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Volumn 6, Issue 10, 2010, Pages 3259-3266

Fast proton titration scheme for multiscale modeling of protein solutions

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EID: 77957946626     PISSN: 15499618     EISSN: 15499626     Source Type: Journal    
DOI: 10.1021/ct1003093     Document Type: Article
Times cited : (44)

References (68)
  • 1
    • 0018094892 scopus 로고
    • Electrostatic Effects in Proteins
    • Perutz, M. F. Electrostatic Effects in Proteins Science 1978, 201, 1187-1191
    • (1978) Science , vol.201 , pp. 1187-1191
    • Perutz, M.F.1
  • 3
    • 11744372415 scopus 로고
    • Potentials of mean force in charged systems: Application to Superoxide Dismutase
    • Woodward, C. E.; Svensson, B. Potentials of mean force in charged systems: Application to Superoxide Dismutase J. Phys. Chem. 1991, 95, 7471-7477
    • (1991) J. Phys. Chem. , vol.95 , pp. 7471-7477
    • Woodward, C.E.1    Svensson, B.2
  • 4
    • 25844500998 scopus 로고    scopus 로고
    • Factors determining the physical properties of protein foams
    • Foegeding, E. A.; Luck, P.; Davis, J. Factors determining the physical properties of protein foams Food Hydrocolloids 2006, 20, 284-292
    • (2006) Food Hydrocolloids , vol.20 , pp. 284-292
    • Foegeding, E.A.1    Luck, P.2    Davis, J.3
  • 5
    • 0023728756 scopus 로고
    • The Chemistry of Lysozyme and its use as a Food Preservative and a Pharmaceutical
    • Proctor, V. A.; Cunningham, F. E. The Chemistry of Lysozyme and its use as a Food Preservative and a Pharmaceutical CRC Crit. Rev. Food Nutrition 1988, 26, 359-3958
    • (1988) CRC Crit. Rev. Food Nutrition , vol.26 , pp. 359-3958
    • Proctor, V.A.1    Cunningham, F.E.2
  • 6
    • 42149164796 scopus 로고    scopus 로고
    • Interfacial structure and stability of food emulsions as affected by protein-polysaccharide interactions
    • Dickinson, E. Interfacial structure and stability of food emulsions as affected by protein-polysaccharide interactions Soft Matter 2008, 4, 932-942
    • (2008) Soft Matter , vol.4 , pp. 932-942
    • Dickinson, E.1
  • 8
    • 0028408943 scopus 로고
    • Effect of solution pH and ionic strength on the separation of albumin from immunoglobulins (IgG) by selective filtration
    • Saksena, S.; Zydney, A. L. Effect of solution pH and ionic strength on the separation of albumin from immunoglobulins (IgG) by selective filtration Biotechnol. Bioeng. 1994, 43, 960-968
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 960-968
    • Saksena, S.1    Zydney, A.L.2
  • 9
    • 0030149441 scopus 로고    scopus 로고
    • Protein Separation via Polyelectrolyte Coacervation: Selectivity and Efficiency
    • Wang, Y.-F.; Gao, J. Y.; Dubin, P. L. Protein Separation via Polyelectrolyte Coacervation: Selectivity and Efficiency Biotechnol. Prog. 1996, 12, 356-362
    • (1996) Biotechnol. Prog. , vol.12 , pp. 356-362
    • Wang, Y.-F.1    Gao, J.Y.2    Dubin, P.L.3
  • 10
    • 0032577356 scopus 로고    scopus 로고
    • Protein binding on polyelectrolyte-treated glass. Effect of structure of adsorbed polyelectrolyte
