메뉴 건너뛰기




Volumn 30, Issue 44, 2014, Pages 13205-13216

Investigation into the molecular and thermodynamic basis of protein interactions in multimodal chromatography using functionalized nanoparticles

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; BIOCHEMISTRY; DISSOCIATION; EXPERIMENTS; LIGANDS; NANOPARTICLES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; TITRATION;

EID: 84910635198     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la502141q     Document Type: Article
Times cited : (37)

References (73)
  • 1
    • 0024335074 scopus 로고
    • Interplay of hydrophobic and electrostatic interactions in biopolymer chromatography: Effect of salts on the retention of proteins
    • Melander, W. R.; El Rassi, Z.; Horvath, C. Interplay of hydrophobic and electrostatic interactions in biopolymer chromatography: Effect of salts on the retention of proteins J. Chromatogr. A 1989, 469, 3-27
    • (1989) J. Chromatogr. A , vol.469 , pp. 3-27
    • Melander, W.R.1    El Rassi, Z.2    Horvath, C.3
  • 2
    • 0019515203 scopus 로고
    • Use of mixed-mode, high-performance liquid-chromatography for the separation of peptide and protein mixtures
    • Hancock, W. S.; Sparrow, J. T. Use of mixed-mode, high-performance liquid-chromatography for the separation of peptide and protein mixtures J. Chromatogr. 1981, 206 (1) 71-82
    • (1981) J. Chromatogr. , vol.206 , Issue.1 , pp. 71-82
    • Hancock, W.S.1    Sparrow, J.T.2
  • 3
    • 0000151872 scopus 로고
    • Mixed-mode chromatography of nucleic-acids
    • Mclaughlin, L. W. Mixed-mode chromatography of nucleic-acids Chem. Rev. 1989, 89 (2) 309-319
    • (1989) Chem. Rev. , vol.89 , Issue.2 , pp. 309-319
    • McLaughlin, L.W.1
  • 4
    • 0031555004 scopus 로고    scopus 로고
    • One step purification of chymosin by mixed mode chromatography
    • Burton, S. C.; Haggarty, N. W.; Harding, D. R. K. One step purification of chymosin by mixed mode chromatography Biotechnol. Bioeng. 1997, 56 (1) 45-55
    • (1997) Biotechnol. Bioeng. , vol.56 , Issue.1 , pp. 45-55
    • Burton, S.C.1    Haggarty, N.W.2    Harding, D.R.K.3
  • 5
    • 0030872712 scopus 로고    scopus 로고
    • High-density ligand attachment to brominated allyl matrices and application to mixed mode chromatography of chymosin
    • Burton, S. C.; Harding, D. R. K. High-density ligand attachment to brominated allyl matrices and application to mixed mode chromatography of chymosin J. Chromatogr. A 1997, 775 (1-2) 39-50
    • (1997) J. Chromatogr. A , vol.775 , Issue.12 , pp. 39-50
    • Burton, S.C.1    Harding, D.R.K.2
  • 6
    • 0141857674 scopus 로고    scopus 로고
    • Preparation and characterization of prototypes for multi-modal separation media aimed for capture of negatively charged biomolecules at high salt conditions
    • Johansson, B. L.; Belew, M.; Eriksson, S.; Glad, G.; Lind, O.; Maloisel, J. L.; Norrman, N. Preparation and characterization of prototypes for multi-modal separation media aimed for capture of negatively charged biomolecules at high salt conditions J. Chromatogr. A 2003, 1016 (1) 21-33
    • (2003) J. Chromatogr. A , vol.1016 , Issue.1 , pp. 21-33
    • Johansson, B.L.1    Belew, M.2    Eriksson, S.3    Glad, G.4    Lind, O.5    Maloisel, J.L.6    Norrman, N.7
  • 7
    • 28844477910 scopus 로고    scopus 로고
    • Antibody variable region interactions with Protein A: Implications for the development of generic purification processes
