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Volumn 4, Issue 9, 2009, Pages 1305-1319

Lysozyme-lysozyme self-interactions as assessed by the osmotic second virial coefficient: Impact for physical protein stabilization

Author keywords

B22; Lysozyme; Osmotic second virial coefficient; Protein protein interaction; Self interaction chromatography; Stabilization

Indexed keywords

B22; LYSOZYME; OSMOTIC SECOND VIRIAL COEFFICIENT; PROTEIN-PROTEIN INTERACTION; SELF-INTERACTION CHROMATOGRAPHY;

EID: 70350123028     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.200800274     Document Type: Article
Times cited : (41)

References (106)
  • 2
    • 33747488943 scopus 로고    scopus 로고
    • Formulation and delivery issues for monoclonal antibody therapeutics
    • Daugherty, A. L., Mrsny, R. J., Formulation and delivery issues for monoclonal antibody therapeutics. Adv. Drug Deliv. Rev. 2006, 58, 686-706.
    • (2006) Adv. Drug Deliv. Rev , vol.58 , pp. 686-706
    • Daugherty, A.L.1    Mrsny, R.J.2
  • 4
    • 33947544337 scopus 로고    scopus 로고
    • Highly concentrated monoclonal antibody solutions: Direct analysis of physical structure and thermal stability
    • Harn, N., Allan, C., Oliver, C., Middaugh, C. R., Highly concentrated monoclonal antibody solutions: Direct analysis of physical structure and thermal stability. J. Pharm. Sci. 2007, 96, 532-546.
    • (2007) J. Pharm. Sci , vol.96 , pp. 532-546
    • Harn, N.1    Allan, C.2    Oliver, C.3    Middaugh, C.R.4
  • 5
    • 0041931122 scopus 로고    scopus 로고
    • Macromolecular crowding: Qualitative and semiquantitative successes, quantitative challenges
    • Hall, D., Minton, A.P., Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges. Biochim. Biophys. Acta 2003, 1649, 127-139.
    • (2003) Biochim. Biophys. Acta , vol.1649 , pp. 127-139
    • Hall, D.1    Minton, A.P.2
  • 6
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • Zimmerman, S. B., Minton, A. P., Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 1993, 22, 27-65.
    • (1993) Annu. Rev. Biophys. Biomol. Struct , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 7
    • 48149088072 scopus 로고    scopus 로고
    • Fourier-transform midinfrared spectroscopy for analysis and screening of liquid protein formulations. Part 2: Detailed analysis and applications
    • Garidel, P., Schott, H., Fourier-transform midinfrared spectroscopy for analysis and screening of liquid protein formulations. Part 2: detailed analysis and applications. Bio-Process Int. 2006, 4, 48-55.
    • (2006) Bio-Process Int , vol.4 , pp. 48-55
    • Garidel, P.1    Schott, H.2
  • 8
    • 37949050629 scopus 로고    scopus 로고
    • Fourier-transform midinfrared spectroscopy for analysis and screening of liquid protein formulations. Part 1: Understanding infrared spectroscopy of protein
    • Garidel, P., Schott, H., Fourier-transform midinfrared spectroscopy for analysis and screening of liquid protein formulations. Part 1: understanding infrared spectroscopy of protein. BioProcess Int. 2006, 4, 40-46.
    • (2006) BioProcess Int , vol.4 , pp. 40-46
    • Garidel, P.1    Schott, H.2
  • 9
    • 33745413982 scopus 로고    scopus 로고
    • Protein structural conformation and not second virial coefficient relates to long-term irreversible aggregation of a monoclonal antibody and ovalbumin in solution
    • Bajaj, H., Sharma, V. K., Badkar, A., Zeng, D. et al., Protein structural conformation and not second virial coefficient relates to long-term irreversible aggregation of a monoclonal antibody and ovalbumin in solution. Pharm. Res. 2006, 23, 1382-1394.
    • (2006) Pharm. Res , vol.23 , pp. 1382-1394
    • Bajaj, H.1    Sharma, V.K.2    Badkar, A.3    Zeng, D.4
  • 10
    • 42749106393 scopus 로고    scopus 로고
    • Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions
    • 051404/1-051404/13
    • Allahyarov, E., Lowen, H., Hansen, J. P., Louis, A. A., Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions. Phys. Rev. E Stat. Nonlin Soft. Matter Phys. 2003, 67, 051404/1-051404/13.
    • (2003) Phys. Rev. E Stat. Nonlin Soft. Matter Phys , vol.67
    • Allahyarov, E.1    Lowen, H.2    Hansen, J.P.3    Louis, A.A.4
  • 11
    • 34248174892 scopus 로고    scopus 로고
    • Protein-polysaccharide interactions: The determination of the osmotic second virial coefficients in aqueous solutions of beta-lactoglobulin and dextran
    • Schaink, H. M., Smit, J. A. M., Protein-polysaccharide interactions: The determination of the osmotic second virial coefficients in aqueous solutions of beta-lactoglobulin and dextran. Food Hydrocolloids 2007, 21, 1389-1396.
    • (2007) Food Hydrocolloids , vol.21 , pp. 1389-1396
    • Schaink, H.M.1    Smit, J.A.M.2
  • 12
    • 0037444490 scopus 로고    scopus 로고
    • The effects of added salt on the second virial coefficients of the complete proteome of E-coli
    • Sear, R. P., The effects of added salt on the second virial coefficients of the complete proteome of E-coli. J. Chem. Phys. 2003, 118, 5157-5161.
    • (2003) J. Chem. Phys , vol.118 , pp. 5157-5161
    • Sear, R.P.1
  • 13
    • 28444457469 scopus 로고    scopus 로고
    • Second virial coefficient studies of cosolvent-induced protein self-interaction
    • Valente, J. J., Verma, K. S., Manning, M.C., Wilson, W.W. et al., Second virial coefficient studies of cosolvent-induced protein self-interaction. Biophys. J. 2005, 89, 4211-4218.
    • (2005) Biophys. J , vol.89 , pp. 4211-4218
    • Valente, J.J.1    Verma, K.S.2    Manning, M.C.3    Wilson, W.W.4
  • 14
    • 0035142983 scopus 로고    scopus 로고
    • Calculation of weak proteinprotein interactions:The pH dependence of the second virial coefficient
    • Elcock, A. H., McCammon, J.A., Calculation of weak proteinprotein interactions:The pH dependence of the second virial coefficient. Biophys. J. 2001, 80, 613-625.
