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Volumn 99, Issue 2, 2010, Pages 645-662

Multi-variate approach to global protein aggregation behavior and kinetics: Effects of pH, NaCl, and temperature for α-chymotrypsinogen A

Author keywords

Protein aggregation; Protein formulation; Stability

Indexed keywords

CHYMOTRYPSINOGEN; PROTEIN; SODIUM CHLORIDE;

EID: 74049123780     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.21869     Document Type: Article
Times cited : (89)

References (69)
  • 1
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink AL. 1998. Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Fold Des 3:R9-R23.
    • (1998) Fold Des , vol.3
    • Fink, A.L.1
  • 2
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • Uversky VN, Fink AL. 2004. Conformational constraints for amyloid fibrillation: The importance of being unfolded. Biochim Biophys Acta Proteins Proteomics 1698:131-153.
    • (2004) Biochim Biophys Acta Proteins Proteomics , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 3
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi EY, Krishnan S, Randolph TW, Carpenter JF. 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    Randolph, T.W.3    Carpenter, J.F.4
  • 4
    • 67449132077 scopus 로고    scopus 로고
    • Principles, approaches, and challenges for predicting protein aggregation rates and shelf life
    • Weiss WF IV, Young TM, Roberts CJ. 2009. Principles, approaches, and challenges for predicting protein aggregation rates and shelf life. J Pharm Sci 98:1246-1277.
    • (2009) J Pharm Sci , vol.98 , pp. 1246-1277
    • Weiss1    WF, I.V.2    Young, T.M.3    Roberts, C.J.4
  • 5
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang W. 2005. Protein aggregation and its inhibition in biopharmaceutics. Int J Pharm 289:1-30.
    • (2005) Int J Pharm , vol.289 , pp. 1-30
    • Wang, W.1
  • 7
    • 0027729733 scopus 로고
    • The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation
    • Cleland JL, Powell MF, Shire SJ. 1993. The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation. Crit Rev Ther Drug Carrier Syst 10:307-377.
    • (1993) Crit Rev Ther Drug Carrier Syst , vol.10 , pp. 307-377
    • Cleland, J.L.1    Powell, M.F.2    Shire, S.J.3
  • 8
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • Dobson CM. 2004. Principles of protein folding, misfolding and aggregation. Sem Cell Dev Biol 15:3-16.
    • (2004) Sem Cell Dev Biol , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 9
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • Roberts CJ. 2007. Non-native protein aggregation kinetics. Biotechnol Bioeng 98:927-938.
    • (2007) Biotechnol Bioeng , vol.98 , pp. 927-938
    • Roberts, C.J.1
  • 10
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An immunologic perspective
    • Rosenberg AS. 2006. Effects of protein aggregates: An immunologic perspective. AAPS J 8:E501-E507.
    • (2006) AAPS , vol.J 8
    • Rosenberg, A.S.1
  • 11
    • 32644434554 scopus 로고    scopus 로고
    • Influence of aggregation on immunogenicity of recombinant human factor VIII in hemophilia A mice
    • Purohit VS, Middaugh CR, Balasubramanian SV. 2006. Influence of aggregation on immunogenicity of recombinant human factor VIII in hemophilia A mice. J Pharm Sci 95:358-371.
    • (2006) J Pharm Sci , vol.95 , pp. 358-371
    • Purohit, V.S.1    Middaugh, C.R.2    Balasubramanian, S.V.3
  • 12
    • 33646546740 scopus 로고    scopus 로고
    • Antibody response to aggregated human interferon alpha2b in wild-type and transgenic immune tolerant mice depends on type and level of aggregation
    • Hermeling S, Schellekens H, Maas C, Gebbink MF, Crommelin DJ, Jiskoot W. 2006. Antibody response to aggregated human interferon alpha2b in wild-type and transgenic immune tolerant mice depends on type and level of aggregation. J Pharm Sci 95:1084-1096.
    • (2006) J Pharm Sci , vol.95 , pp. 1084-1096
    • Hermeling, S.1    Schellekens, H.2    Maas, C.3    Gebbink, M.F.4    Crommelin, D.J.5    Jiskoot, W.6
  • 13
    • 37349050368 scopus 로고    scopus 로고
    • Nonnative protein polymers: Structure, morphology, and relation to nucleation and growth
    • WeissWF IV, Hodgdon TK, Kaler EW, Lenhoff AM, Roberts CJ. 2007. Nonnative protein polymers: Structure, morphology, and relation to nucleation and growth. Biophys J 93:4392-4403.