    • Ghose, S.; Allen, M.; Hubbard, B.; Brooks, C.; Cramer, S. M. Antibody variable region interactions with Protein A: Implications for the development of generic purification processes Biotechnol. Bioeng. 2005, 92 (6) 665-673
    • (2005) Biotechnol. Bioeng. , vol.92 , Issue.6 , pp. 665-673
    • Ghose, S.1    Allen, M.2    Hubbard, B.3    Brooks, C.4    Cramer, S.M.5
  • 8
    • 72449157567 scopus 로고    scopus 로고
    • The distinctive separation attributes of mixed-mode resins and their application in monoclonal antibody downstream purification process
    • Chen, J.; Tetrault, J.; Zhang, Y.; Wasserman, A.; Conley, G.; Dileo, M.; Haimes, E.; Nixon, A. E.; Ley, A. The distinctive separation attributes of mixed-mode resins and their application in monoclonal antibody downstream purification process J. Chromatogr. A 2010, 1217 (2) 216-24
    • (2010) J. Chromatogr. A , vol.1217 , Issue.2 , pp. 216-224
    • Chen, J.1    Tetrault, J.2    Zhang, Y.3    Wasserman, A.4    Conley, G.5    Dileo, M.6    Haimes, E.7    Nixon, A.E.8    Ley, A.9
  • 9
    • 72449154277 scopus 로고    scopus 로고
    • Industrial case study: Evaluation of a mixed-mode resin for selective capture of a human growth factor recombinantly expressed in E. Coli
    • Kaleas, K. A.; Schmelzer, C. H.; Pizarro, S. A. Industrial case study: Evaluation of a mixed-mode resin for selective capture of a human growth factor recombinantly expressed in E. coli J. Chromatogr. A 2010, 1217 (2) 235-242
    • (2010) J. Chromatogr. A , vol.1217 , Issue.2 , pp. 235-242
    • Kaleas, K.A.1    Schmelzer, C.H.2    Pizarro, S.A.3
  • 10
    • 37549009897 scopus 로고    scopus 로고
    • Mixed-mode stationary phases as a complementary selectivity concept in liquid chromatography-tandem mass spectrometry-based bioanalytical assays
    • Bicker, W.; Lammerhofer, M.; Lindner, W. Mixed-mode stationary phases as a complementary selectivity concept in liquid chromatography-tandem mass spectrometry-based bioanalytical assays Anal. Bioanal. Chem. 2008, 390 (1) 263-266
    • (2008) Anal. Bioanal. Chem. , vol.390 , Issue.1 , pp. 263-266
    • Bicker, W.1    Lammerhofer, M.2    Lindner, W.3
  • 11
    • 33947603651 scopus 로고    scopus 로고
    • Evaluation and optimization of ZIC-HILIC-RP as an alternative MudPIT strategy
    • Boersema, P. J.; Divecha, N.; Heck, A. J. R.; Mohammed, S. Evaluation and optimization of ZIC-HILIC-RP as an alternative MudPIT strategy J. Proteome Res. 2007, 6 (3) 937-946
    • (2007) J. Proteome Res. , vol.6 , Issue.3 , pp. 937-946
    • Boersema, P.J.1    Divecha, N.2    Heck, A.J.R.3    Mohammed, S.4
  • 12
    • 78049303519 scopus 로고    scopus 로고
    • Evaluation of protein adsorption and preferred binding regions in multimodal chromatography using NMR
    • Chung, W. K.; Freed, A. S.; Holstein, M. A.; McCallum, S. A.; Cramer, S. M. Evaluation of protein adsorption and preferred binding regions in multimodal chromatography using NMR Proc. Natl. Acad. Sci. U. S. A. 2010, 107 (39) 16811-16816
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , Issue.39 , pp. 16811-16816
    • Chung, W.K.1    Freed, A.S.2    Holstein, M.A.3    McCallum, S.A.4    Cramer, S.M.5
  • 13
    • 84857140420 scopus 로고    scopus 로고
    • Probing multimodal ligand binding regions on ubiquitin using nuclear magnetic resonance, chromatography, and molecular dynamics simulations
