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Volumn 207, Issue , 2015, Pages 21-29

Aggregate structure, morphology and the effect of aggregation mechanisms on viscosity at elevated protein concentrations

Author keywords

Aggregate mechanism; Protein aggregation; Protein structure; Viscosity

Indexed keywords

CHYMOTRYPSINOGEN; MONOMER; POLYMER;

EID: 84939217619     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2015.07.002     Document Type: Article
Times cited : (33)

References (55)
  • 1
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: an immunologic perspective
    • A.S. Rosenberg Effects of protein aggregates: an immunologic perspective AAPS J. 8 2006 E501 E507
    • (2006) AAPS J. , vol.8 , pp. E501-E507
    • Rosenberg, A.S.1
  • 2
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • S.J. Shire, Z. Shahrokh, and J. Liu Challenges in the development of high protein concentration formulations J. Pharm. Sci. 93 2004 1390 1402
    • (2004) J. Pharm. Sci. , vol.93 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 3
    • 84868207432 scopus 로고    scopus 로고
    • Investigating high-concentration monoclonal antibody powder suspension in nonaqueous suspension vehicles for subcutaneous injection
    • M. Bowen, N. Armstrong, and Y. Maa Investigating high-concentration monoclonal antibody powder suspension in nonaqueous suspension vehicles for subcutaneous injection J. Pharm. Sci. 101 2012 4433 4443 10.1002/jps.23324
    • (2012) J. Pharm. Sci. , vol.101 , pp. 4433-4443
    • Bowen, M.1    Armstrong, N.2    Maa, Y.3
  • 4
    • 84863491050 scopus 로고    scopus 로고
    • Weak interactions govern the viscosity of concentrated antibody solutions: high-throughput analysis using the diffusion interaction parameter
    • B.D. Connolly, C. Petry, S. Yadav, B. Demeule, N. Ciaccio, J.M.R. Moore, and et al. Weak interactions govern the viscosity of concentrated antibody solutions: high-throughput analysis using the diffusion interaction parameter Biophys. J. 103 2012 69 78 10.1016/j.bpj.2012.04.047
    • (2012) Biophys. J. , vol.103 , pp. 69-78
    • Connolly, B.D.1    Petry, C.2    Yadav, S.3    Demeule, B.4    Ciaccio, N.5    Moore, J.M.R.6
  • 6
    • 84907260610 scopus 로고    scopus 로고
    • Protein Aggregation and Its Impact on Product Quality
    • C.J. Roberts Protein Aggregation and Its Impact on Product Quality Curr. Opin. Biotech 30 2014 211 217
    • (2014) Curr. Opin. Biotech , vol.30 , pp. 211-217
    • Roberts, C.J.1
  • 7
    • 37349050368 scopus 로고    scopus 로고
    • Nonnative protein polymers: structure, morphology, and relation to nucleation and growth
    • W.F. Weiss, T.K. Hodgdon, E.W. Kaler, A.M. Lenhoff, and C.J. Roberts Nonnative protein polymers: structure, morphology, and relation to nucleation and growth Biophys. J. 93 2007 4392 4403 10.1529/biophysj.107.112102
    • (2007) Biophys. J. , vol.93 , pp. 4392-4403
    • Weiss, W.F.1    Hodgdon, T.K.2    Kaler, E.W.3    Lenhoff, A.M.4    Roberts, C.J.5
  • 8
    • 84870690077 scopus 로고    scopus 로고
    • Comparative signature diagrams to evaluate biophysical data for differences in protein structure across various formulations
    • V. Iyer, N. Maddux, L. Hu, W. Cheng, A.K. Youssef, G. Winter, and et al. Comparative signature diagrams to evaluate biophysical data for differences in protein structure across various formulations J. Pharm. Sci. 102 2013 43 51 10.1002/jps.23367
    • (2013) J. Pharm. Sci. , vol.102 , pp. 43-51
    • Iyer, V.1    Maddux, N.2    Hu, L.3    Cheng, W.4    Youssef, A.K.5    Winter, G.6
  • 9
    • 78049344329 scopus 로고    scopus 로고
