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Volumn 99, Issue 8, 2010, Pages 2657-2665

Diffusion and sedimentation interaction parameters for measuring the second virial coefficient and their utility as predictors of protein aggregation

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EID: 78049344329     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.08.020     Document Type: Article
Times cited : (142)

References (52)
  • 1
    • 0033513738 scopus 로고    scopus 로고
    • Why is the osmotic second virial coefficient related to protein crystallization?
    • Neal, B. L., D. Asthagiri, ⋯, E. W. Kaler. 1999. Why is the osmotic second virial coefficient related to protein crystallization? J. Cryst. Growth. 196:377-387.
    • (1999) J. Cryst. Growth. , vol.196 , pp. 377-387
    • Neal, B.L.1    Asthagiri, D.2    Kaler, E.W.3
  • 2
    • 0001279457 scopus 로고
    • Predicting protein crystallization from a dilute solution property
    • George, A., and W. W. Wilson. 1994. Predicting protein crystallization from a dilute solution property. Acta Crystallogr. D Biol. Crystallogr. 50:361-365.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 361-365
    • George, A.1    Wilson, W.W.2
  • 3
    • 76849089849 scopus 로고    scopus 로고
    • Chemical modification of lysine residues in lysozyme may dramatically influence its amyloid fibrillation
    • Morshedi, D., A. Ebrahim-Habibi, ⋯, M. Nemat-Gorgani. 2010. Chemical modification of lysine residues in lysozyme may dramatically influence its amyloid fibrillation. Biochim. Biophys. Acta. 1804:714-722.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 714-722
    • Morshedi, D.1    Ebrahim-Habibi, A.2    Nemat-Gorgani, M.3
  • 4
    • 70049090962 scopus 로고    scopus 로고
    • Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases
    • Castillo, V., and S. Ventura. 2009. Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases. PLOS Comput. Biol. 5:e1000476.
    • (2009) PLOS Comput. Biol. , vol.5
    • Castillo, V.1    Ventura, S.2
  • 5
    • 40949125214 scopus 로고    scopus 로고
    • Visualizing interaction of proteins relevant to Alzheimer's disease in intact cells
    • Thomas, A. V., O. Berezovska,., C. A. von Arnim. 2008. Visualizing interaction of proteins relevant to Alzheimer's disease in intact cells. Methods. 44:299-303.
    • (2008) Methods , vol.44 , pp. 299-303
    • Thomas, A.V.1    Berezovska, O.2    Von Arnim, C.A.3
  • 6
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper, J. D., and P. T. Lansbury, Jr. 1997. Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66:385-407.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 7
    • 0942276377 scopus 로고    scopus 로고
    • Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation
    • Meehan, S., Y. Berry, ⋯, C. E. MacPhee. 2004. Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation. J. Biol. Chem. 279:3413-3419.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3413-3419
    • Meehan, S.1    Berry, Y.2    MacPhee, C.E.3
  • 8
    • 0142122294 scopus 로고    scopus 로고
    • Measurements of protein selfassociation as a guide to crystallization
    • Tessier, P. M., and A. M. Lenhoff. 2003. Measurements of protein selfassociation as a guide to crystallization. Curr. Opin. Biotechnol. 14:512-516.
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 512-516
    • Tessier, P.M.1    Lenhoff, A.M.2
  • 9
    • 77951652786 scopus 로고    scopus 로고
    • A critical evaluation of self-interaction chromatography as a predictive tool for the assessment of protein-protein interactions in protein formulation development: A case study of a therapeutic monoclonal antibody
    • Le Brun, V., W. Friess, ⋯, P. Garidel. 2010. A critical evaluation of self-interaction chromatography as a predictive tool for the assessment of protein-protein interactions in protein formulation development: A case study of a therapeutic monoclonal antibody. Eur. J. Pharm. Biopharm. 75:16-25.
    • (2010) Eur. J. Pharm. Biopharm. , vol.75 , pp. 16-25
    • Le Brun, V.1    Friess, W.2    Garidel, P.3
  • 10
    • 70350123028 scopus 로고    scopus 로고
    • Lysozyme-lysozyme selfinteractions as assessed by the osmotic second virial coefficient: Impact for physical protein stabilization
    • Le Brun, V., W. Friess, ⋯, P. Garidel. 2009. Lysozyme-lysozyme selfinteractions as assessed by the osmotic second virial coefficient: Impact for physical protein stabilization. Biotechnol. J. 4:1305-1319.
