A.A. Competitive reactions in solution of Poly-L-histidine, Calf thymus DNA, and synthetic polyanions: determining the binding constants of polyelectrolytes. J. Am. Chem. Soc. 2003, 125, 13693-13699.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13693-13699
    • Zelikin, A.1    Trukhanova, E.S.2    Putnam, D.3    Izumrudov, V.A.4    Litmanovich, A.A.5
  • 96
    • 0035912412 scopus 로고    scopus 로고
    • Cooperative interactions of unlike macromolecules 2: NMR and theoretical study of electrostatic binding of sodium poly(styrenesulfonate)s to copolymers with variably distributed cationic groups
    • Křiž, J.; Dautzenberg, H. Cooperative interactions of unlike macromolecules. 2: NMR and theoretical study of electrostatic binding of sodium poly(stryrenesulfonate)s to copolymers with variably distributed cationic groups. J. Phys. Chem. A 2001, 105, 3846-3854. (Pubitemid 33763590)
    • (2001) Journal of Physical Chemistry a , vol.105 , Issue.15 , pp. 3846-3854
    • Kriz, J.1    Dautzenberg, H.2
  • 97
    • 0035960194 scopus 로고    scopus 로고
    • Monte Carlo simulations of polyelectrolyte-protein complexation
    • DOI 10.1021/jp010360o
    • Carlsson, F.; Linse, P.; Malmsten, M. Monte Carlo simulations of polyelectrolyte-protein complexation. J. Phys. Chem. B 2001, 105, 9040-9049. (Pubitemid 35338694)
    • (2001) Journal of Physical Chemistry B , vol.105 , Issue.38 , pp. 9040-9049
    • Carlsson, F.1    Linse, P.2    Malmsten, M.3
  • 98
    • 0242270642 scopus 로고    scopus 로고
    • Simple model for the binding of a polyelectrolyte to an oppositely charged surface
    • Manning, G.S. Simple model for the binding of a polyelectrolyte to an oppositely charged surface. J. Phys. Chem. B 2003, 107, 11485-11490.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 11485-11490
    • Manning, G.S.1
  • 100
    • 0037133842 scopus 로고    scopus 로고
    • Measurement of equilibrium binding of cationic micelles to apolyanion by membrane filtration
    • Feng, X.; Dubin, P.L. Measurement of equilibrium binding of cationic micelles to apolyanion by membrane filtration. Langmuir 2002, 18, 2032-2035.
    • (2002) Langmuir , vol.18 , pp. 2032-2035
    • Feng, X.1    Dubin, P.L.2
  • 101
    • 34250351975 scopus 로고    scopus 로고
    • Nonspecific electrostatic binding characteristics of the heparin-antithrombin interaction
    • DOI 10.1002/bip.20731
    • Seyrek, E.; Dubin, P.L., Henriksen, J. Nonspecific electrostatic binding characteristics if the heparin-antithrombin interaction. Biopolymers 2007, 86, 249-259. (Pubitemid 46910396)
    • (2007) Biopolymers , vol.86 , Issue.3 , pp. 249-259
    • Seyrek, E.1    Dubin, P.L.2    Henriksen, J.3
  • 102
    • 0023229226 scopus 로고
    • A general method of analysis of ligand-macromolecule equilibria using a spectroscopic signal from the ligand to monitor binding. Application to Escherichia coli single-strand binding protein-nucleic acid interactions
    • DOI 10.1021/bi00385a023
    • Bugalowski, W.; Lohman, T. A general method of analysis of ligand-macromolecule equilibria using a spectroscopic signal from the ligand to monitor binding. Application to Escherichia coli single-strand binding protein-nucleic acid interactions. Biochemistry 1987, 26, 3099-3106. (Pubitemid 17087843)
    • (1987) Biochemistry , vol.26 , Issue.11 , pp. 3099-3106
    • Bujalowski, W.1    Lohman, T.M.2
  • 103
    • 0017669272 scopus 로고
    • Measurement of binding constants for protein DNA interactions by DNA cellulose chromatography
    • DeHaseth, P.L.; Gross, C.A.; Burgess, R.R.; Record, M.T. Jr. Measurement of binding constants for protein DNA interactions by DNA-cellulose chromatography. Biochemistry 1977, 16, 4777-4783. (Pubitemid 8220965)
    • (1977) Biochemistry , vol.16 , Issue.22 , pp. 4777-4783
    • Dehaseth, P.L.1    Gross, C.A.2    Burgess, R.R.3    Record Jr., M.T.4
  • 104
    • 0015515070 scopus 로고
    • Thermodynamic and kinetic studies on the cooperative binding of proflavine to linear polyanions
    • Schwarz, G.; Klose, S. Thermodynamic and kinetic studies on the cooperative binding of proflavine to linear polyanions. Eur. J. Biochem. 1972, 29, 249-256.