    • Diffusion and sedimentation interaction parameters for measuring the second virial coefficient and their utility as predictors of protein aggregation
    • A. Saluja, R.M. Fesinmeyer, S. Hogan, D.N. Brems, and Y.R. Gokarn Diffusion and sedimentation interaction parameters for measuring the second virial coefficient and their utility as predictors of protein aggregation Biophys. J. 99 2010 2657 2665 10.1016/j.bpj.2010.08.020
    • (2010) Biophys. J. , vol.99 , pp. 2657-2665
    • Saluja, A.1    Fesinmeyer, R.M.2    Hogan, S.3    Brems, D.N.4    Gokarn, Y.R.5
  • 10
    • 84872843352 scopus 로고    scopus 로고
    • Coarse-grained modeling of protein second osmotic virial coefficients: sterics and short-ranged attractions
    • A. Grünberger, P.-K. Lai, M.A. Blanco, and C.J. Roberts Coarse-grained modeling of protein second osmotic virial coefficients: sterics and short-ranged attractions J. Phys. Chem. B 117 2013 763 770 10.1021/jp308234j
    • (2013) J. Phys. Chem. B , vol.117 , pp. 763-770
    • Grünberger, A.1    Lai, P.-K.2    Blanco, M.A.3    Roberts, C.J.4
  • 11
    • 0031723926 scopus 로고    scopus 로고
    • Molecular origins of osmotic second virial coefficients of proteins
    • B.L. Neal, D. Asthagiri, and A.M. Lenhoff Molecular origins of osmotic second virial coefficients of proteins Biophys. J. 75 1998 2469 2477
    • (1998) Biophys. J. , vol.75 , pp. 2469-2477
    • Neal, B.L.1    Asthagiri, D.2    Lenhoff, A.M.3
  • 12
    • 84902001346 scopus 로고    scopus 로고
    • Protein-protein interactions in dilute to concentrated solutions: α-chymotrypsinogen in acidic conditions
    • M.A. Blanco, T. Perevozchikova, V. Martorana, M. Manno, and C.J. Roberts Protein-protein interactions in dilute to concentrated solutions: α-chymotrypsinogen in acidic conditions J. Phys. Chem. B 118 2014 5817 5831 10.1021/jp412301h
    • (2014) J. Phys. Chem. B , vol.118 , pp. 5817-5831
    • Blanco, M.A.1    Perevozchikova, T.2    Martorana, V.3    Manno, M.4    Roberts, C.J.5
  • 13
    • 78650577461 scopus 로고    scopus 로고
    • Subvisible particle counting provides a sensitive method of detecting and quantifying aggregation of monoclonal antibody caused by freeze-thawing: insights into the roles of particles in the protein aggregation pathway
    • J.G. Barnard, S. Singh, T.W. Randolph, and J.F. Carpenter Subvisible particle counting provides a sensitive method of detecting and quantifying aggregation of monoclonal antibody caused by freeze-thawing: insights into the roles of particles in the protein aggregation pathway J. Pharm. Sci. 100 2011 492 503 10.1002/jps.22305
    • (2011) J. Pharm. Sci. , vol.100 , pp. 492-503
    • Barnard, J.G.1    Singh, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 14
    • 84947201513 scopus 로고    scopus 로고
    • Critical examination of the colloidal particle model of globular proteins
    • P.S. Sarangapani, S.D. Hudson, R.L. Jones, J.F. Douglas, and J.A. Pathak Critical examination of the colloidal particle model of globular proteins Biophys. J. 108 2015 724 737 10.1016/j.bpj.2014.11.3483
    • (2015) Biophys. J. , vol.108 , pp. 724-737
    • Sarangapani, P.S.1    Hudson, S.D.2    Jones, R.L.3    Douglas, J.F.4    Pathak, J.A.5
  • 15
    • 0141567910 scopus 로고    scopus 로고
    • Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy
    • W. Dzwolak, R. Ravindra, J. Lendermann, and R. Winter Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy Biochemistry (Mosc) 42 2003 11347 11355 10.1021/bi034879h
    • (2003) Biochemistry (Mosc) , vol.42 , pp. 11347-11355
    • Dzwolak, W.1    Ravindra, R.2    Lendermann, J.3    Winter, R.4
  • 16
    • 84881001310 scopus 로고    scopus 로고