    • (2001) Biophys. J , vol.80 , pp. 613-625
    • Elcock, A.H.1    McCammon, J.A.2
  • 15
    • 0034728419 scopus 로고    scopus 로고
    • Osmotic pressures and second virial coefficients for aqueous saline solutions of lysozyme
    • Moon, Y. U., Anderson, C. O., Blanch, H.W., Prausnitz, J. M., Osmotic pressures and second virial coefficients for aqueous saline solutions of lysozyme. Fluid Phase Equilib. 2000, 168, 229-239.
    • (2000) Fluid Phase Equilib , vol.168 , pp. 229-239
    • Moon, Y.U.1    Anderson, C.O.2    Blanch, H.W.3    Prausnitz, J.M.4
  • 16
    • 3242687186 scopus 로고    scopus 로고
    • Detection of aggregate formation during production of human immunoglobulin G by means of light scattering
    • Ahrer, K., Buchacher, A., Iberer,G., Junbauer,A. Detection of aggregate formation during production of human immunoglobulin G by means of light scattering. J. Chrom. A. 2004, 1043, 41-46.
    • (2004) J. Chrom. A , vol.1043 , pp. 41-46
    • Ahrer, K.1    Buchacher, A.2    Iberer, G.3    Junbauer, A.4
  • 17
    • 10044279535 scopus 로고    scopus 로고
    • Determination of second virial coefficient of proteins using a dual-detector cell for simultaneous measurement of scattered light intensity and concentration in SEC-HPLC
    • Bajaj, H., Sharma,V. K., Kalonia,D. S., Determination of second virial coefficient of proteins using a dual-detector cell for simultaneous measurement of scattered light intensity and concentration in SEC-HPLC. Biophys. J. 2004, 87, 4048-4055.
    • (2004) Biophys. J , vol.87 , pp. 4048-4055
    • Bajaj, H.1    Sharma, V.K.2    Kalonia, D.S.3
  • 18
    • 33644683427 scopus 로고    scopus 로고
    • Negative second virial coefficients as predictors of protein crystal growth: Evidence from sedimentation equilibrium studies that refutes the designation of those light scattering parameters as osmotic virial coefficients
    • Deszczynski, M., Harding, S. E., Winzor, D. J., Negative second virial coefficients as predictors of protein crystal growth: Evidence from sedimentation equilibrium studies that refutes the designation of those light scattering parameters as osmotic virial coefficients. Biophys. Chem. 2006, 120, 106-113.
    • (2006) Biophys. Chem , vol.120 , pp. 106-113
    • Deszczynski, M.1    Harding, S.E.2    Winzor, D.J.3
  • 19
    • 1942489413 scopus 로고    scopus 로고
    • Correlation of diafiltration sieving behavior of lysozyme-BSA mixtures with osmotic second virial cross-coefficients
    • Tessier, P. M., Verruto,V. J., Sandler, S. I., Lenhoff,A. M., Correlation of diafiltration sieving behavior of lysozyme-BSA mixtures with osmotic second virial cross-coefficients. Biotechnol. Bioeng. 2004, 87, 303-310.
    • (2004) Biotechnol. Bioeng , vol.87 , pp. 303-310
    • Tessier, P.M.1    Verruto, V.J.2    Sandler, S.I.3    Lenhoff, A.M.4
  • 20
    • 1942473133 scopus 로고    scopus 로고
    • Direct measurement of protein osmotic second virial cross coefficients by cross-interaction chromatography
    • Tessier, P. M., Sandler, S. I., Lenhoff, A. M., Direct measurement of protein osmotic second virial cross coefficients by cross-interaction chromatography. Protein Sci. 2004, 13, 1379-1390.
    • (2004) Protein Sci , vol.13 , pp. 1379-1390
    • Tessier, P.M.1    Sandler, S.I.2    Lenhoff, A.M.3
  • 21
    • 35148854475 scopus 로고    scopus 로고
    • A simpler analysis for the measurement of second virial coefficients by self-interaction chromatography
    • Winzor, D. J., Scott, D. J.,Wills, P. R., A simpler analysis for the measurement of second virial coefficients by self-interaction chromatography. Anal. Biochem. 2007, 371, 21-25.
    • (2007) Anal. Biochem , vol.371 , pp. 21-25
    • Winzor, D.J.1    Scott, D.J.2    Wills, P.R.3
  • 22
    • 34247644354 scopus 로고    scopus 로고
    • Nonequivalence of second virial coefficients from sedimentation equilibrium and static light scattering studies of protein solutions
    • Winzor, D. J., Deszczynski, M., Harding, S. E., Wills, P.R., Nonequivalence of second virial coefficients from sedimentation equilibrium and static light scattering studies of protein solutions. Biophys. Chem. 2007, 128, 46-55.
    • (2007) Biophys. Chem , vol.128 , pp. 46-55
    • Winzor, D.J.1    Deszczynski, M.2    Harding, S.E.3    Wills, P.R.4
  • 23
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: A tutorial review
    • Lebowitz, J., Lewis, M. S., Schuck, P., Modern analytical ultracentrifugation in protein science: A tutorial review. Protein Sci. 2002, 11, 2067-2079.
    • (2002) Protein Sci , vol.11 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 24
    • 0003300676 scopus 로고    scopus 로고
    • Alternative strategies for the characterization of associations in multicomponent solutions via measurement of sedimentation equilibrium
    • Minton, A. P., Alternative strategies for the characterization of associations in multicomponent solutions via measurement of sedimentation equilibrium. Prog. Colloid Polym. Sci. 1997, 107, 11-19.
    • (1997) Prog. Colloid Polym. Sci , vol.107 , pp. 11-19
    • Minton, A.P.1
  • 25
    • 0034737606 scopus 로고    scopus 로고
    • Quantitative characterization of reversible macromolecular associations via sedimentation equilibrium: An introduction
    • Minton, A. P., Quantitative characterization of reversible macromolecular associations via sedimentation equilibrium: an introduction. Exp. Mol. Med. 2000, 32, 1-5.
    • (2000) Exp. Mol. Med , vol.32 , pp. 1-5
    • Minton, A.P.1
  • 26
    • 0032743935 scopus 로고    scopus 로고
    • Chromatographic methods to study protein-protein interactions
    • Beeckmans, S., Chromatographic methods to study protein-protein interactions. Methods 1999, 19, 278-305.