    • (2007) Biophys J , vol.93 , pp. 4392-4403
    • WeissWF, I.V.1    Hodgdon, T.K.2    Kaler, E.W.3    Lenhoff, A.M.4    Roberts, C.J.5
  • 14
  • 15
    • 84919835307 scopus 로고    scopus 로고
    • Protein folding, misfolding, stability, and aggregation: An overview
    • Murphy RM, Tsai AM, editors, 1st edition. New York: Springer. pp
    • Murphy RM, Tsai AM. 2006. Protein folding, misfolding, stability, and aggregation: An overview. In: Murphy RM, Tsai AM, editors. Misbehaving proteins: Protein misfolding, aggregation, and stability. 1st edition. New York: Springer. pp. 3-13.
    • (2006) Misbehaving proteins: Protein misfolding, aggregation, and stability , pp. 3-13
    • Murphy, R.M.1    Tsai, A.M.2
  • 16
    • 2342629440 scopus 로고    scopus 로고
    • Regulatory considerations in the development of protein pharmaceuticals
    • Beatrice MG. 2002. Regulatory considerations in the development of protein pharmaceuticals. Pharm Biotechnol 14:405-456.
    • (2002) Pharm Biotechnol , vol.14 , pp. 405-456
    • Beatrice, M.G.1
  • 17
    • 33748742268 scopus 로고    scopus 로고
    • Is any measurement method optimal for all aggregate sizes and types?
    • Philo JS. 2006. Is any measurement method optimal for all aggregate sizes and types? AAPS J 8:E564-E571.
    • (2006) AAPS , vol.J 8
    • Philo, J.S.1
  • 18
    • 70349646469 scopus 로고    scopus 로고
    • Characterization of high molecular-weight nonnative aggregates and aggregation kinetics by size exclusion chromatography with inline multi-angle laser light scattering
    • DOI: 10.1002/jps.21726
    • Li Y, Weiss WF IV, Roberts CJ. 2009. Characterization of high molecular-weight nonnative aggregates and aggregation kinetics by size exclusion chromatography with inline multi-angle laser light scattering. J Pharm Sci DOI: 10.1002/jps.21726.
    • (2009) J Pharm Sci
    • Li, Y.1    Weiss2    WF, I.V.3    Roberts, C.J.4
  • 19
    • 68949085124 scopus 로고    scopus 로고
    • Protein aggregation: Pathways, induction factors and analysis
    • DOI: 10.1002/jps.21566
    • Mahler HC, Friess W, Grauschopf U, Kiese S. 2008. Protein aggregation: Pathways, induction factors and analysis. J Pharm Sci DOI: 10.1002/jps.21566.
    • (2008) J Pharm Sci
    • Mahler, H.C.1    Friess, W.2    Grauschopf, U.3    Kiese, S.4
  • 20
    • 34250834054 scopus 로고    scopus 로고
    • A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding
    • Andrews JM, Roberts CJ. 2007. A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding. J Phys Chem B 111:7897-7913.
    • (2007) J Phys Chem B , vol.111 , pp. 7897-7913
    • Andrews, J.M.1    Roberts, C.J.2
  • 21
    • 67650072650 scopus 로고    scopus 로고
    • A Lumry-Eyring nucleated-polymerization (LENP) model of protein aggregation kinetics. 2. Competing growth via condensation-and chain-polymerization
    • Li Y, Roberts CJ. 2009. A Lumry-Eyring nucleated-polymerization (LENP) model of protein aggregation kinetics. 2. Competing growth via condensation-and chain-polymerization. J Phys Chem B 113:7020-7032.
    • (2009) J Phys Chem B , vol.113 , pp. 7020-7032
    • Li, Y.1    Roberts, C.J.2
  • 22
    • 24144438172 scopus 로고    scopus 로고
    • Structure and morphology of the Alzheimer's amyloid fibril
    • Stromer T, Serpell LC. 2005. Structure and morphology of the Alzheimer's amyloid fibril. Microsc Res Tech 67:210-217.
    • (2005) Microsc Res Tech , vol.67 , pp. 210-217
    • Stromer, T.1    Serpell, L.C.2
  • 23
    • 15444367176 scopus 로고    scopus 로고
    • Correlations among morphology, beta-sheet stability, and molecular structure in prion peptide aggregates
    • Petty SA, Adalsteinsson T, Decatur SM. 2005. Correlations among morphology, beta-sheet stability, and molecular structure in prion peptide aggregates. Biochemistry 44:4720-4726.