    • (2009) Biotechnol. J. , vol.4 , pp. 1305-1319
    • Le Brun, V.1    Friess, W.2    Garidel, P.3
  • 11
    • 34447303560 scopus 로고    scopus 로고
    • Phase behavior of an intact monoclonal antibody
    • Ahamed, T., B. N. Esteban, ⋯, J. Thömmes. 2007. Phase behavior of an intact monoclonal antibody. Biophys. J. 93:610-619.
    • (2007) Biophys. J. , vol.93 , pp. 610-619
    • Ahamed, T.1    Esteban, B.N.2    Thömmes, J.3
  • 12
    • 1942489413 scopus 로고    scopus 로고
    • Correlation of diafiltration sieving behavior of lysozyme-BSA mixtures with osmotic second virial cross-coefficients
    • Tessier, P. M., V. J. Verruto, ⋯, A. M. Lenhoff. 2004. Correlation of diafiltration sieving behavior of lysozyme-BSA mixtures with osmotic second virial cross-coefficients. Biotechnol. Bioeng. 87:303-310.
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 303-310
    • Tessier, P.M.1    Verruto, V.J.2    Lenhoff, A.M.3
  • 13
    • 0037215795 scopus 로고    scopus 로고
    • Protein interactions in undersaturated and supersaturated solutions: A study using light and x-ray scattering
    • Narayanan, J., and X. Y. Liu. 2003. Protein interactions in undersaturated and supersaturated solutions: A study using light and x-ray scattering. Biophys. J. 84:523-532.
    • (2003) Biophys. J. , vol.84 , pp. 523-532
    • Narayanan, J.1    Liu, X.Y.2
  • 14
    • 0032502957 scopus 로고    scopus 로고
    • Repulsive interparticle interactions in a denatured protein solution revealed by small angle neutron scattering
    • Receveur, V., D. Durand, ⋯, P. Calmettes. 1998. Repulsive interparticle interactions in a denatured protein solution revealed by small angle neutron scattering. FEBS Lett. 426:57-61.
    • (1998) FEBS Lett. , vol.426 , pp. 57-61
    • Receveur, V.1    Durand, D.2    Calmettes, P.3
  • 15
    • 1642285049 scopus 로고    scopus 로고
    • Sedimentation equilibrium in a solution containing an arbitrary number of solute species at arbitrary concentrations: Theory and application to concentrated solutions of ribonuclease
    • Zorrilla, S., M. Jiménez, ⋯, A. P. Minton. 2004. Sedimentation equilibrium in a solution containing an arbitrary number of solute species at arbitrary concentrations: Theory and application to concentrated solutions of ribonuclease. Biophys. Chem. 108:89-100.
    • (2004) Biophys. Chem. , vol.108 , pp. 89-100
    • Zorrilla, S.1    Jiménez, M.2    Minton, A.P.3
  • 16
    • 78049338888 scopus 로고    scopus 로고
    • Reduced-viscosity concentrated protein formulations
    • J. Liu, and S. J. Shire. 2002. Reduced-viscosity concentrated protein formulations. Pat. No.WO-0230463.
    • (2002) Pat. No. WO-0230463
    • Liu, J.1    Shire, S.J.2
  • 17
    • 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., T. Arakawa, and J. S. Philo. 1996. Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal. Biochem. 240:155-166.
    • (1996) Anal. Biochem. , vol.240 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 18
    • 0141754043 scopus 로고    scopus 로고
    • Measurements of protein-protein interactions by size exclusion chromatography
    • Bloustine, J., V. Berejnov, and S. Fraden. 2003. Measurements of protein-protein interactions by size exclusion chromatography. Biophys. J. 85:2619-2623.
    • (2003) Biophys. J. , vol.85 , pp. 2619-2623
    • Bloustine, J.1    Berejnov, V.2    Fraden, S.3
  • 20
    • 0036794725 scopus 로고    scopus 로고
    • Self-interaction chromatography: A novel screening method for rational protein crystallization
    • Tessier, P. M., S. D. Vandrey,., A. M. Lenhoff. 2002. Self-interaction chromatography: A novel screening method for rational protein crystallization. Acta Crystallogr. D Biol. Crystallogr. 58:1531-1535.
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , pp. 1531-1535
    • Tessier, P.M.1    Vandrey, S.D.2    Lenhoff, A.M.3
  • 21
    • 74549226587 scopus 로고    scopus 로고
    • Self-interaction chromatography as a tool for optimizing conditions for membrane protein crystallization
    • Gabrielsen, M., L. A. Nagy, ⋯, R. J. Cogdell. 2010. Self-interaction chromatography as a tool for optimizing conditions for membrane protein crystallization. Acta Crystallogr. D Biol. Crystallogr. 66:44-50.