    • DSF method optimization and its application in predicting protein thermal aggregation kinetics
    • S. Shi, A. Semple, J. Cheung, and M. Shameem DSF method optimization and its application in predicting protein thermal aggregation kinetics J. Pharm. Sci. 102 2013 2471 2483 10.1002/jps.23633
    • (2013) J. Pharm. Sci. , vol.102 , pp. 2471-2483
    • Shi, S.1    Semple, A.2    Cheung, J.3    Shameem, M.4
  • 17
    • 84878893050 scopus 로고    scopus 로고
    • Aggregation mechanism of an IgG2 and two IgG1 monoclonal antibodies at low pH: from oligomers to larger aggregates
    • P. Arosio, S. Rima, and M. Morbidelli Aggregation mechanism of an IgG2 and two IgG1 monoclonal antibodies at low pH: from oligomers to larger aggregates Pharm. Res. 30 2013 641 654 10.1007/s11095-012-0885-3
    • (2013) Pharm. Res. , vol.30 , pp. 641-654
    • Arosio, P.1    Rima, S.2    Morbidelli, M.3
  • 18
    • 84873886259 scopus 로고    scopus 로고
    • Aggregation of anti-streptavidin immunoglobulin gamma-1 involves Fab unfolding and competing growth pathways mediated by pH and salt concentration
    • N. Kim, R.L. Remmele, D. Liu, V.I. Razinkov, E.J. Fernandez, and C.J. Roberts Aggregation of anti-streptavidin immunoglobulin gamma-1 involves Fab unfolding and competing growth pathways mediated by pH and salt concentration Biophys. Chem. 172 2013 26 36 10.1016/j.bpc.2012.12.004
    • (2013) Biophys. Chem. , vol.172 , pp. 26-36
    • Kim, N.1    Remmele, R.L.2    Liu, D.3    Razinkov, V.I.4    Fernandez, E.J.5    Roberts, C.J.6
  • 19
    • 84870709849 scopus 로고    scopus 로고
    • Application of second-derivative fluorescence spectroscopy to monitor subtle changes in a monoclonal antibody structure
    • S.A. Abbas, G. Gaspar, V.K. Sharma, T.W. Patapoff, and D.S. Kalonia Application of second-derivative fluorescence spectroscopy to monitor subtle changes in a monoclonal antibody structure J. Pharm. Sci. 102 2013 52 61 10.1002/jps.23354
    • (2013) J. Pharm. Sci. , vol.102 , pp. 52-61
    • Abbas, S.A.1    Gaspar, G.2    Sharma, V.K.3    Patapoff, T.W.4    Kalonia, D.S.5
  • 20
    • 74049123780 scopus 로고    scopus 로고
    • Multi-variate approach to global protein aggregation behavior and kinetics: effects of pH, NaCl, and temperature for alpha-chymotrypsinogen A
    • Y. Li, B.A. Ogunnaike, and C.J. Roberts Multi-variate approach to global protein aggregation behavior and kinetics: effects of pH, NaCl, and temperature for alpha-chymotrypsinogen A J. Pharm. Sci. 99 2010 645 662 10.1002/jps.21869
    • (2010) J. Pharm. Sci. , vol.99 , pp. 645-662
    • Li, Y.1    Ogunnaike, B.A.2    Roberts, C.J.3
  • 21
    • 84863981137 scopus 로고    scopus 로고
    • From macroscopic measurements to microscopic mechanisms of protein aggregation
    • S.I.A. Cohen, M. Vendruscolo, C.M. Dobson, and T.P.J. Knowles From macroscopic measurements to microscopic mechanisms of protein aggregation J. Mol. Biol. 421 2012 160 171 10.1016/j.jmb.2012.02.031
    • (2012) J. Mol. Biol. , vol.421 , pp. 160-171
    • Cohen, S.I.A.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.J.4
  • 22
    • 84904546347 scopus 로고    scopus 로고
    • Explaining the non-Newtonian character of aggregating monoclonal antibody solutions using small-angle neutron scattering
    • M.M. Castellanos, J.A. Pathak, W. Leach, S.M. Bishop, and R.H. Colby Explaining the non-Newtonian character of aggregating monoclonal antibody solutions using small-angle neutron scattering Biophys. J. 107 2014 469 476 10.1016/j.bpj.2014.05.015
    • (2014) Biophys. J. , vol.107 , pp. 469-476
    • Castellanos, M.M.1    Pathak, J.A.2    Leach, W.3    Bishop, S.M.4    Colby, R.H.5