    • Wang, Y.; Dubin, P. Protein binding on polyelectrolyte-treated glass. Effect of structure of adsorbed polyelectrolyte J. Chromatogr. A 1998, 808, 61-70
    • (1998) J. Chromatogr. A , vol.808 , pp. 61-70
    • Wang, Y.1    Dubin, P.2
  • 11
    • 0029394751 scopus 로고
    • Protein fractionation using electrostatic interactions in membranel filtration
    • van Eijndhoven, R. H. C. M.; Saksena, S.; Zydney, A. L. Protein fractionation using electrostatic interactions in membranel filtration Biotechnol. Bioeng. 1995, 48, 406-414
    • (1995) Biotechnol. Bioeng. , vol.48 , pp. 406-414
    • Van Eijndhoven, R.H.C.M.1    Saksena, S.2    Zydney, A.L.3
  • 12
    • 17144365075 scopus 로고    scopus 로고
    • On the charge regulation of proteins
    • Lund, M.; Jönsson, B. On the charge regulation of proteins Biochemistry 2005, 44, 5722-5727
    • (2005) Biochemistry , vol.44 , pp. 5722-5727
    • Lund, M.1    Jönsson, B.2
  • 13
    • 58149155020 scopus 로고    scopus 로고
    • Electrostatics in Macromolecular Solution. Dickinson, E.; Leser, M. E., Eds.; Royal Society of Chemistry: London
    • Jönsson, B.; Lund, M.; da Silva, F. L. B. Electrostatics in Macromolecular Solution. In Food Colloids: Self-Assembly and Material Science; Dickinson, E.; Leser, M. E., Eds.; Royal Society of Chemistry: London, 2007; Vol. 9.
    • (2007) Food Colloids: Self-Assembly and Material Science , vol.9
    • Jönsson, B.1    Lund, M.2    Da Silva, F.L.B.3
  • 14
    • 69249089296 scopus 로고    scopus 로고
    • Polyelectrolyte-protein complexation driven by charge regulation
    • Da Silva, F. L. B.; Jönsson, B. Polyelectrolyte-protein complexation driven by charge regulation Soft Matter 2009, 5, 2862-2868
    • (2009) Soft Matter , vol.5 , pp. 2862-2868
    • Da Silva, F.L.B.1    Jönsson, B.2
  • 16
    • 33947460278 scopus 로고
    • Light Scattering Investigation of Charge Fluctuations in Isoionic Serum Albumin Solutions
    • Timasheff, S. N.; Dintzis, H. M.; Kirkwood, J. G.; Coleman, B. D. Light Scattering Investigation of Charge Fluctuations in Isoionic Serum Albumin Solutions J. Am. Chem. Soc. 1957, 79, 782-791
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 782-791
    • Timasheff, S.N.1    Dintzis, H.M.2    Kirkwood, J.G.3    Coleman, B.D.4
  • 17
    • 84984087319 scopus 로고
    • Specific interactions in proteins due to proton fluctuations
    • Timasheff, S. N. Specific interactions in proteins due to proton fluctuations Biopolymers 1966, 4, 107-120
    • (1966) Biopolymers , vol.4 , pp. 107-120
    • Timasheff, S.N.1
  • 18
    • 0029971050 scopus 로고    scopus 로고
    • Influence of Charge Regulation in Electrostatic Interaction Chromatography of Proteins
    • St'hlberg, J.; Jönsson, B. Influence of Charge Regulation in Electrostatic Interaction Chromatography of Proteins Anal. Chem. 1996, 68, 1536-1544
    • (1996) Anal. Chem. , vol.68 , pp. 1536-1544
    • St'hlberg, J.1    Jönsson, B.2
  • 19
    • 0034669239 scopus 로고    scopus 로고
    • Determination of effective protein charge by capillary electrophoresis: Effects of charge regulation in the analysis of charge ladders
    • Menon, M. K.; Zydney, A. L. Determination of effective protein charge by capillary electrophoresis: effects of charge regulation in the analysis of charge ladders Anal. Chem. 2000, 72, 5714-5717