    • (1972) Eur. J. Biochem. , vol.29 , pp. 249-256
    • Schwarz, G.1    Klose, S.2
  • 105
    • 0015525668 scopus 로고
    • Interactions protéines-acides nucléiques. 1. Etude théorique de l'association
    • Daune, M.P. Interactions protéines-acides nucléiques. 1. Etude théorique de l'association. Eur. J. Biochem. 1972, 26, 207-211.
    • (1972) Eur. J. Biochem. , vol.26 , pp. 207-211
    • Daune, M.P.1
  • 106
    • 0014734299 scopus 로고
    • Cooperative binding to linear biopolymers
    • Schwarz, G. Cooperative binding to linear biopolymers. Eur. J. Biochem. 1970, 12, 442-453.
    • (1970) Eur. J. Biochem. , vol.12 , pp. 442-453
    • Schwarz, G.1
  • 107
    • 0016175370 scopus 로고
    • Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice
    • McGhee, J.D.; vonHippel, P.H. Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice. J. Mol. Biol. 1974, 86, 469-489.
    • (1974) J. Mol. Biol. , vol.86 , pp. 469-489
    • McGhee, J.D.1    Vonhippel, P.H.2
  • 108
  • 110
    • 0026730188 scopus 로고
    • Thermodynamics of single-stranded RNA binding to oligolysines containing tryptophan
    • Mascotti, D.P.; Lohman, T.M. Thermodynamics of single-stranded RNA binding to oligolysines containing tryptophan. Biochemistry 1992, 31, 8932-8946.
    • (1992) Biochemistry , vol.31 , pp. 8932-8946
    • Mascotti, D.P.1    Lohman, T.M.2
  • 111
    • 0029933128 scopus 로고    scopus 로고
    • A highly salt-dependent enthalpy change for Escherichia coli SSB protein- Nucleic acid binding due to ion-protein interactions
    • DOI 10.1021/bi9527606
    • Lohman, T.M.; Overman, L.B.; Ferrari, M.E.; Kozlov, A.G. A highly salt dependant enthalpy change for Escherichia coli SSB protein-nucleic acid binding due to ion-protein interactions. Biochemistry 1996, 35, 5272-5279. (Pubitemid 26129468)
    • (1996) Biochemistry , vol.35 , Issue.16 , pp. 5272-5279
    • Lohman, T.M.1    Overman, L.B.2    Ferrari, M.E.3    Kozlov, A.G.4
  • 112
    • 0030920231 scopus 로고    scopus 로고
    • Thermodynamics of oligoarginines binding to RNA and DNA
    • DOI 10.1021/bi970272n
    • Mascotti, D.P.; Lohman, T.M. Thermodynamics of oligoarginines binding to RNA and DNA. Biochemistry 1997, 36, 7272-7279. (Pubitemid 27258144)
    • (1997) Biochemistry , vol.36 , Issue.23 , pp. 7272-7279
    • Mascotti, D.P.1    Lohman, T.M.2
  • 114
    • 39149145849 scopus 로고    scopus 로고
    • Polyelectrolyte complex characterization with isothermal titration calorimetry and colloid titration
    • Feng, X.; Leduc, M.; Pelton, R. Polyelectrolyte complex characterization with isothermal titration calorimetry and colloid titration. Colloids Surf., A: Physicochem. Eng. Aspects 2008, 317, 535-542.