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 44-50
    • Gabrielsen, M.1    Nagy, L.A.2    Cogdell, R.J.3
  • 22
    • 0022351381 scopus 로고
    • The concentration-dependence of macromolecular parameters
    • Harding, S. E., and P. Johnson. 1985. The concentration-dependence of macromolecular parameters. Biochem. J. 231:543-547.
    • (1985) Biochem. J. , vol.231 , pp. 543-547
    • Harding, S.E.1    Johnson, P.2
  • 23
    • 35648978159 scopus 로고    scopus 로고
    • Dynamic light scattering as a relative tool for assessing the molecular integrity and stability of monoclonal antibodies
    • Nobbmann, U., M. Connah, ⋯, S. E. Harding. 2007. Dynamic light scattering as a relative tool for assessing the molecular integrity and stability of monoclonal antibodies. Biotechnol. Genet. Eng. Rev. 24:117-128.
    • (2007) Biotechnol. Genet. Eng. Rev. , vol.24 , pp. 117-128
    • Nobbmann, U.1    Connah, M.2    Harding, S.E.3
  • 24
    • 62349127428 scopus 로고    scopus 로고
    • Microparticle sizing by dynamic light scattering in fresh-frozen plasma
    • Lawrie, A. S., A. Albanyan,., P. Harrison. 2009. Microparticle sizing by dynamic light scattering in fresh-frozen plasma. Vox Sang. 96: 206-212.
    • (2009) Vox Sang. , vol.96 , pp. 206-212
    • Lawrie, A.S.1    Albanyan, A.2    Harrison, P.3
  • 25
    • 1842422174 scopus 로고    scopus 로고
    • Gradient diffusion and protein solubility: Use of dynamic light scattering to localize crystallization conditions
    • Mirarefi, A. Y., and C. F. Zukoski. 2004. Gradient diffusion and protein solubility: Use of dynamic light scattering to localize crystallization conditions. J. Cryst. Growth. 265:274-283.
    • (2004) J. Cryst. Growth. , vol.265 , pp. 274-283
    • Mirarefi, A.Y.1    Zukoski, C.F.2
  • 26
    • 33745216899 scopus 로고    scopus 로고
    • Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques
    • Philo, J. S. 2006. Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques. Anal. Biochem. 354:238-246.
    • (2006) Anal. Biochem. , vol.354 , pp. 238-246
    • Philo, J.S.1
  • 27
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. 2000. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78:1606-1619.
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 28
    • 0034654352 scopus 로고    scopus 로고
    • A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions
    • Philo, J. S. 2000. A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions. Anal. Biochem. 279:151-163.
    • (2000) Anal. Biochem. , vol.279 , pp. 151-163
    • Philo, J.S.1
  • 29
    • 0034816707 scopus 로고    scopus 로고
    • Non-ideality by sedimentation velocity of halophilic malate dehydrogenase in complex solvents
    • Solovyova, A., P. Schuck,., C. Ebel. 2001. Non-ideality by sedimentation velocity of halophilic malate dehydrogenase in complex solvents. Biophys. J. 81:1868-1880.
    • (2001) Biophys. J. , vol.81 , pp. 1868-1880
    • Solovyova, A.1    Schuck, P.2    Ebel, C.3
  • 30
    • 70349673739 scopus 로고    scopus 로고
    • Quaternary diffusion coefficients in a protein-polymer-salt-water system determined by Rayleigh interferometry
    • Annunziata, O., A. Vergara,., J. G. Albright. 2009. Quaternary diffusion coefficients in a protein-polymer-salt-water system determined by Rayleigh interferometry. J. Phys. Chem. B. 113:13446-13453.
    • (2009) J. Phys. Chem. B. , vol.113 , pp. 13446-13453
    • Annunziata, O.1    Vergara, A.2    Albright, J.G.3
  • 31
    • 0031029481 scopus 로고    scopus 로고
    • Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles
    • Behlke, J., and O. Ristau. 1997. Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles. Biophys. J. 72:428-434.