    • Holstein, M. A.; Chung, W. K.; Parimal, S.; Freed, A. S.; Barquera, B.; McCallum, S. A.; Cramer, S. M. Probing multimodal ligand binding regions on ubiquitin using nuclear magnetic resonance, chromatography, and molecular dynamics simulations J. Chromatogr. A 2012, 1229 (0) 113-120
    • (2012) J. Chromatogr. A , vol.1229 , Issue.0 , pp. 113-120
    • Holstein, M.A.1    Chung, W.K.2    Parimal, S.3    Freed, A.S.4    Barquera, B.5    McCallum, S.A.6    Cramer, S.M.7
  • 14
    • 0142184432 scopus 로고    scopus 로고
    • Studies of protein-ligand interactions by NMR
    • Clarkson, J.; Campbell, I. D. Studies of protein-ligand interactions by NMR Biochem. Soc. Trans. 2003, 31, 1006-1009
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1006-1009
    • Clarkson, J.1    Campbell, I.D.2
  • 15
    • 0032899363 scopus 로고    scopus 로고
    • NMR spectroscopy in structure-based drug design
    • Roberts, G. C. K. NMR spectroscopy in structure-based drug design Curr. Opin. Biotechnol. 1999, 10 (1) 42-47
    • (1999) Curr. Opin. Biotechnol. , vol.10 , Issue.1 , pp. 42-47
    • Roberts, G.C.K.1
  • 17
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • Zuiderweg, E. R. P. Mapping protein-protein interactions in solution by NMR spectroscopy Biochemistry 2001, 41 (1) 1-7
    • (2001) Biochemistry , vol.41 , Issue.1 , pp. 1-7
    • Zuiderweg, E.R.P.1
  • 19
    • 0034673316 scopus 로고    scopus 로고
    • The use of differential chemical shifts for determining the binding site location and orientation of protein-bound ligands
    • Medek, A.; Hajduk, P. J.; Mack, J.; Fesik, S. W. The use of differential chemical shifts for determining the binding site location and orientation of protein-bound ligands J. Am. Chem. Soc. 2000, 122 (6) 1241-1242
    • (2000) J. Am. Chem. Soc. , vol.122 , Issue.6 , pp. 1241-1242
    • Medek, A.1    Hajduk, P.J.2    Mack, J.3    Fesik, S.W.4
  • 20
    • 84872106709 scopus 로고    scopus 로고
    • Effects of urea on selectivity and protein-ligand interactions in multimodal cation exchange chromatography
    • Holstein, M. A.; Parimal, S.; McCallum, S. A.; Cramer, S. M. Effects of urea on selectivity and protein-ligand interactions in multimodal cation exchange chromatography Langmuir 2012, 29 (1) 158-167
    • (2012) Langmuir , vol.29 , Issue.1 , pp. 158-167
    • Holstein, M.A.1    Parimal, S.2    McCallum, S.A.3    Cramer, S.M.4
  • 21
    • 1342302795 scopus 로고    scopus 로고
    • The interaction of proteins with solid surfaces
    • Gray, J. J. The interaction of proteins with solid surfaces Curr. Opin. Struct. Biol. 2004, 14 (1) 110-115
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , Issue.1 , pp. 110-115
    • Gray, J.J.1
  • 22
    • 0035951086 scopus 로고    scopus 로고
    • Structure and dynamics of hydrated statherin on hydroxyapatite as determined by solid-state NMR
    • Long, J. R.; Shaw, W. J.; Stayton, P. S.; Drobny, G. P. Structure and dynamics of hydrated statherin on hydroxyapatite as determined by solid-state NMR Biochemistry 2001, 40 (51) 15451-15455
    • (2001) Biochemistry , vol.40 , Issue.51 , pp. 15451-15455
    • Long, J.R.1    Shaw, W.J.2    Stayton, P.S.3    Drobny, G.P.4
  • 23
    • 0038745552 scopus 로고    scopus 로고
    • Asymmetric α-helicity loss within a peptide adsorbed onto charged colloidal substrates