    • (2008) Colloids Surf., A: Physicochem. Eng. Aspects , vol.317 , pp. 535-542
    • Feng, X.1    Leduc, M.2    Pelton, R.3
  • 115
    • 33750324656 scopus 로고    scopus 로고
    • Ideal mixing in polyelectrolyte complexes and multilayers: Entropy driven assembly
    • Bucur, C.B.; Sui, Z.; Schlenoff, J.B. Ideal mixing in polyelectrolyte complexes and multilayers: entropy driven assembly. J. Am. Chem. Soc. 2006, 128, 13690-13691.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 13690-13691
    • Bucur, C.B.1    Sui, Z.2    Schlenoff, J.B.3
  • 116
    • 40149111869 scopus 로고    scopus 로고
    • Melittin interaction with sulfated cell surface sugars
    • DOI 10.1021/bi702258z
    • Klocek, G.; Seelig, J. Melittin interaction with sulfated cell surface sugars. Biochemistry 2008, 47, 2841-2849. (Pubitemid 351328835)
    • (2008) Biochemistry , vol.47 , Issue.9 , pp. 2841-2849
    • Klocek, G.1    Seelig, J.2
  • 117
    • 0002114304 scopus 로고
    • Polyelectrolyte complexes
    • Michaels, A.S. Polyelectrolyte complexes. Ind. Eng. Chem. 1965, 57, 32-41.
    • (1965) Ind. Eng. Chem. , vol.57 , pp. 32-41
    • Michaels, A.S.1
  • 118
    • 33750304802 scopus 로고    scopus 로고
    • Relationship between the growth regime of polyelectrolyte multilayers and the polyanion/polycation complexation enthalpy
    • DOI 10.1021/jp062264z
    • Laugel, N.; Betscha, C.; Winterhalter, M.; Voegel, J.-C.; Schaaf, P.; Ball, V. Relationship between the growth regime of polyelectrolyte multilayers and the polyanion/polycation complexation enthalpy. J. Phys. Chem. B 2006, 110, 19443-19449. (Pubitemid 44626421)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.39 , pp. 19443-19449
    • Laugel, N.1    Betscha, C.2    Winterhalter, M.3    Voegel, J.C.4    Schaaf, P.5    Ball, V.6
  • 119
    • 0011338828 scopus 로고
    • Enthalpies of mixing polyelectrolytes with simple aqueous electrolyte solutions
    • Boyd, G.E.; Wilson, D.P.; Manning, G.S. Enthalpies of mixing polyelectrolytes with simple aqueous electrolyte solutions. J. Phys. Chem. 1976, 80, 808-810.
    • (1976) J. Phys. Chem. , vol.80 , pp. 808-810
    • Boyd, G.E.1    Wilson, D.P.2    Manning, G.S.3
  • 121
    • 0034598941 scopus 로고    scopus 로고
    • Thermodynamics of DNA binding and condensation: Isothermal titration calorimetry and electrostatic mechanism
    • Matulis, D.; Rouzina, I.; Bloomfield, V.A. Thermodynamics of DNA binding and condensation: isothermal titration calorimetry and electrostatic mechanism. J. Mol. Biol. 2000, 296, 1053-1063.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1053-1063
    • Matulis, D.1    Rouzina, I.2    Bloomfield, V.A.3
  • 122
    • 0030715273 scopus 로고    scopus 로고
    • Thermodynamics of the binding of a cationic lipid to DNA
    • DOI 10.1021/ja964324s
    • Spink, C.H.; Chaires J.B. Thermodynamics of the binding of a cationic lipid to DNA. J. Am. Chem. Soc. 1997, 119, 10920-10928. (Pubitemid 27528837)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.45 , pp. 10920-10928
    • Spink, C.H.1    Chaires, J.B.2
  • 123
    • 0035824010 scopus 로고    scopus 로고
    • P-Sulfonatocalix[6]arene is an effective coacervator of poly(allylamine htdrochloride)
    • Ball, V.; Winterhalter, M.; Perret, F.; Esposito, G.; Coleman, A.W. p-Sulfonatocalix[6]arene is an effective coacervator of poly(allylamine htdrochloride). Chem. Comm. 2001, 7, 2276-2277.