    • (1999) Methods , vol.19 , pp. 278-305
    • Beeckmans, S.1
  • 28
    • 10144225635 scopus 로고    scopus 로고
    • Self-interaction chromatography: A tool for the study of protein-protein interactions in bioprocessing environments
    • Patro, S.Y., Przybycien,T. M., Self-interaction chromatography: A tool for the study of protein-protein interactions in bioprocessing environments. Biotechnol. Bioeng. 1996, 52, 193-203.
    • (1996) Biotechnol. Bioeng , vol.52 , pp. 193-203
    • Patro, S.Y.1    Przybycien, T.M.2
  • 29
    • 0034454326 scopus 로고    scopus 로고
    • Performance of affinity chromatography with peptide ligands: Influence of spacer, matrix composition and immobilization chemistry
    • Hahn, R.,Amatschek, K., Schallaun, E., Necina, R. et al., Performance of affinity chromatography with peptide ligands: Influence of spacer, matrix composition and immobilization chemistry. Int. J. Bio-Chromatogr. 2000, 5, 175-185.
    • (2000) Int. J. Bio-Chromatogr , vol.5 , pp. 175-185
    • Hahn, R.1    Amatschek, K.2    Schallaun, E.3    Necina, R.4
  • 30
    • 0142246549 scopus 로고    scopus 로고
    • A personal perspective
    • The development of chromatography for the characterization of protein interactions
    • Winzor, D. J., The development of chromatography for the characterization of protein interactions: A personal perspective. Biochem. Soc.Trans. 2003, 31, 1010-1014.
    • (2003) Biochem. Soc.Trans , vol.31 , pp. 1010-1014
    • Winzor, D.J.1
  • 32
    • 0023046621 scopus 로고
    • Analysis of protein-protein interaction by simulation of small-zone size-exclusion chromatography: Application to an antibody-antigen association
    • Stevens, F. J.,Analysis of protein-protein interaction by simulation of small-zone size-exclusion chromatography: Application to an antibody-antigen association. Biochemistry 1986, 25, 981-993.
    • (1986) Biochemistry , vol.25 , pp. 981-993
    • Stevens, F.J.1
  • 33
    • 0030571043 scopus 로고    scopus 로고
    • Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions
    • Wen, J., Arakawa,T., Philo, J.S., Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal. Biochem. 1996, 240, 155-166.
    • (1996) Anal. Biochem , vol.240 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 34
    • 0026506216 scopus 로고
    • Study of the adsorption of self-associating proteins on an anion exchanger: Application to the chromatography of β-lactoglobulin B
    • Lemque, R., Jaulmes, A., Sébille, B., Vidal-Madjar, C. et al., Study of the adsorption of self-associating proteins on an anion exchanger: Application to the chromatography of β-lactoglobulin B. J. Chrom. 1992, 599, 255-265.
    • (1992) J. Chrom , vol.599 , pp. 255-265
    • Lemque, R.1    Jaulmes, A.2    Sébille, B.3    Vidal-Madjar, C.4
  • 35
    • 0031950561 scopus 로고    scopus 로고
    • Protein-protein interactions as a means of purification
    • Przybycien, T. M., Protein-protein interactions as a means of purification. Curr. Opin. Biotechnol. 1998, 9, 164-170.
    • (1998) Curr. Opin. Biotechnol , vol.9 , pp. 164-170
    • Przybycien, T.M.1
  • 36
    • 0141754043 scopus 로고    scopus 로고
    • Measurements of protein protein interactions by size exclusion chromatography
    • Bloustine, J., Berejnov,V., Fraden, S., Measurements of protein protein interactions by size exclusion chromatography. Biophys. J. 2003, 85, 2619-2623.
    • (2003) Biophys. J , vol.85 , pp. 2619-2623
    • Bloustine, J.1    Berejnov, V.2    Fraden, S.3
  • 37
    • 36849131807 scopus 로고
    • Application of the methods of molecular distribution to solutions of large molecules
    • Zimm,B. H., Application of the methods of molecular distribution to solutions of large molecules. J. Chem. Phys. 1946, 14, 164-179.
    • (1946) J. Chem. Phys , vol.14 , pp. 164-179
    • Zimm, B.H.1
  • 38
    • 23544458810 scopus 로고
    • The statistical thermodynamics of multicomponent systems
    • McMillan,W.G.,Mayer, J. E.,The statistical thermodynamics of multicomponent systems. J. Chem. Phys. 1945, 13, 276-305.
    • (1945) J. Chem. Phys , vol.13 , pp. 276-305
    • McMillan, W.G.1    Mayer, J.E.2
  • 39
    • 0033513785 scopus 로고    scopus 로고
    • Second virial coefficient: Variations with lysozyme crystallization conditions
    • Bonnete, F., Finet, S., Tardieu, A., Second virial coefficient: variations with lysozyme crystallization conditions. J. Crys. Growth 1999, 196, 403-414.
    • (1999) J. Crys. Growth , vol.196 , pp. 403-414
    • Bonnete, F.1    Finet, S.2    Tardieu, A.3
  • 40
    • 0036794625 scopus 로고    scopus 로고
    • Interest of the normalized second virial coefficient and interaction potentials for crystallizing large macromolecules
    • Bonnete, F., Vivares, D., Interest of the normalized second virial coefficient and interaction potentials for crystallizing large macromolecules. Acta Crystallogr. D Biol. Crystallogr. 2002, 58, 1571-1575.
    • (2002) Acta Crystallogr. D Biol. Crystallogr , vol.58 , pp. 1571-1575
    • Bonnete, F.1    Vivares, D.2
  • 41
    • 0031053090 scopus 로고    scopus 로고
    • Second virial coefficient as predictor in protein crystal growth
    • George, A., Chiang, Y., Guo, B., Arabshahi, A. et al., Second virial coefficient as predictor in protein crystal growth. Macromol. Crystallogr. 1997, 276, 100-110.
    • (1997) Macromol. Crystallogr , vol.276 , pp. 100-110
    • George, A.1    Chiang, Y.2    Guo, B.3    Arabshahi, A.4
  • 42
    • 0033513739 scopus 로고    scopus 로고
    • Correlation of second virial coefficients and solubilities useful in protein crystal growth
    • Guo, B., Kao, S., McDonald, H., Asanov, A. et al., Correlation of second virial coefficients and solubilities useful in protein crystal growth. J. Crys. Growth 1999, 196, 424-433.
    • (1999) J. Crys. Growth , vol.196 , pp. 424-433
    • Guo, B.1    Kao, S.2    McDonald, H.3    Asanov, A.4
  • 43
    • 0033513738 scopus 로고    scopus 로고
    • Why is the osmotic second virial coefficient related to protein crystallization?