    • Read, M. J.; Burkett, S. L. Asymmetric α-helicity loss within a peptide adsorbed onto charged colloidal substrates J. Colloid Interface Sci. 2003, 261 (2) 255-263
    • (2003) J. Colloid Interface Sci. , vol.261 , Issue.2 , pp. 255-263
    • Read, M.J.1    Burkett, S.L.2
  • 24
    • 0034653463 scopus 로고    scopus 로고
    • Adsorbed layers of ferritin at solid and fluid interfaces studied by atomic force microscopy
    • Johnson, C. A.; Yuan, Y.; Lenhoff, A. M. Adsorbed layers of ferritin at solid and fluid interfaces studied by atomic force microscopy J. Colloid Interface Sci. 2000, 223 (2) 261-272
    • (2000) J. Colloid Interface Sci. , vol.223 , Issue.2 , pp. 261-272
    • Johnson, C.A.1    Yuan, Y.2    Lenhoff, A.M.3
  • 25
    • 77955562565 scopus 로고    scopus 로고
    • Protein-nanoparticle interaction: Identification of the ubiquitin-gold nanoparticle interaction site
    • Calzolai, L.; Franchini, F.; Gilliland, D.; Rossi, F. O. Protein-nanoparticle interaction: Identification of the ubiquitin-gold nanoparticle interaction site Nano Lett. 2010, 10 (8) 3101-3105
    • (2010) Nano Lett. , vol.10 , Issue.8 , pp. 3101-3105
    • Calzolai, L.1    Franchini, F.2    Gilliland, D.3    Rossi, F.O.4
  • 26
    • 0037342549 scopus 로고    scopus 로고
    • α-Lactalbumin tertiary structure changes on hydrophobic interaction chromatography surfaces
    • Tibbs Jones, T.; Fernandez, E. J. α-Lactalbumin tertiary structure changes on hydrophobic interaction chromatography surfaces J. Colloid Interface Sci. 2003, 259 (1) 27-35
    • (2003) J. Colloid Interface Sci. , vol.259 , Issue.1 , pp. 27-35
    • Tibbs Jones, T.1    Fernandez, E.J.2
  • 27
    • 0035152884 scopus 로고    scopus 로고
    • Protein unfolding during reversed-phase chromatography: I. Effect of surface properties and duration of adsorption
    • McNay, J. L. M.; Fernandez, E. J. Protein unfolding during reversed-phase chromatography: I. Effect of surface properties and duration of adsorption Biotechnol. Bioeng. 2001, 76 (3) 224-232
    • (2001) Biotechnol. Bioeng. , vol.76 , Issue.3 , pp. 224-232
    • McNay, J.L.M.1    Fernandez, E.J.2
  • 28
    • 3843093727 scopus 로고    scopus 로고
    • Conformation and orientation of a protein folding intermediate trapped by adsorption
    • Engel, M. F. M.; Visser, A. J. W. G.; van Mierlo, C. P. M. Conformation and orientation of a protein folding intermediate trapped by adsorption Proc. Natl. Acad. Sci. U. S. A. 2004, 101 (31) 11316-11321
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , Issue.31 , pp. 11316-11321
    • Engel, M.F.M.1    Visser, A.J.W.G.2    Van Mierlo, C.P.M.3
  • 29
    • 10044277018 scopus 로고    scopus 로고
    • Protein adsorption onto silica nanoparticles: Conformational changes depend on the particles: Curvature and the protein stability
    • Lundqvist, M.; Sethson, I.; Jonsson, B.-H. Protein adsorption onto silica nanoparticles: conformational changes depend on the particles: curvature and the protein stability Langmuir 2004, 20 (24) 10639-10647
    • (2004) Langmuir , vol.20 , Issue.24 , pp. 10639-10647
    • Lundqvist, M.1    Sethson, I.2    Jonsson, B.-H.3
  • 30
    • 0002181394 scopus 로고
    • Reversibility and the Mechanism of Protein Adsorption
    • American Chemical Society: Washington, DC
    • Norde, W.; Haynes Charles, A. Reversibility and the Mechanism of Protein Adsorption. In Proteins at Interfaces II; American Chemical Society: Washington, DC, 1995; Vol. 602, pp 26-40.