    • (2005) Biochemistry , vol.44 , pp. 4720-4726
    • Petty, S.A.1    Adalsteinsson, T.2    Decatur, S.M.3
  • 24
    • 33144466335 scopus 로고    scopus 로고
    • Population balance modeling of aggregation kinetics of recombinant human interleukin-1 receptor antagonist
    • Chi EY, Kendrick BS, Carpenter JF, Randolph TW. 2005. Population balance modeling of aggregation kinetics of recombinant human interleukin-1 receptor antagonist. J Pharm Sci 94:2735-2748.
    • (2005) J Pharm Sci , vol.94 , pp. 2735-2748
    • Chi, E.Y.1    Kendrick, B.S.2    Carpenter, J.F.3    Randolph, T.W.4
  • 25
    • 0037462946 scopus 로고    scopus 로고
    • Alternate aggregation pathways of the Alzheimer beta-amyloid peptide: A beta association kinetics at endosomal pH
    • Gorman PM, Yip CM, Fraser PE, Chakrabartty A. 2003. Alternate aggregation pathways of the Alzheimer beta-amyloid peptide: A beta association kinetics at endosomal pH. J Mol Biol 325:743-757.
    • (2003) J Mol Biol , vol.325 , pp. 743-757
    • Gorman, P.M.1    Yip, C.M.2    Fraser, P.E.3    Chakrabartty, A.4
  • 26
    • 0036407227 scopus 로고    scopus 로고
    • Peptide aggregation in neuro-degenerative disease
    • Murphy RM. 2002. Peptide aggregation in neuro-degenerative disease. Annu Rev Biomed Eng 4:155-174.
    • (2002) Annu Rev Biomed Eng , vol.4 , pp. 155-174
    • Murphy, R.M.1
  • 27
    • 59849109485 scopus 로고    scopus 로고
    • A universal pathway for amyloid nucleus and precursor formation for insulin
    • Nayak A, Sorci M, Krueger S, Belfort G. 2009. A universal pathway for amyloid nucleus and precursor formation for insulin. Proteins 74:556-565.
    • (2009) Proteins , vol.74 , pp. 556-565
    • Nayak, A.1    Sorci, M.2    Krueger, S.3    Belfort, G.4
  • 28
    • 0034599720 scopus 로고    scopus 로고
    • Mutational analysis of the propensity for amyloid formation by a globular protein
    • Chiti F, Taddei N, Bucciantini M, White P, Ramponi G, Dobson CM. 2000. Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J 19:1441-1449.
    • (2000) EMBO J , vol.19 , pp. 1441-1449
    • Chiti, F.1    Taddei, N.2    Bucciantini, M.3    White, P.4    Ramponi, G.5    Dobson, C.M.6
  • 29
    • 0001202494 scopus 로고
    • Amino-acid sequence of bovine chymotrypsinogen-A
    • Hartley BS. 1964. Amino-acid sequence of bovine chymotrypsinogen-A. Nature 201:1284-1287.
    • (1964) Nature , vol.201 , pp. 1284-1287
    • Hartley, B.S.1
  • 30
    • 34250870678 scopus 로고    scopus 로고
    • Non-native aggregation of alpha-chymotrypsinogen occurs through nucleation and growth with competing nucleus sizes and negative activation energies
    • Andrews JM, Roberts CJ. 2007. Non-native aggregation of alpha-chymotrypsinogen occurs through nucleation and growth with competing nucleus sizes and negative activation energies. Biochemistry 46:7558-7571.
    • (2007) Biochemistry , vol.46 , pp. 7558-7571
    • Andrews, J.M.1    Roberts, C.J.2
  • 31
    • 39749110693 scopus 로고    scopus 로고
    • Nucleation, growth, and activation energies for seeded and unseeded aggregation of alpha- chymotrypsinogen A
    • Andrews JM, Weiss WF, Roberts CJ. 2008. Nucleation, growth, and activation energies for seeded and unseeded aggregation of alpha- chymotrypsinogen A. Biochemistry 47:2397-2403.
    • (2008) Biochemistry , vol.47 , pp. 2397-2403
    • Andrews, J.M.1    Weiss, W.F.2    Roberts, C.J.3
  • 33
    • 0031768735 scopus 로고    scopus 로고
    • Protein interactions in solution characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen
    • Velev OD, Kaler EW, Lenhoff AM. 1998. Protein interactions in solution characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen. Biophys J 75:2682-2697.