    • (2001) Chem. Comm. , vol.7 , pp. 2276-2277
    • Ball, V.1    Winterhalter, M.2    Perret, F.3    Esposito, G.4    Coleman, A.W.5
  • 124
    • 0035824372 scopus 로고    scopus 로고
    • Protein-calixarene interactions: Complexation of Bovine Serum Albumin by sulfonatocalix[n]arenes
    • Memmi, L.; Lazar, A.; Brioude, A.; Ball, V.; Coleman, A.W. Protein-calixarene interactions: complexation of Bovine serum albumin by sulfonatocalix[n]arenes. Chem. Comm. 2001, 2474-2475. (Pubitemid 33124092)
    • (2001) Chemical Communications , Issue.23 , pp. 2474-2475
    • Memmi, L.1    Lazar, A.2    Brioude, A.3    Ball, V.4    Coleman, A.W.5
  • 125
    • 2342483719 scopus 로고    scopus 로고
    • The microcalorimetry of lipid membranes
    • Heerklotz, H. The microcalorimetry of lipid membranes. J. Phys. Condens. Matter 2004, 16, R441-R467.
    • (2004) J. Phys. Condens. Matter , vol.16
    • Heerklotz, H.1
  • 126
    • 0031567121 scopus 로고    scopus 로고
    • Titration calorimetry of lipid-peptide interactions
    • Seelig, J. Titration calorimetry of lipid-peptide interactions. Biochim. Biphys. Acta 1997, 1331, 103-116.
    • (1997) Biochim. Biphys. Acta , vol.1331 , pp. 103-116
    • Seelig, J.1
  • 127
    • 7044235790 scopus 로고    scopus 로고
    • Thermodynamics of lipid-peptide interactions
    • Seelig, J. Thermodynamics of lipid-peptide interactions. Biochim. Biophys. Acta 2004, 1666, 40-50.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 40-50
    • Seelig, J.1
  • 128
    • 0025789799 scopus 로고
    • Interaction of charged and uncharged calcium channel antagonists with phospholipid membranes. Binding equilibrium, binding enthalpy and membrane location
    • Bäuerle, H.-D.; Seelig, J. Interaction of charged and uncharged calcium channel antagonists with phospholipid membranes. Binding equilibrium, binding enthalpy and membrane location. Biochemistry 1991, 30, 7203-7211.
    • (1991) Biochemistry , vol.30 , pp. 7203-7211
    • Bäuerle, H.-D.1    Seelig, J.2
  • 129
    • 0025996974 scopus 로고
    • Nonclassical hydrophobic effect in membrane binding equilibria
    • Seelig, J.; Ganz, P. Nonclassical hydrophobic effect in membrane binding equilibria. Biochemistry 1991, 30, 9354-9359.
    • (1991) Biochemistry , vol.30 , pp. 9354-9359
    • Seelig, J.1    Ganz, P.2
  • 130
    • 4544240958 scopus 로고    scopus 로고
    • Halogenation of drugs enhances membrane binding and permeation
    • DOI 10.1002/cbic.200400017
    • Gerebtzoff, G.; Li-Blatter, X.; Fischer, H. Frentzel, A.; Seelig, A. Halogenation of drugs enhances membrane binding and permeation. ChemBioChem 2004, 5, 676-684. (Pubitemid 39257090)
    • (2004) ChemBioChem , vol.5 , Issue.5 , pp. 676-684
    • Gerebtzoff, G.1    Li-Blatter, X.2    Fischer, H.3    Frentzel, A.4    Seelig, A.5
  • 131
    • 1442325506 scopus 로고    scopus 로고
    • Calorimetric Measurement of Phospholipid Interaction with Methyl-β-Cyclodextrin
    • DOI 10.1021/bi0358869
    • Anderson, T.G.; Tan, A.; Ganz, P.; Seelig, J. Calorimetric measurement of phospholipid interaction with methyl-β-cyclodextrin. Biochemistry 2004, 43, 2251-2261. (Pubitemid 38279970)
    • (2004) Biochemistry , vol.43 , Issue.8 , pp. 2251-2261
    • Anderson, T.G.1    Tan, A.2    Ganz, P.3    Seelig, J.4
  • 132
    • 33749522506 scopus 로고    scopus 로고
    • Interaction of verapamil with lipid membranes and P-glycoprotein: Connecting thermodynamics and membrane structure with functional activity
    • DOI 10.1529/biophysj.106.089581
    • Meier, M.; Li Blatter, X.; Seelig, A.; Seelig, J. Interactions of verapamil with lipid membranes and P-Glycoprotein: connecting thermodynamics and membrane structure with functional activity. Biophys. J. 2006, 91, 2943-2955. (Pubitemid 44526485)