    • (2000) Anal. Chem. , vol.72 , pp. 5714-5717
    • Menon, M.K.1    Zydney, A.L.2
  • 21
    • 73649110233 scopus 로고    scopus 로고
    • Field Theoretical Analysis of Driving Forces for the Uptake of Proteins by Like-Charged Polyelectrolyte Brushes: Effects of Charge Regulation and Patchiness
    • de Vos, W. M.; Leermakers, F. A. M.; de Keizer, A.; Cohen Stuart, M. A.; Kleijn, J. M. Field Theoretical Analysis of Driving Forces for the Uptake of Proteins by Like-Charged Polyelectrolyte Brushes: Effects of Charge Regulation and Patchiness Langmuir 2010, 26, 249-259
    • (2010) Langmuir , vol.26 , pp. 249-259
    • De Vos, W.M.1    Leermakers, F.A.M.2    De Keizer, A.3    Cohen Stuart, M.A.4    Kleijn, J.M.5
  • 23
    • 0000243480 scopus 로고
    • Forces between Protein Molecules in Solution Arising from Fluctuations in Proton Charge and Configuration
    • Kirkwood, J. G.; Shumaker, J. B. Forces Between Protein Molecules in Solution Arising from Fluctuations in Proton Charge and Configuration Proc. Natl. Acad. Sci. U.S.A. 1952, 38, 863-871
    • (1952) Proc. Natl. Acad. Sci. U.S.A. , vol.38 , pp. 863-871
    • Kirkwood, J.G.1    Shumaker, J.B.2
  • 24
    • 0001552389 scopus 로고    scopus 로고
    • Electrostatics of counter-ions in and between planar charged walls: From Poisson-Boltzmann to the strong-coupling theory
    • Netz, R. R. Electrostatics of counter-ions in and between planar charged walls: From Poisson-Boltzmann to the strong-coupling theory Eur. Phys. J. E. 2001, 5, 557-574
    • (2001) Eur. Phys. J. E. , vol.5 , pp. 557-574
    • Netz, R.R.1
  • 28
    • 0013080346 scopus 로고    scopus 로고
    • Titrating Polyelectrolytes - Variational Calculations and Monte Carlo Simulations
    • Jönsson, B.; Ullner, M.; Peterson, C.; Sommelius, O.; Söderberg, B. Titrating Polyelectrolytes-Variational Calculations and Monte Carlo Simulations J. Phys. Chem. 1996, 100, 409-417
    • (1996) J. Phys. Chem. , vol.100 , pp. 409-417
    • Jönsson, B.1    Ullner, M.2    Peterson, C.3    Sommelius, O.4    Söderberg, B.5
  • 30
    • 4444270810 scopus 로고    scopus 로고
    • The Role of Electrostatic Interactions in Calmodulin-Peptide Complex Formation
    • André, I.; Kesvatera, T.; Jönsson, B.; Åerfeldt, K. S.; Linse, S. The Role of Electrostatic Interactions in Calmodulin-Peptide Complex Formation Biophys. J. 2004, 87, 1929-1938
    • (2004) Biophys. J. , vol.87 , pp. 1929-1938
    • André, I.1    Kesvatera, T.2    Jönsson, B.3    Åerfeldt, K.S.4    Linse, S.5
  • 31
    • 67650034260 scopus 로고    scopus 로고
    • Ion-Ion Correlation and Charge Reversal at Titrating Solid Interfaces
    • Labbez, C.; Jönsson, B.; Skarba, M.; Borkovec, M. Ion-Ion Correlation and Charge Reversal at Titrating Solid Interfaces Langmuir 2009, 25, 7209-7213
    • (2009) Langmuir , vol.25 , pp. 7209-7213
    • Labbez, C.1    Jönsson, B.2    Skarba, M.3    Borkovec, M.4
  • 32
    • 20644431615 scopus 로고
    • Theory of Solutions of Molecules Containing Widely Separated Charges with Special Application to Zwitterions
    • Kirkwood, J. G. Theory of Solutions of Molecules Containing Widely Separated Charges with Special Application to Zwitterions J. Chem. Phys. 1934, 2, 351-361