    • Neal, B. L., Asthagiri, D., Velev, O.D., Lenhoff, A.M. et al.,Why is the osmotic second virial coefficient related to protein crystallization? J. Crys. Growth 1999, 196, 377-387.
    • (1999) J. Crys. Growth , vol.196 , pp. 377-387
    • Neal, B.L.1    Asthagiri, D.2    Velev, O.D.3    Lenhoff, A.M.4
  • 44
    • 0037295516 scopus 로고    scopus 로고
    • Predictive crystallization of ribonuclease A via rapid screening of osmotic second virial coefficients
    • Tessier, P. M., Johnson, H. R., Pazhianur, R., Berger, B.W. et al., Predictive crystallization of ribonuclease A via rapid screening of osmotic second virial coefficients. Proteins: Structure, Function, and Genetics 2003, 50, 303-311.
    • (2003) Proteins: Structure, Function, and Genetics , vol.50 , pp. 303-311
    • Tessier, P.M.1    Johnson, H.R.2    Pazhianur, R.3    Berger, B.W.4
  • 45
    • 0036794725 scopus 로고    scopus 로고
    • Self-interaction chromatography: A novel screening method for rational protein crystallization
    • Tessier, P. M., Vandrey, S. D., Berger, S. D., Pazhianur, R., et al., Self-interaction chromatography: A novel screening method for rational protein crystallization. Acta Crystallograph. D Biol. Crystallogr. 2002, 58, 1531-1535.
    • (2002) Acta Crystallograph. D Biol. Crystallogr , vol.58 , pp. 1531-1535
    • Tessier, P.M.1    Vandrey, S.D.2    Berger, S.D.3    Pazhianur, R.4
  • 46
    • 26444571904 scopus 로고    scopus 로고
    • Protein crystal nucleation: Is the pair interaction potential the primary determinant of kinetics?
    • Bhamidi,V., Varanasi, S., Schall, C. A., Protein crystal nucleation: Is the pair interaction potential the primary determinant of kinetics? Langmuir 2005, 21, 9044-9050.
    • (2005) Langmuir , vol.21 , pp. 9044-9050
    • Bhamidi, V.1    Varanasi, S.2    Schall, C.A.3
  • 47
    • 49549102447 scopus 로고    scopus 로고
    • Salting-out of lysozyme and ovalbumin from mixtures: Predicting precipitation performance from protein-protein interactions
    • Cheng,Y. C., Bianco, C. L., Sandler, S. I:, Lenhoff,A. M., Salting-out of lysozyme and ovalbumin from mixtures: Predicting precipitation performance from protein-protein interactions. Ind. Eng. Chem. Res. 2008, 47, 5203-5213.
    • (2008) Ind. Eng. Chem. Res , vol.47 , pp. 5203-5213
    • Cheng, Y.C.1    Bianco, C.L.2    Sandler, S.I.3    Lenhoff, A.M.4
  • 48
    • 0142122294 scopus 로고    scopus 로고
    • Measurements of protein self-association as a guide to crystallization
    • Tessier, P. M., Lenhoff,A. M., Measurements of protein self-association as a guide to crystallization. Curr. Opin. Biotechnol. 2003, 14, 512-516.
    • (2003) Curr. Opin. Biotechnol , vol.14 , pp. 512-516
    • Tessier, P.M.1    Lenhoff, A.M.2
  • 49
    • 23044505404 scopus 로고    scopus 로고
    • Design of self-interaction chromatography as an analytical tool for predicting protein phase behavior
    • Ahamed,T., Ottens, M., van Dedem,G.W. K., van der Wielen, L. A. M., Design of self-interaction chromatography as an analytical tool for predicting protein phase behavior. J. Chrom. A 2005, 1089, 11-124.
    • (2005) J. Chrom. A , vol.1089 , pp. 11-124
    • Ahamed, T.1    Ottens, M.2    van Dedem, G.W.K.3    van der Wielen, L.A.M.4
  • 50
    • 0001516764 scopus 로고    scopus 로고
    • Relation between the solubility of proteins in aqueous solutions and the second virial coefficient of the solution
    • Haas, C., Drenth, J., Wilson,W.W., Relation between the solubility of proteins in aqueous solutions and the second virial coefficient of the solution. J. Phys. Chem. B 1999, 103, 2808-2811.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 2808-2811
    • Haas, C.1    Drenth, J.2    Wilson, W.W.3
  • 51
    • 0037378389 scopus 로고    scopus 로고
    • Ho, J.G. S., Middelberg, A. P. J., Ramag,e P., Kocher,H. P.,The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient. Protein Sci. 2003, 12, 708-716.
    • Ho, J.G. S., Middelberg, A. P. J., Ramag,e P., Kocher,H. P.,The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient. Protein Sci. 2003, 12, 708-716.
  • 52
    • 0031723926 scopus 로고    scopus 로고
    • Molecular origins of osmotic second virial coefficients of proteins
    • Neal, B. L., Asthagiri,D., Lenhoff, A. M., Molecular origins of osmotic second virial coefficients of proteins. Biophys. J. 1998, 75, 2469-2477.
    • (1998) Biophys. J , vol.75 , pp. 2469-2477
    • Neal, B.L.1    Asthagiri, D.2    Lenhoff, A.M.3
  • 53
    • 31344474356 scopus 로고    scopus 로고
    • Colloidal behavior of proteins: Effects of the second virial coefficient on solubility, crystallization and aggregation of proteins in aqueous solution
    • Valente, J. J., Payne, R.W., Manning, M.C., Wilson, W.W. et al., Colloidal behavior of proteins: effects of the second virial coefficient on solubility, crystallization and aggregation of proteins in aqueous solution. Curr. Pharm. Biotechnol. 2005, 6, 427-436.
    • (2005) Curr. Pharm. Biotechnol , vol.6 , pp. 427-436
    • Valente, J.J.1    Payne, R.W.2    Manning, M.C.3    Wilson, W.W.4
  • 54
    • 36849104120 scopus 로고
    • Percus-Yevick equation for hard spheres with surface adhesion
    • Baxter, R. J., Percus-Yevick equation for hard spheres with surface adhesion. J. Chem. Phys. 1968, 49, 2770-2774.
    • (1968) J. Chem. Phys , vol.49 , pp. 2770-2774
    • Baxter, R.J.1
  • 55
    • 5844235959 scopus 로고    scopus 로고
    • Phase behavior of small attractive colloidal particles
    • Rosenbaum,D., Zamora, P. C., Zukoski, C. F., Phase behavior of small attractive colloidal particles. Phys. Rev. Lett. 1996, 76, 150-153.