    • (1995) Proteins at Interfaces II , vol.602 , pp. 26-40
    • Norde, W.1    Haynes Charles, A.2
  • 31
    • 0002445915 scopus 로고
    • Structure of adsorbed and desorbed proteins
    • Norde, W.; Favier, J. P. Structure of adsorbed and desorbed proteins Colloids Surf. 1992, 64 (1) 87-93
    • (1992) Colloids Surf. , vol.64 , Issue.1 , pp. 87-93
    • Norde, W.1    Favier, J.P.2
  • 32
    • 0034717340 scopus 로고    scopus 로고
    • BSA structural changes during homomolecular exchange between the adsorbed and the dissolved states
    • Norde, W.; Giacomelli, C. E. BSA structural changes during homomolecular exchange between the adsorbed and the dissolved states J. Biotechnol. 2000, 79 (3) 259-268
    • (2000) J. Biotechnol. , vol.79 , Issue.3 , pp. 259-268
    • Norde, W.1    Giacomelli, C.E.2
  • 33
    • 0037117890 scopus 로고    scopus 로고
    • Functionalized poly(ethylene glycol)-grafted polysiloxane monolayers for control of protein binding
    • Xia, N.; Hu, Y.; Grainger, D. W.; Castner, D. G. Functionalized poly(ethylene glycol)-grafted polysiloxane monolayers for control of protein binding Langmuir 2002, 18 (8) 3255-3262
    • (2002) Langmuir , vol.18 , Issue.8 , pp. 3255-3262
    • Xia, N.1    Hu, Y.2    Grainger, D.W.3    Castner, D.G.4
  • 34
    • 0013172998 scopus 로고    scopus 로고
    • Controlling antibody orientation on charged self-assembled monolayers
    • Chen, S.; Liu, L.; Zhou, J.; Jiang, S. Controlling antibody orientation on charged self-assembled monolayers Langmuir 2003, 19 (7) 2859-2864
    • (2003) Langmuir , vol.19 , Issue.7 , pp. 2859-2864
    • Chen, S.1    Liu, L.2    Zhou, J.3    Jiang, S.4
  • 35
    • 0038061482 scopus 로고    scopus 로고
    • Protein adsorption on alkanethiolate self-assembled monolayers: Nanoscale surface structural and chemical effects
    • Li, L.; Chen, S.; Jiang, S. Protein adsorption on alkanethiolate self-assembled monolayers: Nanoscale surface structural and chemical effects Langmuir 2003, 19 (7) 2974-2982
    • (2003) Langmuir , vol.19 , Issue.7 , pp. 2974-2982
    • Li, L.1    Chen, S.2    Jiang, S.3
  • 36
    • 0037418426 scopus 로고    scopus 로고
    • Adsorption of proteins to hydrophobic sites on mixed self-assembled monolayers
    • Ostuni, E.; Grzybowski, B. A.; Mrksich, M.; Roberts, C. S.; Whitesides, G. M. Adsorption of proteins to hydrophobic sites on mixed self-assembled monolayers Langmuir 2003, 19 (5) 1861-1872
    • (2003) Langmuir , vol.19 , Issue.5 , pp. 1861-1872
    • Ostuni, E.1    Grzybowski, B.A.2    Mrksich, M.3    Roberts, C.S.4    Whitesides, G.M.5
  • 39
    • 34848898194 scopus 로고    scopus 로고
    • Biomimetic interactions of proteins with functionalized nanoparticles: A thermodynamic study
    • De, M.; You, C.-C.; Srivastava, S.; Rotello, V. M. Biomimetic interactions of proteins with functionalized nanoparticles: A thermodynamic study J. Am. Chem. Soc. 2007, 129 (35) 10747-10753
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.35 , pp. 10747-10753
    • De, M.1    You, C.-C.2    Srivastava, S.3    Rotello, V.M.4
  • 40
    • 25144471199 scopus 로고    scopus 로고
    • Tunable inhibition and denaturation of α-chymotrypsin with amino acid-functionalized gold nanoparticles
    • You, C.-C.; De, M.; Han, G.; Rotello, V. M. Tunable inhibition and denaturation of α-chymotrypsin with amino acid-functionalized gold nanoparticles J. Am. Chem. Soc. 2005, 127 (37) 12873-12881
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.37 , pp. 12873-12881
    • You, C.-C.1    De, M.2    Han, G.3    Rotello, V.M.4
  • 42
    • 0032630577 scopus 로고    scopus 로고
    • Dynamics of place-exchange reactions on monolayer-protected gold cluster molecules
    • Hostetler, M. J.; Templeton, A. C.; Murray, R. W. Dynamics of place-exchange reactions on monolayer-protected gold cluster molecules Langmuir 1999, 15 (11) 3782-3789
    • (1999) Langmuir , vol.15 , Issue.11 , pp. 3782-3789
    • Hostetler, M.J.1    Templeton, A.C.2    Murray, R.W.3
  • 43
    • 0030009986 scopus 로고    scopus 로고
    • Monolayers in three dimensions: Synthesis and electrochemistry of ω-functionalized alkanethiolate-stabilized gold cluster compounds
    • Hostetler, M. J.; Green, S. J.; Stokes, J. J.; Murray, R. W. Monolayers in three dimensions: Synthesis and electrochemistry of ω-functionalized alkanethiolate-stabilized gold cluster compounds J. Am. Chem. Soc. 1996, 118 (17) 4212-4213
    • (1996) J. Am. Chem. Soc. , vol.118 , Issue.17 , pp. 4212-4213
    • Hostetler, M.J.1    Green, S.J.2    Stokes, J.J.3    Murray, R.W.4
  • 44
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T.; Williston, S.; Brandts, J. F.; Lin, L.-N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter Anal. Biochem. 1989, 179 (1) 131-137
    • (1989) Anal. Biochem. , vol.179 , Issue.1 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.-N.4
  • 45
  • 46
    • 84910683881 scopus 로고    scopus 로고
    • SPARKY 3; University of California, San Francisco.