  • 23
    • 1642633079 scopus 로고    scopus 로고
    • Solution properties of branched macromolecules
    • Springer ((accessed July 21, 2014))
    • W. Burchard Solution properties of branched macromolecules Branched Polym. II 1999 Springer 113 194 (http://link.springer.com/chapter/10.1007/3-540-49780-3-3 (accessed July 21, 2014))
    • (1999) Branched Polym. II , pp. 113-194
    • Burchard, W.1
  • 25
    • 34250834054 scopus 로고    scopus 로고
    • A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. aggregation with pre-equilibrated unfolding
    • J.M. Andrews, and C.J. Roberts A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. aggregation with pre-equilibrated unfolding J. Phys. Chem. B 111 2007 7897 7913 10.1021/jp070212j
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7897-7913
    • Andrews, J.M.1    Roberts, C.J.2
  • 26
    • 67650072650 scopus 로고    scopus 로고
    • Lumry-Eyring nucleated-polymerization model of protein aggregation kinetics. 2. Competing growth via condensation and chain polymerization
    • Y. Li, and C.J. Roberts Lumry-Eyring nucleated-polymerization model of protein aggregation kinetics. 2. Competing growth via condensation and chain polymerization J. Phys. Chem. B 113 2009 7020 7032 10.1021/jp8083088
    • (2009) J. Phys. Chem. B , vol.113 , pp. 7020-7032
    • Li, Y.1    Roberts, C.J.2
  • 27
    • 84862693132 scopus 로고    scopus 로고
    • Population balance modeling of antibodies aggregation kinetics
    • P. Arosio, S. Rima, M. Lattuada, and M. Morbidelli Population balance modeling of antibodies aggregation kinetics J. Phys. Chem. B 116 2012 7066 7075 10.1021/jp301091n
    • (2012) J. Phys. Chem. B , vol.116 , pp. 7066-7075
    • Arosio, P.1    Rima, S.2    Lattuada, M.3    Morbidelli, M.4
  • 28
    • 84924491222 scopus 로고    scopus 로고
    • A multiscale view of therapeutic protein aggregation: a colloid science perspective
    • L. Nicoud, M. Owczarz, P. Arosio, and M. Morbidelli A multiscale view of therapeutic protein aggregation: a colloid science perspective Biotechnol. J. 10 2015 367 378 10.1002/biot.201400858
    • (2015) Biotechnol. J. , vol.10 , pp. 367-378
    • Nicoud, L.1    Owczarz, M.2    Arosio, P.3    Morbidelli, M.4
  • 29
    • 79954531753 scopus 로고    scopus 로고
    • Nonnative aggregation of an IgG1 antibody in acidic conditions: part 1. Unfolding, colloidal interactions, and formation of high-molecular-weight aggregates
    • R.K. Brummitt, D.P. Nesta, L. Chang, S.F. Chase, T.M. Laue, and C.J. Roberts Nonnative aggregation of an IgG1 antibody in acidic conditions: part 1. Unfolding, colloidal interactions, and formation of high-molecular-weight aggregates J. Pharm. Sci. 100 2011 2087 2103 10.1002/jps.22448
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2087-2103
    • Brummitt, R.K.1    Nesta, D.P.2    Chang, L.3    Chase, S.F.4    Laue, T.M.5    Roberts, C.J.6
  • 30
    • 84928963134 scopus 로고    scopus 로고
    • Specific-ion effects on the aggregation mechanisms and protein-protein interactions for anti-streptavidin immunoglobulin gamma-1
    • G.V. Barnett, V.I. Razinkov, B.A. Kerwin, T.M. Laue, A.H. Woodka, P.D. Butler, and et al. Specific-ion effects on the aggregation mechanisms and protein-protein interactions for anti-streptavidin immunoglobulin gamma-1 J. Phys. Chem. B 2015 10.1021/acs.jpcb.5b01881
    • (2015) J. Phys. Chem. B
    • Barnett, G.V.1    Razinkov, V.I.2    Kerwin, B.A.3    Laue, T.M.4    Woodka, A.H.5    Butler, P.D.6
  • 31
    • 0014963345 scopus 로고
    • Thermodynamics of protein denaturation. Calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation
    • W.M. Jackson, and J.F. Brandts Thermodynamics of protein denaturation. Calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation Biochemistry (Mosc) 9 1970 2294 2301 10.1021/bi00813a011
    • (1970) Biochemistry (Mosc) , vol.9 , pp. 2294-2301
    • Jackson, W.M.1    Brandts, J.F.2
  • 32
    • 34250870678 scopus 로고    scopus 로고
    • Non-native aggregation of α-chymotrypsinogen occurs through nucleation and growth with competing nucleus sizes and negative activation energies
    • J.M. Andrews, and C.J. Roberts Non-native aggregation of α-chymotrypsinogen occurs through nucleation and growth with competing nucleus sizes and negative activation energies Biochemistry (Mosc) 46 2007 7558 7571 10.1021/bi700296f
    • (2007) Biochemistry (Mosc) , vol.46 , pp. 7558-7571
    • Andrews, J.M.1    Roberts, C.J.2
  • 34
    • 84919752783 scopus 로고    scopus 로고
    • Combined dynamic light scattering and Raman spectroscopy approach for characterizing the aggregation of therapeutic proteins
    • E.N. Lewis, W. Qi, L.H. Kidder, S. Amin, S.M. Kenyon, and S. Blake Combined dynamic light scattering and Raman spectroscopy approach for characterizing the aggregation of therapeutic proteins Molecules (Basel Switz.) 19 2014 20888 20905 10.3390/molecules191220888
    • (2014) Molecules (Basel Switz.) , vol.19 , pp. 20888-20905
    • Lewis, E.N.1    Qi, W.2    Kidder, L.H.3    Amin, S.4    Kenyon, S.M.5    Blake, S.6
  • 35
    • 84921021627 scopus 로고    scopus 로고
    • Concomitant Raman spectroscopy and dynamic light scattering for characterization of therapeutic proteins at high concentrations
    • C. Zhou, W. Qi, E. Neil Lewis, and J.F. Carpenter Concomitant Raman spectroscopy and dynamic light scattering for characterization of therapeutic proteins at high concentrations Anal. Biochem. 472 2015 7 20 10.1016/j.ab.2014.11.016
    • (2015) Anal. Biochem. , vol.472 , pp. 7-20
    • Zhou, C.1    Qi, W.2    Neil Lewis, E.3    Carpenter, J.F.4
  • 36
    • 84919683934 scopus 로고    scopus 로고
    • A novel combination of DLS-optical microrheology and low frequency Raman spectroscopy to reveal underlying biopolymer self-assembly and gelation mechanisms
    • S. Amin, S. Blake, S.M. Kenyon, R.C. Kennel, and E.N. Lewis A novel combination of DLS-optical microrheology and low frequency Raman spectroscopy to reveal underlying biopolymer self-assembly and gelation mechanisms J. Chem. Phys. 141 2014 234201 10.1063/1.4903785
    • (2014) J. Chem. Phys. , vol.141 , pp. 234201
    • Amin, S.1    Blake, S.2    Kenyon, S.M.3    Kennel, R.C.4    Lewis, E.N.5
  • 37
    • 0038161224 scopus 로고    scopus 로고
    • Revisiting the method of cumulants for the analysis of dynamic light-scattering data
    • B.J. Frisken Revisiting the method of cumulants for the analysis of dynamic light-scattering data Appl. Opt. 40 2001 4087 4091
    • (2001) Appl. Opt. , vol.40 , pp. 4087-4091
    • Frisken, B.J.1
  • 38
    • 78650154417 scopus 로고    scopus 로고
    • Molecular level insights into thermally induced α-chymotrypsinogen A amyloid aggregation mechanism and semiflexible protofibril morphology
    • A. Zhang, J.L. Jordan, M.I. Ivanova, W.F. Weiss, C.J. Roberts, and E.J. Fernandez Molecular level insights into thermally induced α-chymotrypsinogen A amyloid aggregation mechanism and semiflexible protofibril morphology Biochemistry (Mosc) 49 2010 10553 10564 10.1021/bi1014216
    • (2010) Biochemistry (Mosc) , vol.49 , pp. 10553-10564
    • Zhang, A.1    Jordan, J.L.2    Ivanova, M.I.3    Weiss, W.F.4    Roberts, C.J.5    Fernandez, E.J.6
  • 39
    • 0015510189 scopus 로고
    • Effect of light scattering on the circular dichroism of biological membranes