    • (1996) Phys. Rev. Lett , vol.76 , pp. 150-153
    • Rosenbaum, D.1    Zamora, P.C.2    Zukoski, C.F.3
  • 56
    • 0030566439 scopus 로고    scopus 로고
    • Protein interactions and crystallization
    • Rosenbaum, D. F., Zukoski, C. F., Protein interactions and crystallization. J. Crys. Growth 1996, 169, 752-758.
    • (1996) J. Crys. Growth , vol.169 , pp. 752-758
    • Rosenbaum, D.F.1    Zukoski, C.F.2
  • 57
    • 36048955752 scopus 로고    scopus 로고
    • Osmotic second virial coefficients and phase diagrams for aqueous proteins from a much-improved Poisson-Boltzmann equation
    • Lima, E. R. A., Biscaia, E. C., Bostrom, M.,Tavares, F.W. et al., Osmotic second virial coefficients and phase diagrams for aqueous proteins from a much-improved Poisson-Boltzmann equation. J. Phys. Chem. C 2007, 111, 16055-16059.
    • (2007) J. Phys. Chem. C , vol.111 , pp. 16055-16059
    • Lima, E.R.A.1    Biscaia, E.C.2    Bostrom, M.3    Tavares, F.W.4
  • 58
    • 0035121714 scopus 로고    scopus 로고
    • Correlation between the osmotic second virial coefficient and the solubility of proteins
    • Ruppert, S., Sandler, S. I., Lenhoff, A. M., Correlation between the osmotic second virial coefficient and the solubility of proteins. Biotechnol. Prog. 2001, 17, 182-187.
    • (2001) Biotechnol. Prog , vol.17 , pp. 182-187
    • Ruppert, S.1    Sandler, S.I.2    Lenhoff, A.M.3
  • 59
    • 33947478967 scopus 로고
    • Theory of the Donnan membrane equilibrium 2. calculation of the osmotic pressure and of the salt distribution in a Donnan system with highly charged colloid particles
    • Stigter, D., Hill, T. L.,Theory of the Donnan membrane equilibrium 2. calculation of the osmotic pressure and of the salt distribution in a Donnan system with highly charged colloid particles. J. Phys. Chem. 1959, 63, 551-556.
    • (1959) J. Phys. Chem , vol.63 , pp. 551-556
    • Stigter, D.1    Hill, T.L.2
  • 60
    • 70350106011 scopus 로고    scopus 로고
    • Die Bedeutung des zweiten osmotischen Virialkoeffizienten für die Proteinkristallization.
    • Wanka, J., Peukert, W., Die Bedeutung des zweiten osmotischen Virialkoeffizienten für die Proteinkristallization. Chemie Ing. Tech. 2008, 2996, 273-278.
    • (2008) Chemie Ing. Tech , vol.2996 , pp. 273-278
    • Wanka, J.1    Peukert, W.2
  • 61
    • 0026169665 scopus 로고
    • An approach to determine the 2nd virial-coefficient for calculation of phase-equilibria in water-protein-neutral polymer systems
    • Polyakov, V. I., Dezhenkova, L. G., Vainerman, E.S., An approach to determine the 2nd virial-coefficient for calculation of phase-equilibria in water-protein-neutral polymer systems. Polymer Bulletin 1991, 25, 709-716.
    • (1991) Polymer Bulletin , vol.25 , pp. 709-716
    • Polyakov, V.I.1    Dezhenkova, L.G.2    Vainerman, E.S.3
  • 62
    • 33750520125 scopus 로고    scopus 로고
    • Effect of salts and organic additives on the solubility of proteins in aqueous solutions
    • Ruckenstein, E., Shulgin, I.L., Effect of salts and organic additives on the solubility of proteins in aqueous solutions. Adv. Colloid Interface Sci. 2006, 123, 97-103.
    • (2006) Adv. Colloid Interface Sci , vol.123 , pp. 97-103
    • Ruckenstein, E.1    Shulgin, I.L.2
  • 63
    • 57249093785 scopus 로고    scopus 로고
    • Various contributions to the osmotic second virial coefficient in protein-water-cosolvent solutions
    • Shulgin, I. L., Ruckenstein, E.,Various contributions to the osmotic second virial coefficient in protein-water-cosolvent solutions. J. Phys. Chem. B 2008, 112, 14665-14671.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 14665-14671
    • Shulgin, I.L.1    Ruckenstein, E.2
  • 64
    • 39149104991 scopus 로고    scopus 로고
    • Recent applications of Kirkwood-Buff theory to biological systems
    • Pierce, V., Kang, M., Aburi, M.,Weerasinghe, S. et al., Recent applications of Kirkwood-Buff theory to biological systems. Cell Biochem. Biophys. 2008, 50, 1-22.
    • (2008) Cell Biochem. Biophys , vol.50 , pp. 1-22
    • Pierce, V.1    Kang, M.2    Aburi, M.3    Weerasinghe, S.4
  • 65
    • 33749470157 scopus 로고    scopus 로고
    • Second virial coefficient determination of a therapeutic peptide by self-interaction chromatography
    • Payne, R.W., Nayar, R.,Tarantino, R., Del Terzo, S. et al., Second virial coefficient determination of a therapeutic peptide by self-interaction chromatography. Biopolymers 2006, 84, 527-533.
    • (2006) Biopolymers , vol.84 , pp. 527-533
    • Payne, R.W.1    Nayar, R.2    Tarantino, R.3    Del Terzo, S.4
  • 66
    • 0036194842 scopus 로고    scopus 로고
    • Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography
    • Tessier, P. M., Lenhoff, A. M., Sandler, S. I., Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography. Biophys. J. 2002, 82, 1620-1631.
    • (2002) Biophys. J , vol.82 , pp. 1620-1631
    • Tessier, P.M.1    Lenhoff, A.M.2    Sandler, S.I.3
  • 67
    • 0001578536 scopus 로고
    • Thermodynamic properties of aqueous alpha-chymotrypsin solutions from membrane osmometry measurements
    • Haynes, C. A.,Tamura, K., Korfer, H. R., Blanch, H.W. et al., Thermodynamic properties of aqueous alpha-chymotrypsin solutions from membrane osmometry measurements. J. Phys. Chem. 1992, 96, 905-912.