    • (1934) J. Chem. Phys. , vol.2 , pp. 351-361
    • Kirkwood, J.G.1
  • 33
    • 33947468892 scopus 로고
    • Theory of Protein Titration Curves I. General Equations for Impenetrable spheres
    • Tanford, C.; Kirkwood, J. G. Theory of Protein Titration Curves I. General Equations for Impenetrable spheres J. Am. Chem. Soc. 1957, 79, 5333-5339
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 5333-5339
    • Tanford, C.1    Kirkwood, J.G.2
  • 37
    • 0042532737 scopus 로고    scopus 로고
    • Protein self-association in solution: The bovine β-lactoglobulin dimer and octamer
    • Gottschalk, M.; Nilsson, H.; Roos, H.; Halle, B. Protein self-association in solution: The bovine β-lactoglobulin dimer and octamer Protein Sci. 2003, 12, 2404-2411
    • (2003) Protein Sci. , vol.12 , pp. 2404-2411
    • Gottschalk, M.1    Nilsson, H.2    Roos, H.3    Halle, B.4
  • 38
    • 13244274907 scopus 로고    scopus 로고
    • Stability of HAMLET - A kinetically trapped α-lactalbumin oleic acid complex
    • Fast, J.; Mossberg, A.-K.; Svanborg, C.; Linse, S. Stability of HAMLET-A kinetically trapped α-lactalbumin oleic acid complex Protein Sci. 2005, 14, 329-340
    • (2005) Protein Sci. , vol.14 , pp. 329-340
    • Fast, J.1    Mossberg, A.-K.2    Svanborg, C.3    Linse, S.4
  • 39
    • 0034711229 scopus 로고    scopus 로고
    • Crystal structures of apo- and holo-bovine alpha-lactalbumin at 2.2-A resolution reveal an effect of calcium on inter-lobe interactions
    • Chrysina, E.; Brew, K.; Acharya, K. Crystal structures of apo- and holo-bovine alpha-lactalbumin at 2.2-A resolution reveal an effect of calcium on inter-lobe interactions J. Biol. Chem. 200, 275, 37021-37029
    • (2000) J. Biol. Chem. , vol.275 , pp. 37021-37029
    • Chrysina, E.1    Brew, K.2    Acharya, K.3
  • 41
    • 36749120155 scopus 로고
    • Excess chemical potential of dilute solutions of spherical polyelectrolytes
    • Phillies, G. D. J. Excess chemical potential of dilute solutions of spherical polyelectrolytes J. Chem. Phys. 1974, 60, 2721-2731
    • (1974) J. Chem. Phys. , vol.60 , pp. 2721-2731
    • Phillies, G.D.J.1
  • 42
    • 0037066876 scopus 로고    scopus 로고
    • Nonuniform Charge Effects in Protein-Protein Interactions
    • Grant, M. L. Nonuniform Charge Effects in Protein-Protein Interactions J. Phys. Chem. B 2001, 105, 2858-2863
    • (2001) J. Phys. Chem. B , vol.105 , pp. 2858-2863
    • Grant, M.L.1
  • 43
    • 0345455600 scopus 로고
    • Hydrogen Ion Equilibria of Ribonuclease
    • Tanford, C.; Hauenstein, J. D. Hydrogen Ion Equilibria of Ribonuclease J. Am. Chem. Soc. 1956, 78, 5287-5291
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 5287-5291
    • Tanford, C.1    Hauenstein, J.D.2
  • 47
    • 0030243083 scopus 로고    scopus 로고
    • A Monte Carlo Study of Titrating Polyelectrolytes in the Presence of Salt
    • Ullner, M.; Jönsson, B. A Monte Carlo Study of Titrating Polyelectrolytes in the Presence of Salt Macromolecules 1996, 29, 6645-6655
    • (1996) Macromolecules , vol.29 , pp. 6645-6655
    • Ullner, M.1    Jönsson, B.2
  • 49
    • 70349881890 scopus 로고    scopus 로고