    • B.J. Litman Effect of light scattering on the circular dichroism of biological membranes Biochemistry (Mosc) 11 1972 3243 3247 10.1021/bi00767a018
    • (1972) Biochemistry (Mosc) , vol.11 , pp. 3243-3247
    • Litman, B.J.1
  • 40
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • A. Barth, and C. Zscherp What vibrations tell us about proteins Q. Rev. Biophys. 35 2002 369 430
    • (2002) Q. Rev. Biophys. , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 41
    • 36849073223 scopus 로고    scopus 로고
    • Raman spectroscopy of protein pharmaceuticals
    • Z.-Q. Wen Raman spectroscopy of protein pharmaceuticals J. Pharm. Sci. 96 2007 2861 2878 10.1002/jps.20895
    • (2007) J. Pharm. Sci. , vol.96 , pp. 2861-2878
    • Wen, Z.-Q.1
  • 42
    • 84894282128 scopus 로고    scopus 로고
    • Aggregates of α-chymotrypsinogen anneal to access more stable states: annealed aggregates are more stable
    • R.W. Maurer, A.K. Hunter, A.S. Robinson, and C.J. Roberts Aggregates of α-chymotrypsinogen anneal to access more stable states: annealed aggregates are more stable Biotechnol. Bioeng. 111 2014 782 791 10.1002/bit.25129
    • (2014) Biotechnol. Bioeng. , vol.111 , pp. 782-791
    • Maurer, R.W.1    Hunter, A.K.2    Robinson, A.S.3    Roberts, C.J.4
  • 43
    • 84864131010 scopus 로고    scopus 로고
    • Size-exclusion chromatography with multi-angle light scattering for elucidating protein aggregation mechanisms
    • E. Sahin, and C.J. Roberts Size-exclusion chromatography with multi-angle light scattering for elucidating protein aggregation mechanisms Methods Mol. Biol. (Clifton NJ) 899 2012 403 423 10.1007/978-1-61779-921-1-25
    • (2012) Methods Mol. Biol. (Clifton NJ) , vol.899 , pp. 403-423
    • Sahin, E.1    Roberts, C.J.2
  • 44
    • 79954494833 scopus 로고    scopus 로고
    • Nonnative aggregation of an IgG1 antibody in acidic conditions, part 2: nucleation and growth kinetics with competing growth mechanisms
    • R.K. Brummitt, D.P. Nesta, L. Chang, A.M. Kroetsch, and C.J. Roberts Nonnative aggregation of an IgG1 antibody in acidic conditions, part 2: nucleation and growth kinetics with competing growth mechanisms J. Pharm. Sci. 100 2011 2104 2119 10.1002/jps.22447
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2104-2119
    • Brummitt, R.K.1    Nesta, D.P.2    Chang, L.3    Kroetsch, A.M.4    Roberts, C.J.5
  • 45
    • 39749110693 scopus 로고    scopus 로고
    • Roberts, nucleation, growth, and activation energies for seeded and unseeded aggregation of α-chymotrypsinogen A
    • J.M. Andrews, and C.J. Weiss Roberts, nucleation, growth, and activation energies for seeded and unseeded aggregation of α-chymotrypsinogen A Biochemistry (Mosc) 47 2008 2397 2403 10.1021/bi7019244
    • (2008) Biochemistry (Mosc) , vol.47 , pp. 2397-2403
    • Andrews, J.M.1    Weiss, C.J.2
  • 46
    • 71549118233 scopus 로고    scopus 로고
    • Chapter 6 Buffers
    • Elsevier ((accessed February 20, 2015))
    • V.S. Stoll, and J.S. Blanchard Chapter 6 Buffers Methods Enzymol 2009 Elsevier 43 56 (http://linkinghub.elsevier.com/retrieve/pii/S0076687909630068 (accessed February 20, 2015))
    • (2009) Methods Enzymol , pp. 43-56
    • Stoll, V.S.1    Blanchard, J.S.2
  • 47
    • 57349090665 scopus 로고    scopus 로고
    • Very fast prediction and rationalization of pKa values for protein-ligand complexes
    • D.C. Bas, D.M. Rogers, and J.H. Jensen Very fast prediction and rationalization of pKa values for protein-ligand complexes Proteins: Struct., Funct., Bioinf. 73 2008 765 783 10.1002/prot.22102
    • (2008) Proteins: Struct., Funct., Bioinf. , vol.73 , pp. 765-783