    • (1992) J. Phys. Chem , vol.96 , pp. 905-912
    • Haynes, C.A.1    Tamura, K.2    Korfer, H.R.3    Blanch, H.W.4
  • 68
    • 0030566049 scopus 로고    scopus 로고
    • Nucleation and crystallization of globular proteins - What we know and what is missing
    • Rosenberger, F., Vekilov, P. G., Muschol, M., Thomas, B. R., Nucleation and crystallization of globular proteins - What we know and what is missing. J. Crys.Growth 1996, 168, 1-27.
    • (1996) J. Crys.Growth , vol.168 , pp. 1-27
    • Rosenberger, F.1    Vekilov, P.G.2    Muschol, M.3    Thomas, B.R.4
  • 69
    • 0030262786 scopus 로고    scopus 로고
    • Lack of evidence for prenucleation aggregate formation in lysozyme crystal growth solutions
    • Muschol, M., Rosenberger, F., Lack of evidence for prenucleation aggregate formation in lysozyme crystal growth solutions. J. Crys. Growth 1996, 167, 738-747.
    • (1996) J. Crys. Growth , vol.167 , pp. 738-747
    • Muschol, M.1    Rosenberger, F.2
  • 70
    • 0031559476 scopus 로고    scopus 로고
    • Liquid-liquid phase separation in supersaturated lysozyme solutions and associated precipitate formation/ crystallization
    • Muschol, M., Rosenberger, F., Liquid-liquid phase separation in supersaturated lysozyme solutions and associated precipitate formation/ crystallization. J. Chem. Phys. 1997, 107, 1953-1962.
    • (1997) J. Chem. Phys , vol.107 , pp. 1953-1962
    • Muschol, M.1    Rosenberger, F.2
  • 71
    • 0029540627 scopus 로고
    • Interactions in undersaturated and supersaturated lysozyme solutions: Static and dynamic light scattering results
    • Muschol, M., Rosenberger, F., Interactions in undersaturated and supersaturated lysozyme solutions: static and dynamic light scattering results. J. Chem. Phys. 1995, 103, 10424-10432.
    • (1995) J. Chem. Phys , vol.103 , pp. 10424-10432
    • Muschol, M.1    Rosenberger, F.2
  • 72
    • 0042440398 scopus 로고    scopus 로고
    • Protein interactions and phase behavior: Sensitivity to the form of the pair potential
    • Rosenbaum, D. F., Kulkarni, A., Ramakrishnan, S., Zukoski, C. F., Protein interactions and phase behavior: Sensitivity to the form of the pair potential. J. Chem. Phys. 1999, 111, 9882-9890.
    • (1999) J. Chem. Phys , vol.111 , pp. 9882-9890
    • Rosenbaum, D.F.1    Kulkarni, A.2    Ramakrishnan, S.3    Zukoski, C.F.4
  • 73
    • 0034201441 scopus 로고    scopus 로고
    • the European Molecular Biology Open Software Suite
    • EMBOSS
    • Rice, P., Longden, I., Bleasby, A., EMBOSS: the European Molecular Biology Open Software Suite. Trends Genet. 2000, 16, 276-277.
    • (2000) Trends Genet , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 74
    • 36649033018 scopus 로고    scopus 로고
    • Conformational analysis of protein secondary structure during spray-drying of antibody/mannitol formulations
    • Schüle, S., Friess,W., Bechtold-Peters, K., Garidel, P., Conformational analysis of protein secondary structure during spray-drying of antibody/mannitol formulations. Eur. J. Pharm. Biopharm. 2007, 65, 1-9.
    • (2007) Eur. J. Pharm. Biopharm , vol.65 , pp. 1-9
    • Schüle, S.1    Friess, W.2    Bechtold-Peters, K.3    Garidel, P.4
  • 75
    • 0002737621 scopus 로고
    • Isolation of lysozyme from egg white
    • Alderton, G., Ward, W. H., Fevold, H. L., Isolation of lysozyme from egg white. J. Biol. Chem. 1945, 157, 43-58.
    • (1945) J. Biol. Chem , vol.157 , pp. 43-58
    • Alderton, G.1    Ward, W.H.2    Fevold, H.L.3
  • 76
    • 18744405982 scopus 로고
    • Immunological studies on egg white proteins.4. Immunochemical and physical studies of lysozyme
    • Wetter, L. R., Deutsch, H. F., Immunological studies on egg white proteins.4. Immunochemical and physical studies of lysozyme. J. Biol. Chem. 1951, 192, 237-242.
    • (1951) J. Biol. Chem , vol.192 , pp. 237-242
    • Wetter, L.R.1    Deutsch, H.F.2
  • 77
    • 15244340397 scopus 로고    scopus 로고
    • Modulation of lysozyme charge influences interaction with phospholipid vesicles
    • Zschornig, O., Paasche, G.,Thieme, C., Korb, N. et al., Modulation of lysozyme charge influences interaction with phospholipid vesicles. Colloids Surf. B Biointerfaces 2005, 42, 69-78.
    • (2005) Colloids Surf. B Biointerfaces , vol.42 , pp. 69-78
    • Zschornig, O.1    Paasche, G.2    Thieme, C.3    Korb, N.4
  • 78
    • 0342813099 scopus 로고    scopus 로고
    • No salting-in of lysozyme chloride observed at how ionic strength over a large range of pH
    • Retailleau, P., RiesKautt, M., Ducruix, A., No salting-in of lysozyme chloride observed at how ionic strength over a large range of pH. Biophys. J. 1997, 73, 2156-2163.
    • (1997) Biophys. J , vol.73 , pp. 2156-2163
    • Retailleau, P.1    RiesKautt, M.2    Ducruix, A.3
  • 79
    • 0036793453 scopus 로고    scopus 로고
    • Importance of the nature of anions in lysozyme crystallisation correlated with protein net charge variation
    • Retailleau, P., Ducruix,A., Ries-Kautt, M., Importance of the nature of anions in lysozyme crystallisation correlated with protein net charge variation. Acta Crystallograph. D Biol. Crystallogr. 2002, 58, 1576-1581.