    • (2006) Biophysical Journal , vol.91 , Issue.8 , pp. 2943-2955
    • Meier, M.1    Li Blatter, X.2    Seelig, A.3    Seelig, J.4
  • 133
    • 0037065703 scopus 로고    scopus 로고
    • Specific binding of Ro 09-0198 (cinnamycin) to phosphatidylethanolamine: A thermodynamic analysis
    • DOI 10.1021/bi015841c
    • Machaidze, G.; Ziegler, A.; Seelig, J. Specific binding of Ro 09-O198 (cynnamycin) to phosphatidylethanol amine:a thermodynamic analysis. Biochemistry 2002, 41, 1965-1971. (Pubitemid 34132271)
    • (2002) Biochemistry , vol.41 , Issue.6 , pp. 1965-1971
    • Machaidze, G.1    Ziegler, A.2    Seelig, J.3
  • 134
    • 0032539980 scopus 로고    scopus 로고
    • Magainin 2 amide interaction with lipid membranes: Calorimetric detection of peptide binding and pore formation
    • DOI 10.1021/bi972615n
    • Wenk, M.; Seelig, J. Magainin 2 amide interaction with lipid membranes: calorimetric detection of peptide binding and pore formation. Biochemistry 1998, 37, 39909-43916 (Pubitemid 28162948)
    • (1998) Biochemistry , vol.37 , Issue.11 , pp. 3909-3916
    • Wenk, M.R.1    Seelig, J.2
  • 135
    • 0037007486 scopus 로고    scopus 로고
    • Thermodynamics of the coil-helix transition of amphipathic peptides in a membrane environment: The role of vesicle curvature
    • DOI 10.1016/S0301-4622(02)00025-X, PII S030146220200025X
    • Wieprecht, T.; Beyermann, M.; Seelig, J. Thermodynamics of the coil-helix transition of amphipatic peptides in a membrane environment: the role of vesicle curvature. Biophys. Chem. 2002, 96, 191-201. (Pubitemid 34548232)
    • (2002) Biophysical Chemistry , vol.96 , Issue.2-3 , pp. 191-201
    • Wieprecht, T.1    Beyermann, M.2    Seelig, J.3
  • 136
    • 38349121952 scopus 로고    scopus 로고
    • Length dependence of the coil ⇔ β-sheet transition in a membrane environement
    • Meier, M.; Seelig, J. Length dependence of the coil ⇔ β-sheet transition in a membrane environement. J. Am. Chem. Soc. 2008, 130, 1017-1024.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 1017-1024
    • Meier, M.1    Seelig, J.2
  • 137
    • 34247368438 scopus 로고    scopus 로고
    • Thermodynamics of the Coil ↔ β-Sheet Transition in a Membrane Environment
    • DOI 10.1016/j.jmb.2007.02.082, PII S0022283607002884
    • Meier, M.; Seelig, J. Thermodynamics of the coil↔β sheet transition in a membrane environment. J. Mol. Biol. 2007, 369, 277-289. (Pubitemid 46635428)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.1 , pp. 277-289
    • Meier, M.1    Seelig, J.2
  • 138
    • 0035960561 scopus 로고    scopus 로고
    • 2-glycoprotein I with negatively charged phospholipid membranes
    • DOI 10.1021/bi0114372
    • Hammel, M.; Schwarzenbacher, R.; Gries, A.; Kostner, G.M.; Lagner, P.; Prassl, R. Mechanism of the interaction of β2-Glycoprotein I with negatively charged phospholipid membranes. Biochemistry 2001, 40, 14173-14181. (Pubitemid 33081620)
    • (2001) Biochemistry , vol.40 , Issue.47 , pp. 14173-14181
    • Hammel, M.1    Schwarzenbacher, R.2    Gries, A.3    Kostner, G.M.4    Laggner, P.5    Prassl, R.6
  • 139
    • 56449084739 scopus 로고    scopus 로고
    • Interactions between antimicrobial polynorbornenes and phospholipid vesicles monitored by light scattering and microcalorimetry
    • Gabriel, G.J.; Pool, J.G.; Som, A.; Dabkowski, J.M.; Coughlin, E.B.; Muthukumar, M.; Tew, G.N. Interactions between antimicrobial polynorbornenes and phospholipid vesicles monitored by light scattering and microcalorimetry. Langmuir 2008, 24, 12489-12495.