    • (1997) Biophys. J. , vol.72 , pp. 428-434
    • Behlke, J.1    Ristau, O.2
  • 32
    • 77950259335 scopus 로고    scopus 로고
    • Correlating aggregation kinetics and stationary diffusion in protein-sodium salt systems observed with dynamic light scattering
    • Rubin, J., A. San Miguel, ⋯, S. H. Behrens. 2010. Correlating aggregation kinetics and stationary diffusion in protein-sodium salt systems observed with dynamic light scattering. J. Phys. Chem. B. 114:4383-4387.
    • (2010) J. Phys. Chem. B. , vol.114 , pp. 4383-4387
    • Rubin, J.1    San Miguel, A.2    Behrens, S.H.3
  • 33
    • 0036194842 scopus 로고    scopus 로고
    • Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography
    • Tessier, P. M., A. M. Lenhoff, and S. I. Sandler. 2002. Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography. Biophys. J. 82:1620-1631.
    • (2002) Biophys. J. , vol.82 , pp. 1620-1631
    • Tessier, P.M.1    Lenhoff, A.M.2    Sandler, S.I.3
  • 34
    • 0030566439 scopus 로고    scopus 로고
    • Protein interaction and crystallization
    • Rosenbaum, D. F., and C. F. Zukoski. 1996. Protein interaction and crystallization. J. Cryst. Growth. 169:752-758.
    • (1996) J. Cryst. Growth. , vol.169 , pp. 752-758
    • Rosenbaum, D.F.1    Zukoski, C.F.2
  • 35
    • 34247644354 scopus 로고    scopus 로고
    • Nonequivalence of second virial coefficients from sedimentation equilibrium and static light scattering studies of protein solutions
    • Winzor, D. J., M. Deszczynski, ⋯, P. R. Wills. 2007. Nonequivalence of second virial coefficients from sedimentation equilibrium and static light scattering studies of protein solutions. Biophys. Chem. 128:46-55.
    • (2007) Biophys. Chem. , vol.128 , pp. 46-55
    • Winzor, D.J.1    Deszczynski, M.2    Wills, P.R.3
  • 36
    • 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., S. E. Harding, and D. J. Winzor. 2006. 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. 120:106-113.
    • (2006) Biophys. Chem. , vol.120 , pp. 106-113
    • Deszczynski, M.1    Harding, S.E.2    Winzor, D.J.3
  • 37
    • 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., R.W. Payne,., C. S. Henry. 2005. Colloidal behavior of proteins: Effects of the second virial coefficient on solubility, crystallization and aggregation of proteins in aqueous solution. Curr. Pharm. Biotechnol. 6:427-436.
    • (2005) Curr. Pharm. Biotechnol. , vol.6 , pp. 427-436
    • Valente, J.J.1    Payne, R.W.2    Henry, C.S.3
  • 38
    • 3242670796 scopus 로고    scopus 로고
    • Opalescent appearance of an IgG1 antibody at high concentrations and its relationship to noncovalent association
    • Sukumar, M., B. L. Doyle, ⋯, A. H. Pekar. 2004. Opalescent appearance of an IgG1 antibody at high concentrations and its relationship to noncovalent association. Pharm. Res. 21:1087-1093.
    • (2004) Pharm. Res. , vol.21 , pp. 1087-1093
    • Sukumar, M.1    Doyle, B.L.2    Pekar, A.H.3
  • 39
    • 0348207551 scopus 로고    scopus 로고
    • Effect of protein-protein interactions on protein aggregation kinetics
    • Zhang, J., and X. Y. Liu. 2003. Effect of protein-protein interactions on protein aggregation kinetics. J. Chem. Phys. 119:10972-10976.
    • (2003) J. Chem. Phys. , vol.119 , pp. 10972-10976
    • Zhang, J.1    Liu, X.Y.2
  • 40
    • 0031053090 scopus 로고    scopus 로고
    • Second virial coefficient as predictor in protein crystal growth
    • George, A., Y. Chiang, ⋯, W. W. Wilson. 1997. Second virial coefficient as predictor in protein crystal growth. Methods Enzymol. 276:100-110.
    • (1997) Methods Enzymol. , vol.276 , pp. 100-110
    • George, A.1    Chiang, Y.2    Wilson, W.W.3
  • 41
    • 34249706387 scopus 로고    scopus 로고
    • Ions in water: Characterizing the forces that control chemical processes and biological structure
    • Collins, K. D., G. W. Neilson, and J. E. Enderby. 2007. Ions in water: Characterizing the forces that control chemical processes and biological structure. Biophys. Chem. 128:95-104.