    • (1998) Biophys J , vol.75 , pp. 2682-2697
    • Velev, O.D.1    Kaler, E.W.2    Lenhoff, A.M.3
  • 34
    • 0242515822 scopus 로고    scopus 로고
    • Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor
    • Chi EY, Krishnan S, Kendrick BS, Chang BS, Carpenter JF, Randolph TW. 2003. Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Protein Sci 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    Carpenter, J.F.5    Randolph, T.W.6
  • 35
    • 0037378389 scopus 로고    scopus 로고
    • The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient
    • Ho JG, Middelberg AP, Ramage P, Kocher HP. 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.1    Middelberg, A.P.2    Ramage, P.3    Kocher, H.P.4
  • 36
    • 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 VK, Badkar A, Zeng D, Nema S, Kalonia DS. 2006. Protein structural conformation and not second virial coefficient relates to long-term irreversible aggregation of a monoclonal antibody and ovalbumin in solution. Pharm Res 23:1382-1394.
    • (2006) Pharm Res , vol.23 , pp. 1382-1394
    • Bajaj, H.1    Sharma, V.K.2    Badkar, A.3    Zeng, D.4    Nema, S.5    Kalonia, D.S.6
  • 37
    • 33645911471 scopus 로고    scopus 로고
    • Interrelationships of glycosylation and aggregation kinetics for Peniophora lycii phytase
    • Hoiberg-Nielsen R, Fuglsang CC, Arleth L, Westh P. 2006. Interrelationships of glycosylation and aggregation kinetics for Peniophora lycii phytase. Biochemistry 45:5057-5066.
    • (2006) Biochemistry , vol.45 , pp. 5057-5066
    • Hoiberg-Nielsen, R.1    Fuglsang, C.C.2    Arleth, L.3    Westh, P.4
  • 38
    • 52449112053 scopus 로고    scopus 로고
    • High concentration formulations of recombinant human interleukin-1 receptor antagonist: II. Aggregation kinetics
    • Alford JR, Kendrick BS, Carpenter JF, Randolph TW. 2008. High concentration formulations of recombinant human interleukin-1 receptor antagonist: II. Aggregation kinetics. J Pharm Sci 97:3005-3021.
    • (2008) J Pharm Sci , vol.97 , pp. 3005-3021
    • Alford, J.R.1    Kendrick, B.S.2    Carpenter, J.F.3    Randolph, T.W.4
  • 40
    • 5844368173 scopus 로고
    • The scattering of light and the radial distribution function of high-polymer solutions
    • Zimm BH. 1948. The scattering of light and the radial distribution function of high-polymer solutions. J Chem Phys 16:1093-1099.
    • (1948) J Chem Phys , vol.16 , pp. 1093-1099
    • Zimm, B.H.1
  • 42
    • 0004204454 scopus 로고
    • Peptides and proteins
    • Sober H, editor, 1st edition. Cleveland, OH: The Chemical Rubber Co. pp
    • Smith M. 1970. Peptides and proteins. In: Sober H, editor. Handbook of biochemistry. 1st edition. Cleveland, OH: The Chemical Rubber Co. pp. 71-98.
    • (1970) Handbook of biochemistry , pp. 71-98
    • Smith, M.1
  • 43
    • 3342998629 scopus 로고    scopus 로고
    • Acoustical properties of aqueous solutions of urea: Reference data for the ultrasonic spectrometry of liquids
    • Hagen R, Behrends R, Kaatze U. 2004. Acoustical properties of aqueous solutions of urea: Reference data for the ultrasonic spectrometry of liquids. J Chem Eng Data 49:988-991.
    • (2004) J Chem Eng Data , vol.49 , pp. 988-991
    • Hagen, R.1    Behrends, R.2    Kaatze, U.3
  • 44
    • 0023055734 scopus 로고
    • Pressure dissociation and conformational drift of the beta dimer of tryptophan synthase
    • Silva JL, Miles EW, Weber G. 1986. Pressure dissociation and conformational drift of the beta dimer of tryptophan synthase. Biochemistry 25:5780-5786.
    • (1986) Biochemistry , vol.25 , pp. 5780-5786
    • Silva, J.L.1    Miles, E.W.2    Weber, G.3
  • 45
    • 0002343673 scopus 로고
    • Measuring the conformational stability of a protein
    • Creighton TE, editor, 1st edition. New York: IRL Press at Oxford University Press. pp
    • Pace CN, Shirley BA, Thomson JA. 1989. Measuring the conformational stability of a protein. In: Creighton TE, editor. Protein structure, a practical approach. 1st edition. New York: IRL Press at Oxford University Press. pp. 311-330.