    • (2008) Langmuir , vol.24 , pp. 12489-12495
    • Gabriel, G.J.1    Pool, J.G.2    Som, A.3    Dabkowski, J.M.4    Coughlin, E.B.5    Muthukumar, M.6    Tew, G.N.7
  • 140
    • 0035973479 scopus 로고    scopus 로고
    • The interaction of phospholipid liposomes with zinc citrate particles: A microcalorimetric investigation
    • Scott, M.J.; Jones, M.N. The interaction of phospholipid liposomes with zinc citrate particles: a microcalorimetric investigation. Colloids Surf., A: Phys. Engineer. Aspects 2001, 182, 247-256.
    • (2001) Colloids Surf., A: Phys. Engineer. Aspects , vol.182 , pp. 247-256
    • Scott, M.J.1    Jones, M.N.2
  • 141
    • 34347401701 scopus 로고    scopus 로고
    • Model-free analysis of binding at lipid membranes employing micro-calorimetric measurements
    • DOI 10.1007/s00249-007-0143-5
    • Schwarz, G.; Damian, L.; Winterhalter, M. Model-free analysis of binding at lipid membranes employing micro-calorimetric measurements. Eur. Biophys. J. 2007, 36, 571-579. (Pubitemid 47019979)
    • (2007) European Biophysics Journal , vol.36 , Issue.6 , pp. 571-579
    • Schwarz, G.1    Damian, L.2    Winterhalter, M.3
  • 142
    • 0024553457 scopus 로고
    • The electrostatic properties of membranes
    • McLaughlin, S. The electrostatic properties of membranes. Ann. Rev. Biophys. Biophys. Chem. 1989, 18, 113-116.
    • (1989) Ann. Rev. Biophys. Biophys. Chem. , vol.18 , pp. 113-116
    • McLaughlin, S.1
  • 143
    • 0037122767 scopus 로고    scopus 로고
    • What happens to negatively charged lipid vesicles upon interacting with polycation species?
    • Kabanov, V.A.; Yaroslavov, A.A. What happens to negatively charged lipid vesicles upon interacting with polycation species? J. Controlled Release 2002, 78, 267-271.
    • (2002) J. Controlled Release , vol.78 , pp. 267-271
    • Kabanov, V.A.1    Yaroslavov, A.A.2
  • 144
    • 33846353824 scopus 로고    scopus 로고
    • Complexation of phosphocholine liposomes with polylysine. Stabilization by surface coverage versus aggregation
    • DOI 10.1016/j.bbamem.2006.09.015, PII S0005273606003567
    • Volodkin, D.; Ball, V.; Voegel, J.-C., Möhwald, H. Complexation of phosphocholine liposomes with polylysine. Stabilization by surface coverage or aggregation? Biochim. Biophys. Acta, Biomembr. 2007, 1768, 280-290. (Pubitemid 46136185)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.2 , pp. 280-290
    • Volodkin, D.1    Ball, V.2    Schaaf, P.3    Voegel, J.-C.4    Mohwald, H.5
  • 145
    • 0029057673 scopus 로고
    • Calorimetric detection of influenza virus induced membrane fusion
    • Nebel, S.; Bartoldus, I.; Stegmann, T. Calorimetric detection of influenza virus induced membrane fusion. Biochemistry 1995, 34, 5705-5711.
    • (1995) Biochemistry , vol.34 , pp. 5705-5711
    • Nebel, S.1    Bartoldus, I.2    Stegmann, T.3
  • 146
    • 0012864313 scopus 로고    scopus 로고
    • Thermodynamics of adsorption of amino acids, small peptides, and nucleic acid components on silica adsorbents
    • Malmsten, M., Ed.; Marcel Dekker: New York. NY, USA
    • Basiuk, V.A. Thermodynamics of adsorption of amino acids, small peptides, and nucleic acid components on silica adsorbents. In Biopolymers at Interfaces. Surfactant Science Series. Malmsten, M., Ed.; Marcel Dekker: New York. NY, USA, 2003; volume 113, pp. 45-70.