    • (2002) Acta Crystallograph. D Biol. Crystallogr , vol.58 , pp. 1576-1581
    • Retailleau, P.1    Ducruix, A.2    Ries-Kautt, M.3
  • 80
    • 2942748360 scopus 로고    scopus 로고
    • Measurement of lysozyme-lysozyme interactions with quantitative affinity chromatography
    • Teske, C. A., Blanch, H.W., Prausnitz, J. M., Measurement of lysozyme-lysozyme interactions with quantitative affinity chromatography. J. Phys. Chem. B 2004, 108, 7437-7444.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 7437-7444
    • Teske, C.A.1    Blanch, H.W.2    Prausnitz, J.M.3
  • 81
    • 20344394673 scopus 로고    scopus 로고
    • Interactions of lysozyme in guanidinium chloride solutions from static and dynamic light-scattering measurements
    • Liu,W., Cellmer, T., Keerl, D., Prausnitz, J. M. et al., Interactions of lysozyme in guanidinium chloride solutions from static and dynamic light-scattering measurements. Biotechnol. Bioeng. 2005, 90, 482-490.
    • (2005) Biotechnol. Bioeng , vol.90 , pp. 482-490
    • Liu, W.1    Cellmer, T.2    Keerl, D.3    Prausnitz, J.M.4
  • 82
    • 17844405882 scopus 로고    scopus 로고
    • A consistent experimental and modeling approach to lightscattering studies of protein-protein interactions in solution
    • Asthagiri, D., Paliwal, A., Abras, D., Lenhoff, A. M. et al., A consistent experimental and modeling approach to lightscattering studies of protein-protein interactions in solution. Biophys. J. 2005, 88, 3300-3309.
    • (2005) Biophys. J , vol.88 , pp. 3300-3309
    • Asthagiri, D.1    Paliwal, A.2    Abras, D.3    Lenhoff, A.M.4
  • 83
    • 36549032551 scopus 로고    scopus 로고
    • Precipitants and additives for membrane crystallization of lysozyme
    • Zhang, X., El-Bourawi, M. S., Wei, K., Tao, F. et al., Precipitants and additives for membrane crystallization of lysozyme. Biotechnol. J. 2006, 1, 1302-1311.
    • (2006) Biotechnol. J , vol.1 , pp. 1302-1311
    • Zhang, X.1    El-Bourawi, M.S.2    Wei, K.3    Tao, F.4
  • 84
    • 49549102447 scopus 로고    scopus 로고
    • Salting-out of lysozyme and ovalbumin from mixtures: Predicting precipitation performance from protein-protein interactions
    • Cheng,Y. C., Bianco, C. L., Sandler, S. I., Lenhoff,A. M., Salting-out of lysozyme and ovalbumin from mixtures: Predicting precipitation performance from protein-protein interactions. Ind. Eng. Chem. Res. 2008, 47, 5203-5213.
    • (2008) Ind. Eng. Chem. Res , vol.47 , pp. 5203-5213
    • Cheng, Y.C.1    Bianco, C.L.2    Sandler, S.I.3    Lenhoff, A.M.4
  • 85
    • 40849083446 scopus 로고    scopus 로고
    • Effects of pH on protein-protein interactions and implications for protein phase behavior
    • Dumetz, A.C., Chockla, A. M., Kaler,E.W., Lenhoff,A. M., Effects of pH on protein-protein interactions and implications for protein phase behavior. Biochim. Biophys. Acta 2008, 1784, 600-610.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 600-610
    • Dumetz, A.C.1    Chockla, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 86
    • 38349042010 scopus 로고    scopus 로고
    • Protein phase behavior in aqueous solutions: Crystallization, liquid-liquid phase separation, gels, and aggregates
    • Dumetz, A. C., Chockla, A. M., Kaler, E.W., Lenhoff, A. M., Protein phase behavior in aqueous solutions: crystallization, liquid-liquid phase separation, gels, and aggregates. Biophys. J. 2008, 94, 570-583.
    • (2008) Biophys. J , vol.94 , pp. 570-583
    • Dumetz, A.C.1    Chockla, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 87
    • 34548427923 scopus 로고    scopus 로고
    • Patterns of protein protein interactions in salt solutions and implications for protein crystallization
    • Dumetz, A. C., Snellinger-O'brien, A. M., Kaler, E. W., Lenhoff, A. M., Patterns of protein protein interactions in salt solutions and implications for protein crystallization. Protein Sci. 2007, 16, 1867-1877.
    • (2007) Protein Sci , vol.16 , pp. 1867-1877
    • Dumetz, A.C.1    Snellinger-O'brien, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 88
    • 0033043375 scopus 로고    scopus 로고
    • Effect of sucrose on the thermodynamic properties of ovalbumin and sodium caseinate in bulk solution and at air-water interface
    • Antipova, A. S., Semenova, M. G., Belyakova, L. E., Effect of sucrose on the thermodynamic properties of ovalbumin and sodium caseinate in bulk solution and at air-water interface. Colloids Surf. B Biointerfaces 1999, 12, 261-270.
    • (1999) Colloids Surf. B Biointerfaces , vol.12 , pp. 261-270
    • Antipova, A.S.1    Semenova, M.G.2    Belyakova, L.E.3
  • 89
    • 0022322069 scopus 로고
    • Theory of protein solubility
    • Arakawa, T., Timasheff, S. N., Theory of protein solubility. Meth. Enzymol. 1985, 114, 49-77.
    • (1985) Meth. Enzymol , vol.114 , pp. 49-77
    • Arakawa, T.1    Timasheff, S.N.2
  • 90
    • 0035819206 scopus 로고    scopus 로고
    • Monte Carlo simulations of lysozyme self-association in aqueous solution
    • Carlsson, F., Malmsten, M., Linse, P., Monte Carlo simulations of lysozyme self-association in aqueous solution. J. Phys. Chem. B 2001, 105, 12189-12195.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 12189-12195
    • Carlsson, F.1    Malmsten, M.2    Linse, P.3
  • 91
    • 0020196284 scopus 로고
    • A biophysical model of lysozyme self-association
    • Hampe, O. G., Tondo, C.V., A biophysical model of lysozyme self-association. Biophys. J. 1982, 39, 77-82.
    • (1982) Biophys. J , vol.39 , pp. 77-82
    • Hampe, O.G.1    Tondo, C.V.2
  • 92
    • 39649086703 scopus 로고    scopus 로고
    • similarities and differences compared with lysozyme monimer association
    • Lysozyme dimer association
    • Onuma, K., Inaka, K., Lysozyme dimer association: similarities and differences compared with lysozyme monimer association. J. Crystal Growth 2008, 310, 1174-1181.
    • (2008) J. Crystal Growth , vol.310 , pp. 1174-1181
    • Onuma, K.1    Inaka, K.2
  • 93
    • 58349084293 scopus 로고    scopus 로고
    • Self-interaction of native and denatured lysozyme in the presence of osmolytes, l-arginine and guanidine hydrochloride
    • Dong, X. Y., Liu, J. H., Liu, F. F., Sun, Y., Self-interaction of native and denatured lysozyme in the presence of osmolytes, l-arginine and guanidine hydrochloride. Biochem. Eng. J. 2009, 43, 321-326.