    • Bas, D.C.1    Rogers, D.M.2    Jensen, J.H.3
  • 48
    • 28644432877 scopus 로고    scopus 로고
    • Very fast empirical prediction and rationalization of protein pKa values
    • H. Li, A.D. Robertson, and J.H. Jensen Very fast empirical prediction and rationalization of protein pKa values Proteins 61 2005 704 721 10.1002/prot.20660
    • (2005) Proteins , vol.61 , pp. 704-721
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 49
    • 79951476387 scopus 로고    scopus 로고
    • PROPKA3: consistent treatment of internal and surface residues in empirical pKa predictions
    • M.H.M. Olsson, C.R. Søndergaard, M. Rostkowski, and J.H. Jensen PROPKA3: consistent treatment of internal and surface residues in empirical pKa predictions J. Chem. Theory Comput. 7 2011 525 537 10.1021/ct100578z
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 525-537
    • Olsson, M.H.M.1    Søndergaard, C.R.2    Rostkowski, M.3    Jensen, J.H.4
  • 50
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • C.J. Roberts Non-native protein aggregation kinetics Biotechnol. Bioeng. 98 2007 927 938 10.1002/bit.21627
    • (2007) Biotechnol. Bioeng. , vol.98 , pp. 927-938
    • Roberts, C.J.1
  • 51
    • 84887904347 scopus 로고    scopus 로고
    • The limitations of an exclusively colloidal view of protein solution hydrodynamics and rheology
    • P.S. Sarangapani, S.D. Hudson, K.B. Migler, and J.A. Pathak The limitations of an exclusively colloidal view of protein solution hydrodynamics and rheology Biophys. J. 105 2013 2418 2426 10.1016/j.bpj.2013.10.012
    • (2013) Biophys. J. , vol.105 , pp. 2418-2426
    • Sarangapani, P.S.1    Hudson, S.D.2    Migler, K.B.3    Pathak, J.A.4
  • 52
    • 79957507854 scopus 로고    scopus 로고
    • Rheology of globular proteins: apparent yield stress, high shear rate viscosity and interfacial viscoelasticity of bovine serum albumin solutions
    • V. Sharma, A. Jaishankar, Y.-C. Wang, and G.H. McKinley Rheology of globular proteins: apparent yield stress, high shear rate viscosity and interfacial viscoelasticity of bovine serum albumin solutions Soft Matter 7 2011 5150 10.1039/c0sm01312a
    • (2011) Soft Matter , vol.7 , pp. 5150
    • Sharma, V.1    Jaishankar, A.2    Wang, Y.-C.3    McKinley, G.H.4
  • 53
    • 77951766649 scopus 로고    scopus 로고
    • Structure and linear viscoelasticity of flexible polymer solutions: comparison of polyelectrolyte and neutral polymer solutions
    • R.H. Colby Structure and linear viscoelasticity of flexible polymer solutions: comparison of polyelectrolyte and neutral polymer solutions Rheol. Acta 49 2009 425 442 10.1007/s00397-009-0413-5
    • (2009) Rheol. Acta , vol.49 , pp. 425-442
    • Colby, R.H.1
  • 54
    • 30344436634 scopus 로고    scopus 로고
    • The scaling of zero-shear viscosities of semidilute polymer solutions with concentration
    • 1978-Present
    • Y. Heo, and R.G. Larson The scaling of zero-shear viscosities of semidilute polymer solutions with concentration J. Rheol. 49 2005 1117 1128 10.1122/1.1993595 (1978-Present)
    • (2005) J. Rheol. , vol.49 , pp. 1117-1128
    • Heo, Y.1    Larson, R.G.2
  • 55
    • 0042438241 scopus 로고
    • Dependence of viscosity of concentrated polymer solutions upon molecular weight and concentration
    • S. Onogi, T. Masuda, N. Miyanaga, and Y. Kimura Dependence of viscosity of concentrated polymer solutions upon molecular weight and concentration J. Polym. Sci. 2 Polym. Phys. 5 1967 899 913 10.1002/pol.1967.160050508
    • (1967) J. Polym. Sci. 2 Polym. Phys. , vol.5 , pp. 899-913
    • Onogi, S.1    Masuda, T.2    Miyanaga, N.3    Kimura, Y.4


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