    • (2003) Biopolymers at Interfaces. Surfactant Science Series , vol.113 , pp. 45-70
    • Basiuk, V.A.1
  • 148
    • 0001418781 scopus 로고
    • The adsorption of human plasma albumin and bovine pancreas ribonuclease at negatively charged polystyrene surfaces: V. Microcalorimetry
    • Norde, W.; Lyklema, J. The adsorption of human plasma albumin and bovine pancreas ribonuclease at negatively charged polystyrene surfaces: V. Microcalorimetry. J. Colloid Interface Sci. 1978, 66, 295-302.
    • (1978) J. Colloid Interface Sci. , vol.66 , pp. 295-302
    • Norde, W.1    Lyklema, J.2
  • 149
    • 49249141995 scopus 로고
    • Thermodynamics of protein adsorption. Theory with special reference to the adsorption of Human Plasma Albumin and Bovine pancreas ribonuclease at polystyrene surfaces
    • Norde, W.; Lyklema, J. Thermodynamics of protein adsorption. Theory with special reference to the adsorption of Human Plasma Albumin and Bovine pancreas ribonuclease at polystyrene surfaces. J. Colloid Interface Sci. 1979, 71, 350-366.
    • (1979) J. Colloid Interface Sci. , vol.71 , pp. 350-366
    • Norde, W.1    Lyklema, J.2
  • 150
    • 33646774999 scopus 로고    scopus 로고
    • Adsorption-induced conformational changes of proteins onto ceramic particles: Differential scanning calorimetry and FTIR analysis
    • Brandes, N.; Welzel, P.B.; Werner, C.; Kroh, L.W. Adsorption-induced conformational changes of proteins onto ceramic particles: differential scanning calorimetry and FTIR analysis. J. Colloid Interface Sci. 2006, 299, 56-69.
    • (2006) J. Colloid Interface Sci. , vol.299 , pp. 56-69
    • Brandes, N.1    Welzel, P.B.2    Werner, C.3    Kroh, L.W.4
  • 151
    • 3242723297 scopus 로고    scopus 로고
    • Thermodynamic analysis of lysozyme adsorbed to silica
    • DOI 10.1016/j.jcis.2004.03.056, PII S0021979704003364
    • Larsericsdotter, H.; Oscarsson, S.; Buijs, J. Thermodynamic analysis of lysozyme adsorbed to silica. J. Colloid Interface Sci. 2004, 276, 261-268. (Pubitemid 38950985)
    • (2004) Journal of Colloid and Interface Science , vol.276 , Issue.2 , pp. 261-268
    • Larsericsdotter, H.1    Oscarsson, S.2    Buijs, J.3
  • 152
    • 0033563871 scopus 로고    scopus 로고
    • Microcalorimetric studies of the interactions of lysozyme with immobilized metal ions: Effects of ion, pH value, and salt concentration
    • Lin, F.-Y.; Chen, W.Y; Sang, L.-C. Microcalorimetric studies of the interactions of lysozyme with immobilized metal ions: effects of ion, pH value, and salt concentration. J. Colloid Interface Sci. 1999, 214, 373-379.
    • (1999) J. Colloid Interface Sci. , vol.214 , pp. 373-379
    • Lin, F.-Y.1    Chen, W.Y.2    Sang, L.-C.3
  • 153
    • 0035880579 scopus 로고    scopus 로고
    • Microcalorimetric studies on the interaction mechanism between proteins and hydrophobic solid surfaces in hydrophobic interaction chromatography: Effects of salt, hydrophobicity of the solvent, and the structure of the protein
    • Lin, F.-Y.; Chen, W.-Y. Hearn, M.T.W. Microcalorimetric studies on the interaction mechanism between proteins and hydrophobic solid surfaces in hydrophobic interaction chromatography: effects of salt, hydrophobicity of the solvent, and the structure of the protein. Anal. Chem. 2001, 73, 3875-3883.