    • (1989) Protein structure, a practical approach , pp. 311-330
    • Pace, C.N.1    Shirley, B.A.2    Thomson, J.A.3
  • 46
    • 84919873764 scopus 로고    scopus 로고
    • Non-native protein aggregation: Pathways, kinetics, and shelf-life prediction
    • Murphy RM, Tsai AM, editors, 1st edition. New York: Springer. pp
    • Roberts CJ. 2006. Non-native protein aggregation: Pathways, kinetics, and shelf-life prediction. In: Murphy RM, Tsai AM, editors. Misbehaving proteins: Protein misfolding, aggregation, and stability. 1st edition. New York: Springer. pp. 17-46.
    • (2006) Misbehaving proteins: Protein misfolding, aggregation, and stability , pp. 17-46
    • Roberts, C.J.1
  • 47
    • 0242684664 scopus 로고    scopus 로고
    • Irreversible aggregation of recombinant bovine granulocyte-colony stimulating factor (bG-CSF) and implications for predicting protein shelf life
    • Roberts CJ, Darrington RT, Whitley MB. 2003. Irreversible aggregation of recombinant bovine granulocyte-colony stimulating factor (bG-CSF) and implications for predicting protein shelf life. J Pharm Sci 92:1095-1111.
    • (2003) J Pharm Sci , vol.92 , pp. 1095-1111
    • Roberts, C.J.1    Darrington, R.T.2    Whitley, M.B.3
  • 48
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone F. 1999. Analysis of protein aggregation kinetics. Methods Enzymol 309:256-274.
    • (1999) Methods Enzymol , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 49
    • 55749109195 scopus 로고    scopus 로고
    • Shaken, not stirred: Mechanical stress testing of an IgG1 antibody
    • Kiese S, Papppenberger A, Friess W, Mahler HC. 2008. Shaken, not stirred: Mechanical stress testing of an IgG1 antibody. J Pharm Sci 97:4347-4366.
    • (2008) J Pharm Sci , vol.97 , pp. 4347-4366
    • Kiese, S.1    Papppenberger, A.2    Friess, W.3    Mahler, H.C.4
  • 50
    • 0036239473 scopus 로고    scopus 로고
    • Aggregation of recombinant bovine granulocyte colony stimulating factor in solution
    • Bartkowski R, Kitchel R, Peckham N, Margulis L. 2002. Aggregation of recombinant bovine granulocyte colony stimulating factor in solution. J Protein Chem 21:137-143.
    • (2002) J Protein Chem , vol.21 , pp. 137-143
    • Bartkowski, R.1    Kitchel, R.2    Peckham, N.3    Margulis, L.4
  • 51
    • 0028576509 scopus 로고
    • Approaches to analysis of aggregates and demonstrating mass balance in pharmaceutical protein (basic fibroblast growth factor) formulations
    • Shahrokh Z, Stratton PR, Eberlein GA, Wang YJ. 1994. Approaches to analysis of aggregates and demonstrating mass balance in pharmaceutical protein (basic fibroblast growth factor) formulations. J Pharm Sci 83:1645-1650.
    • (1994) J Pharm Sci , vol.83 , pp. 1645-1650
    • Shahrokh, Z.1    Stratton, P.R.2    Eberlein, G.A.3    Wang, Y.J.4
  • 52
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state
    • Pallitto MM, Murphy RM. 2001. A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state. Biophys J 81:1805-1822.
    • (2001) Biophys J , vol.81 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 53
    • 35848945494 scopus 로고    scopus 로고
    • Reconsidering the mechanism of polyglutamine peptide aggregation
    • Lee CC, Walters RH, Murphy RM. 2007. Reconsidering the mechanism of polyglutamine peptide aggregation. Biochemistry 46:12810-12820.
    • (2007) Biochemistry , vol.46 , pp. 12810-12820
    • Lee, C.C.1    Walters, R.H.2    Murphy, R.M.3
  • 54
    • 0343247668 scopus 로고    scopus 로고
    • The native and the heat-induced denatured states of alpha-chymotrypsinogen A: Thermodynamic and spectroscopic studies
    • Chalikian TV, Volker J, Anafi D, Breslauer KJ. 1997. The native and the heat-induced denatured states of alpha-chymotrypsinogen A: Thermodynamic and spectroscopic studies. J Mol Biol 274: 237-252.