    • (2007) Biophys. Chem. , vol.128 , pp. 95-104
    • Collins, K.D.1    Neilson, G.W.2    Enderby, J.E.3
  • 42
    • 4344565219 scopus 로고    scopus 로고
    • Ions from the Hofmeister series and osmolytes: Effects on proteins in solution and in the crystallization process
    • Collins, K. D. 2004. Ions from the Hofmeister series and osmolytes: Effects on proteins in solution and in the crystallization process. Methods. 34:300-311.
    • (2004) Methods , vol.34 , pp. 300-311
    • Collins, K.D.1
  • 43
    • 0028999046 scopus 로고
    • Sticky ions in biological systems
    • Collins, K. D. 1995. Sticky ions in biological systems. Proc. Natl. Acad. Sci. USA. 92:5553-5557.
    • (1995) Proc. Natl. Acad. Sci. USA. , vol.92 , pp. 5553-5557
    • Collins, K.D.1
  • 44
    • 61449121954 scopus 로고    scopus 로고
    • Effect of ions on agitation- and temperature-induced aggregation reactions of antibodies
    • Fesinmeyer, R. M., S. Hogan,., Y. R. Gokarn. 2009. Effect of ions on agitation- and temperature-induced aggregation reactions of antibodies. Pharm. Res. 26:903-913.
    • (2009) Pharm. Res. , vol.26 , pp. 903-913
    • Fesinmeyer, R.M.1    Hogan, S.2    Gokarn, Y.R.3
  • 45
    • 57749184562 scopus 로고    scopus 로고
    • Anion binding mediated precipitation of a peptibody
    • Saluja, A., S. Crampton, ⋯, Y. R. Gokarn. 2009. Anion binding mediated precipitation of a peptibody. Pharm. Res. 26:152-160.
    • (2009) Pharm. Res. , vol.26 , pp. 152-160
    • Saluja, A.1    Crampton, S.2    Gokarn, Y.R.3
  • 46
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An immunologic perspective
    • Rosenberg, A. S. 2006. Effects of protein aggregates: An immunologic perspective. AAPS J. 8:E501-E507. http://www.aaps.org.
    • (2006) AAPS J. , vol.8
    • Rosenberg, A.S.1
  • 47
    • 70449704158 scopus 로고    scopus 로고
    • Formulation and manufacturability of biologics
    • Shire, S. J. 2009. Formulation and manufacturability of biologics. Curr. Opin. Biotechnol. 20:708-714.
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 708-714
    • Shire, S.J.1
  • 48
    • 0036462040 scopus 로고    scopus 로고
    • Transient clustering in protein solutions
    • Piazza, R., and S. Iacopini. 2002. Transient clustering in protein solutions. Eur. Phys. J. E. 7:45-48.
    • (2002) Eur. Phys. J. E. , vol.7 , pp. 45-48
    • Piazza, R.1    S., Iacopini.2
  • 49
    • 0037150072 scopus 로고    scopus 로고
    • Aggregation of granulocyte colony stimulating factor under physiological conditions: Characterization and thermodynamic inhibition
    • Krishnan, S., E. Y. Chi,., J. F. Carpenter. 2002. Aggregation of granulocyte colony stimulating factor under physiological conditions: Characterization and thermodynamic inhibition. Biochemistry. 41: 6422-6431.
    • (2002) Biochemistry , vol.41 , pp. 6422-6431
    • Krishnan, S.1    Chi, E.Y.2    Carpenter, J.F.3
  • 50
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi, E. Y., S. Krishnan, ⋯, J. F. Carpenter. 2003. Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation. Pharm. Res. 20:1325-1336.
    • (2003) Pharm. Res. , vol.20 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Carpenter, J.F.3
  • 51
    • 0037378389 scopus 로고    scopus 로고
    • The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient
    • Ho, J. G. S., A. P. J. Middelberg,., H. P. Kocher. 2003. The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient. Protein Sci. 12:708-716.
    • (2003) Protein Sci. , vol.12 , pp. 708-716
    • Ho, J.G.S.1    Middelberg, A.P.J.2    Kocher, H.P.3
  • 52
    • 0033513785 scopus 로고    scopus 로고
    • Second virial coefficient: Variations with lysozyme crystallization conditions
    • Bonnete, F., S. Finet, and A. Tardieu. 1999. Second virial coefficient: Variations with lysozyme crystallization conditions. J. Cryst. Growth. 196:403-414.
    • (1999) J. Cryst. Growth. , vol.196 , pp. 403-414
    • Bonnete, F.1    Finet, S.2    Tardieu, A.3


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