    • (2001) Anal. Chem. , vol.73 , pp. 3875-3883
    • Lin, F.-Y.1    Chen, W.-Y.2    Hearn, M.T.W.3
  • 154
    • 0036010796 scopus 로고    scopus 로고
    • Thermodynamic analysis of the interaction between proteins and solid surfaces: Application to liquid chromatography
    • DOI 10.1002/jmr.564
    • Lin, F.Y.; Chen, W.Y.; Hearn, M.T.W. Thermodynamic analysis of the interaction between proteins and solid surfaces: application to liquid chromatography. J. Mol. Recognit. 2002, 15, 55-93. (Pubitemid 34416013)
    • (2002) Journal of Molecular Recognition , vol.15 , Issue.2 , pp. 55-93
    • Lin, F.-Y.1    Chen, W.-Y.2    Hearn, M.T.W.3
  • 155
    • 20344374398 scopus 로고    scopus 로고
    • Microcalorimetry of the adsorption of lysozyme onto polymeric substrates
    • DOI 10.1016/j.jcis.2005.02.057, PII S002197970500202X
    • Lee, V.A.; Craig, R.G.; Filisko, F.E.; Zand, R. Microcalorimetry of the adsorption of lysozyme onto polymeric substrates. J. Colloid Interface Sci. 2005, 288, 6-13. (Pubitemid 40779495)
    • (2005) Journal of Colloid and Interface Science , vol.288 , Issue.1 , pp. 6-13
    • Lee, V.A.1    Craig, R.G.2    Filisko, F.E.3    Zand, R.4
  • 156
    • 33846860662 scopus 로고    scopus 로고
    • The hydrophobic interactions of the ion-exchanger resin ligands with proteins at high salt concentrations by adsorption isotherms and isothermal titration calorimetry
    • DOI 10.1016/j.seppur.2006.09.008, PII S1383586606002899
    • Chen, W.-Y.; Liu, Z.-C.; Lin, P.-H.; Fang, C.-I.; Yamamoto, S. The hydrophobic interactions of the ion-exchanger resin ligands with proteins at high salt concentrations by adsorption isotherms and isothermal titration calorimetry. Sep. Purif. Technol. 2007, 54, 212-219. (Pubitemid 46228030)
    • (2007) Separation and Purification Technology , vol.54 , Issue.2 , pp. 212-219
    • Chen, W.-Y.1    Liu, Z.-C.2    Lin, P.-H.3    Fang, C.-I.4    Yamamoto, S.5
  • 157
    • 33646339151 scopus 로고    scopus 로고
    • Thermodynamics of statherin adsorption onto hydroxyapatite
    • Goobes, R.; Goobes, G.; Campbell, C.T.; Stayton, P.S. Thermodynamics of statherin adsorption onto hydroxyapatite. Biochemistry 2006, 45, 5576-5586.
    • (2006) Biochemistry , vol.45 , pp. 5576-5586
    • Goobes, R.1    Goobes, G.2    Campbell, C.T.3    Stayton, P.S.4
  • 158
    • 34848898194 scopus 로고    scopus 로고
    • Biomimetic interactions of proteins with functionalized nanoparticles: A thermodynamic study
    • De, M.; You, C.-C.; Srivastava, S.; Rotello, V.M. Biomimetic interactions of proteins with functionalized nanoparticles: a thermodynamic study. J. Am. Chem. Soc. 2007, 129, 10747-10753.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 10747-10753
    • De, M.1    You, C.-C.2    Srivastava, S.3    Rotello, V.M.4
  • 159
    • 33846377850 scopus 로고    scopus 로고
    • Calorimetric comparison of the interactions between salivary proteins and Streptococcus mutans with and without antigen I/II
    • DOI 10.1016/j.colsurfb.2006.10.016, PII S0927776506003390
    • Xu, C.-P.; van de Belt-Gritter, B.; Busscher, H.J.; van der Mei, H.C.; Norde, W. Calorimetric comparison of the interaction between salivary proteins and Streptococcus Mutans with and without antigen I/II. Colloids Surf., B: Biointerfaces 2007, 54, 193-199. (Pubitemid 46136927)
    • (2007) Colloids and Surfaces B: Biointerfaces , vol.54 , Issue.2 , pp. 193-199
    • Xu, C.-P.1    Van De Belt-Gritter, B.2    Busscher, H.J.3    Van Der Mei, H.C.4    Norde, W.5


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