    • Association and electrostatic steering of alpha-lactalbumin-lysozyme heterodimers
    • Persson, B. A.; Lund, M. Association and electrostatic steering of alpha-lactalbumin-lysozyme heterodimers Phys. Chem. Chem. Phys. 2009, 11, 8879-8885
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 8879-8885
    • Persson, B.A.1    Lund, M.2
  • 50
    • 0001461682 scopus 로고
    • Examination of titration behavior
    • Nozaki, Y.; Tanford, C. Examination of titration behavior Methods Enzymol. 1967, 11, 715-734
    • (1967) Methods Enzymol. , vol.11 , pp. 715-734
    • Nozaki, Y.1    Tanford, C.2
  • 51
    • 34250702227 scopus 로고    scopus 로고
    • Implications of a high dielectric constant in proteins
    • Lund, M.; Jönsson, B.; Woodward, C. E. Implications of a high dielectric constant in proteins J. Chem. Phys. 2007, 126, 225103-225110
    • (2007) J. Chem. Phys. , vol.126 , pp. 225103-225110
    • Lund, M.1    Jönsson, B.2    Woodward, C.E.3
  • 53
    • 0034974669 scopus 로고    scopus 로고
    • A critical investigation of the Tanford-Kirkwood scheme by means of Monte Carlo simulations
    • da Silva, F. L. B.; Jönsson, B.; Penfold, R. A critical investigation of the Tanford-Kirkwood scheme by means of Monte Carlo simulations Protein Sci. 2001, 10, 1415-1425
    • (2001) Protein Sci. , vol.10 , pp. 1415-1425
    • Da Silva, F.L.B.1    Jönsson, B.2    Penfold, R.3
  • 54
    • 58149166568 scopus 로고    scopus 로고
    • Protein-Ion Binding Process on Finite Macromolecular Concentration. A Poisson-Boltzmann and Monte Carlo Study
    • de Carvalho, S. J.; Fenley, M. O.; da Silva, F. L. B. Protein-Ion Binding Process on Finite Macromolecular Concentration. A Poisson-Boltzmann and Monte Carlo Study J. Phys. Chem. B 2008, 112, 16766-16776
    • (2008) J. Phys. Chem. B , vol.112 , pp. 16766-16776
    • De Carvalho, S.J.1    Fenley, M.O.2    Da Silva, F.L.B.3
  • 55
    • 0000979954 scopus 로고    scopus 로고
    • Electrostatic Models for Calcium Binding Proteins
    • Penfold, R.; Warwicker, J.; Jönsson, B. Electrostatic Models for Calcium Binding Proteins J. Phys. Chem. B 1998, 102, 8599-8610
    • (1998) J. Phys. Chem. B , vol.102 , pp. 8599-8610
    • Penfold, R.1    Warwicker, J.2    Jönsson, B.3
  • 56
    • 0032586777 scopus 로고    scopus 로고
    • a and acid pH-dependent stability estimation in proteins: Removing dielectric and counterion boundaries
    • a and acid pH-dependent stability estimation in proteins: Removing dielectric and counterion boundaries Protein Sci. 1999, 8, 418-425
    • (1999) Protein Sci. , vol.8 , pp. 418-425
    • Warwicker, J.1
  • 57
    • 0017885434 scopus 로고
    • Brownian Motion of Highly Charged Poly(L-lysine). Effects of salt and polyion concentration
    • Lin, S.-C.; Lee, W. I.; Shurr, J. M. Brownian Motion of Highly Charged Poly(L-lysine). Effects of salt and polyion concentration Biopolymers 1978, 17, 1041-1064
    • (1978) Biopolymers , vol.17 , pp. 1041-1064
    • Lin, S.-C.1    Lee, W.I.2    Shurr, J.M.3
  • 59
    • 0005417419 scopus 로고    scopus 로고
    • Effective ionic charges, permittivity and screening length: Dressed ion theory applied to 1:2 electrolyte solutions