    • (2009) Biochem. Eng. J , vol.43 , pp. 321-326
    • Dong, X.Y.1    Liu, J.H.2    Liu, F.F.3    Sun, Y.4
  • 94
    • 34247513828 scopus 로고
    • Zur Lehre von der Wirkung der Salze.
    • Hofmeister, F., Zur Lehre von der Wirkung der Salze. Arch. Exp. Pathol. Pharmakol. 1888, 24, 247-260.
    • (1888) Arch. Exp. Pathol. Pharmakol , vol.24 , pp. 247-260
    • Hofmeister, F.1
  • 95
    • 0037143801 scopus 로고    scopus 로고
    • Protein-protein interactions in concentrated electrolyte solutions
    • Curtis, R. A., Ulrich, J., Montaser, A., Prausnitz, J. M. et al., Protein-protein interactions in concentrated electrolyte solutions. Biotechnol. Bioeng. 2002, 79, 367-380.
    • (2002) Biotechnol. Bioeng , vol.79 , pp. 367-380
    • Curtis, R.A.1    Ulrich, J.2    Montaser, A.3    Prausnitz, J.M.4
  • 96
    • 0000774910 scopus 로고
    • Enzymstudien. II: Mitteilung. Über die Messung und die Bedeutung der Wasserstoffionenkonzentration bei enzymatischen Prozessen.
    • Sorensen, S. P. L., Enzymstudien. II: Mitteilung. Über die Messung und die Bedeutung der Wasserstoffionenkonzentration bei enzymatischen Prozessen. Biochem. Z. 1909, 21, 131-304.
    • (1909) Biochem. Z , vol.21 , pp. 131-304
    • Sorensen, S.P.L.1
  • 97
    • 0030727624 scopus 로고    scopus 로고
    • The Hofmeister series: Salt and solvent effects on interfacial phenomena
    • Cacace, M. G., Landau, E. M., Ramsden, J. J.,The Hofmeister series: salt and solvent effects on interfacial phenomena. Q. Rev. Biophys. 1997, 30, 241-277.
    • (1997) Q. Rev. Biophys , vol.30 , pp. 241-277
    • Cacace, M.G.1    Landau, E.M.2    Ramsden, J.J.3
  • 98
    • 1542295067 scopus 로고    scopus 로고
    • Thermal stability of proteins in aqueous polyol solutions: Role of the surface tension of water in the stabilizing effect of polyols
    • Kaushik, J. K., Bhat, R., Thermal stability of proteins in aqueous polyol solutions: Role of the surface tension of water in the stabilizing effect of polyols. J. Phys. Chem. B. 1998, 102, 7058-7066.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 7058-7066
    • Kaushik, J.K.1    Bhat, R.2
  • 99
    • 33748290394 scopus 로고    scopus 로고
    • Screening for physical stability of a Pseudomonas amylase using self-interaction chromatography
    • Valente, J. J., Fryksdale, B. G., Dale, A. D., Gaertner, A. L. et al., Screening for physical stability of a Pseudomonas amylase using self-interaction chromatography. Anal. Biochem. 2006, 357, 35-42.
    • (2006) Anal. Biochem , vol.357 , pp. 35-42
    • Valente, J.J.1    Fryksdale, B.G.2    Dale, A.D.3    Gaertner, A.L.4
  • 100
    • 24144467366 scopus 로고    scopus 로고
    • Light-scattering studies of protein solutions: Role of hydration in weak protein-protein interactions
    • Paliwal, A., Asthagiri, D., Abras, D., Lenhoff, A. M. et al., Light-scattering studies of protein solutions: Role of hydration in weak protein-protein interactions. Biophys. J. 2005, 89, 1564-1576.
    • (2005) Biophys. J , vol.89 , pp. 1564-1576
    • Paliwal, A.1    Asthagiri, D.2    Abras, D.3    Lenhoff, A.M.4
  • 101
    • 0026409134 scopus 로고
    • Differential scanning calorimetric studies on bovine serum albumin: II. Effects of neutral salts and urea
    • Yamasaki, M., Yano, H., Aoki, K., Differential scanning calorimetric studies on bovine serum albumin: II. Effects of neutral salts and urea. Int. J. Biol. Macromol. 1991, 13, 322-328.
    • (1991) Int. J. Biol. Macromol , vol.13 , pp. 322-328
    • Yamasaki, M.1    Yano, H.2    Aoki, K.3
  • 102
    • 0024969402 scopus 로고
    • Relative effectiveness of various ions on the solubility and crystal-growth of lysozyme
    • Rieskautt, M. M., Ducruix, A.F., Relative effectiveness of various ions on the solubility and crystal-growth of lysozyme. J. Biol. Chem. 1989, 264, 745-748.
    • (1989) J. Biol. Chem , vol.264 , pp. 745-748
    • Rieskautt, M.M.1    Ducruix, A.F.2
  • 103
    • 58549106756 scopus 로고    scopus 로고
    • High-throughput self-interaction chromatography: Applicationd in protein formulation prediction
    • Johnson, D. H., Parupudi, A.,Wilson,W.W., DeLucas, L. J., High-throughput self-interaction chromatography: Applicationd in protein formulation prediction. Pharm. Res. 2009, 26, 296-305.
    • (2009) Pharm. Res , vol.26 , pp. 296-305
    • Johnson, D.H.1    Parupudi, A.2    Wilson, W.W.3    DeLucas, L.J.4
  • 105
    • 0041931122 scopus 로고    scopus 로고
    • Macromolecular crowding: Qualitative and semiquantitative successes, quantitative challenges
    • Hall, D., Minton, A. P., Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges. Biochim. Biophys. Acta 2003, 1649, 127-139.
    • (2003) Biochim. Biophys. Acta , vol.1649 , pp. 127-139
    • Hall, D.1    Minton, A.P.2
  • 106
    • 0242515822 scopus 로고    scopus 로고
    • Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor
    • Chi, E. Y., Krishnan, S., Kendrick, B. S., Chang, B. S. et al., Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Protein Sci. 2003, 12, 903-913.
    • (2003) Protein Sci , vol.12 , pp. 903-913
    • Chi, E.Y.1    Krishnan, S.2    Kendrick, B.S.3    Chang, B.S.4


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