    • (1997) J Mol Biol , vol.274 , pp. 237-252
    • Chalikian, T.V.1    Volker, J.2    Anafi, D.3    Breslauer, K.J.4
  • 57
    • 0003527976 scopus 로고    scopus 로고
    • 1st edition. Sausalito, CA: University Science Books
    • McQuarrie DA. 2000. Statistical mechanics. 1st edition. Sausalito, CA: University Science Books.
    • (2000) Statistical mechanics
    • McQuarrie, D.A.1
  • 58
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin RL. 1996. How Hofmeister ion interactions affect protein stability. Biophys J 71:2056-2063.
    • (1996) Biophys J , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 59
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • Pace CN, Shirley BA, McNutt M, Gajiwala K. 1996. Forces contributing to the conformational stability of proteins. FASEB J 10:75-83.
    • (1996) FASEB J , vol.10 , pp. 75-83
    • Pace, C.N.1    Shirley, B.A.2    McNutt, M.3    Gajiwala, K.4
  • 60
    • 0024291318 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of delta G degrees N-U values in a thermodynamic cycle
    • Bolen DW, Santoro MM. 1988. Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of delta G degrees N-U values in a thermodynamic cycle. Biochemistry 27:8069-8074.
    • (1988) Biochemistry , vol.27 , pp. 8069-8074
    • Bolen, D.W.1    Santoro, M.M.2
  • 61
    • 0000586259 scopus 로고
    • Low temperature denaturation of chymotrypsinogen in aqueous solution and in frozen aqueous solution. Frozen Cell, A
    • Brandts JF, Fu J, Nordin JH. 1970. Low temperature denaturation of chymotrypsinogen in aqueous solution and in frozen aqueous solution. Frozen Cell, A Ciba Foundation Symposium, pp. 189-212.
    • (1970) Ciba Foundation Symposium , pp. 189-212
    • Brandts, J.F.1    Fu, J.2    Nordin, J.H.3
  • 62
    • 33947481462 scopus 로고
    • The thermodynamics of protein denaturation. I. The denaturation of chymotrypsinogen
    • Brandts JF. 1964. The thermodynamics of protein denaturation. I. The denaturation of chymotrypsinogen. J Am Chem Soc 86:4291-4301.
    • (1964) J Am Chem Soc , vol.86 , pp. 4291-4301
    • Brandts, J.F.1
  • 63
    • 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 JJ, Payne RW, Manning MC, Wilson WW, Henry CS. 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    Manning, M.C.3    Wilson, W.W.4    Henry, C.S.5
  • 64
    • 0035121714 scopus 로고    scopus 로고
    • Correlation between the osmotic second virial coefficient and the solubility of proteins
    • Ruppert S, Sandler SI, Lenhoff AM. 2001. Correlation between the osmotic second virial coefficient and the solubility of proteins. Biotechnol Prog 17:182-187.
    • (2001) Biotechnol Prog , vol.17 , pp. 182-187
    • Ruppert, S.1    Sandler, S.I.2    Lenhoff, A.M.3
  • 66
    • 0142122294 scopus 로고    scopus 로고
    • Measurements of protein self-association as a guide to crystallization
    • Tessier PM, Lenhoff AM. 2003. Measurements of protein self-association 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
  • 67
    • 50849109872 scopus 로고    scopus 로고
    • Common motifs in protein self-assembly
    • discussion 309-225, 419-220
    • Krebs MR, Domike KR, Cannon D, Donald AM. 2008. Common motifs in protein self-assembly. Faraday Discuss 139:265-274 (discussion 309-225, 419-220).
    • (2008) Faraday Discuss , vol.139 , pp. 265-274
    • Krebs, M.R.1    Domike, K.R.2    Cannon, D.3    Donald, A.M.4
  • 68
    • 34247644354 scopus 로고    scopus 로고
    • Nonequivalence of second virial coefficients from sedimentation equilibrium and static light scattering studies of protein solutions
    • Winzor DJ, Deszczynski M, Harding SE, Wills PR. 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    Harding, S.E.3    Wills, P.R.4
  • 69
    • 61949220851 scopus 로고    scopus 로고
    • Liquid state theory of polyelectrolyte solutions
    • Yethiraj A. 2009. Liquid state theory of polyelectrolyte solutions. J Phys Chem B 113:1539-1551.
    • (2009) J Phys Chem B , vol.113 , pp. 1539-1551
    • Yethiraj, A.1


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