    • Kjellander, R.; Ulander, J. Effective ionic charges, permittivity and screening length: dressed ion theory applied to 1:2 electrolyte solutions Mol. Phys. 1996, 95, 495-505
    • (1996) Mol. Phys. , vol.95 , pp. 495-505
    • Kjellander, R.1    Ulander, J.2
  • 60
    • 0020935448 scopus 로고
    • Electrical double-layer interactions in concentrated colloidal systems
    • Beresford-Smith, B.; Chan, D. Y. C. Electrical double-layer interactions in concentrated colloidal systems Faraday Discuss. Chem. Soc. 1983, 76, 65-75
    • (1983) Faraday Discuss. Chem. Soc. , vol.76 , pp. 65-75
    • Beresford-Smith, B.1    Chan, D.Y.C.2
  • 61
    • 13444257969 scopus 로고    scopus 로고
    • Binding of Charged Ligands to Macromolecules. Anomalous Salt Dependence
    • da Silva, F. L. B.; Linse, S.; Jönsson, B. Binding of Charged Ligands to Macromolecules. Anomalous Salt Dependence J. Phys. Chem. B 2005, 109, 2007-2013
    • (2005) J. Phys. Chem. B , vol.109 , pp. 2007-2013
    • Da Silva, F.L.B.1    Linse, S.2    Jönsson, B.3
  • 62
    • 33751298792 scopus 로고    scopus 로고
    • Testing the relevance of effective interaction potentials between highly-charged colloids in suspension
    • Dobnikar, J.; Castañeda Priego, R.; Grünberg, H. H. V.; Trizac, E. Testing the relevance of effective interaction potentials between highly-charged colloids in suspension New J. Phys. 2006, 8, 277+
    • (2006) New J. Phys. , vol.8
    • Dobnikar, J.1    Castañeda Priego, R.2    Grünberg, H.H.V.3    Trizac, E.4
  • 63
    • 40749110634 scopus 로고    scopus 로고
    • Faunus: An object oriented framework for molecular simulation
    • [doi:10.1186/1751-0473-3-1]
    • Lund, M.; Trulsson, M.; Persson, B. Faunus: An object oriented framework for molecular simulation Source Code Biol. Med. 2008, 3:1 [doi:10.1186/1751- 0473-3-1].
    • (2008) Source Code Biol. Med. , pp. 31
    • Lund, M.1    Trulsson, M.2    Persson, B.3
  • 66
    • 0024347869 scopus 로고
    • Lactoferrin from human breast milk and from neutrophil granulocytes. Comparative studies of isolation, quantitation, characterization and iron binding properties
    • Bezwoda, W. R.; Mansoor, N. Lactoferrin from human breast milk and from neutrophil granulocytes. Comparative studies of isolation, quantitation, characterization and iron binding properties Biomed. Chromatogr. 1989, 3, 121-126
    • (1989) Biomed. Chromatogr. , vol.3 , pp. 121-126
    • Bezwoda, W.R.1    Mansoor, N.2
  • 67
    • 0034492988 scopus 로고    scopus 로고
    • Occurrence, structure, biochemical properties and technological characterist ics of lactoferrin
    • Steijns, J. M.; van Hooijdonk, A. C. M. Occurrence, structure, biochemical properties and technological characterist ics of lactoferrin Br. J. Nutr. 2000, 84, 11-17
    • (2000) Br. J. Nutr. , vol.84 , pp. 11-17
    • Steijns, J.M.1    Van Hooijdonk, A.C.M.2
  • 68
    • 58149125767 scopus 로고    scopus 로고
    • A structural framework for understanding the multifunctional character of lactoferrin
    • Baker, E.; Baker, H. A structural framework for understanding the multifunctional character of lactoferrin Biochimie 2009, 91, 3-10
    • (2009) Biochimie , vol.91 , pp. 3-10
    • Baker, E.1    Baker, H.2


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