    • Goddard, T. D.; Kneller, D. G. SPARKY 3; University of California, San Francisco.
    • Goddard, T.D.1    Kneller, D.G.2
  • 47
    • 84910659226 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System, v 1.3.
    • Schrödinger, L. The PyMOL Molecular Graphics System, v 1.3.
    • Schrödinger, L.1
  • 48
    • 74249092297 scopus 로고    scopus 로고
    • Utilization of lysozyme charge ladders to examine the effects of protein surface charge distribution on binding affinity in ion exchange systems
    • Chung, W. K.; Evans, S. T.; Freed, A. S.; Keba, J. J.; Baer, Z. C.; Rege, K.; Cramer, S. M. Utilization of lysozyme charge ladders to examine the effects of protein surface charge distribution on binding affinity in ion exchange systems Langmuir 2010, 26 (2) 759-68
    • (2010) Langmuir , vol.26 , Issue.2 , pp. 759-768
    • Chung, W.K.1    Evans, S.T.2    Freed, A.S.3    Keba, J.J.4    Baer, Z.C.5    Rege, K.6    Cramer, S.M.7
  • 49
    • 60349125332 scopus 로고    scopus 로고
    • Investigation of protein binding affinity and preferred orientations in ion exchange systems using a homologous protein library
    • Chung, W. K.; Hou, Y.; Freed, A.; Holstein, M.; Makhatadze, G. I.; Cramer, S. M. Investigation of protein binding affinity and preferred orientations in ion exchange systems using a homologous protein library Biotechnol. Bioeng. 2009, 102 (3) 869-881
    • (2009) Biotechnol. Bioeng. , vol.102 , Issue.3 , pp. 869-881
    • Chung, W.K.1    Hou, Y.2    Freed, A.3    Holstein, M.4    Makhatadze, G.I.5    Cramer, S.M.6
  • 50
    • 77958591673 scopus 로고    scopus 로고
    • Ion exchange chromatographic behavior of a homologous cytochrome C variant library obtained by controlled succinylation
    • Chung, W. K.; Holstein, M. A.; Freed, A. S.; Evans, S. T.; Baer, Z. C.; Cramer, S. M. Ion exchange chromatographic behavior of a homologous cytochrome C variant library obtained by controlled succinylation Sep. Sci. Technol. 2010, 45 (15) 2144-2152
    • (2010) Sep. Sci. Technol. , vol.45 , Issue.15 , pp. 2144-2152
    • Chung, W.K.1    Holstein, M.A.2    Freed, A.S.3    Evans, S.T.4    Baer, Z.C.5    Cramer, S.M.6
  • 51
    • 80855139883 scopus 로고    scopus 로고
    • Molecular simulations of multimodal ligand-protein binding: Elucidation of binding sites and correlation with experiments
    • Freed, A. S.; Garde, S.; Cramer, S. M. Molecular simulations of multimodal ligand-protein binding: Elucidation of binding sites and correlation with experiments J. Phys. Chem. B 2011, 115 (45) 13320-13327
    • (2011) J. Phys. Chem. B , vol.115 , Issue.45 , pp. 13320-13327
    • Freed, A.S.1    Garde, S.2    Cramer, S.M.3
  • 53
    • 77952467953 scopus 로고    scopus 로고
    • Prediction of aggregation prone regions of therapeutic proteins
    • Chennamsetty, N.; Voynov, V.; Kayser, V.; Helk, B.; Trout, B. L. Prediction of aggregation prone regions of therapeutic proteins J. Phys. Chem. B 2010, 114 (19) 6614-6624
    • (2010) J. Phys. Chem. B , vol.114 , Issue.19 , pp. 6614-6624
    • Chennamsetty, N.1    Voynov, V.2    Kayser, V.3    Helk, B.4    Trout, B.L.5
  • 54
    • 1642535341 scopus 로고    scopus 로고
    • Control of protein structure and function through surface recognition by tailored nanoparticle scaffolds
    • Hong, R.; Fischer, N. O.; Verma, A.; Goodman, C. M.; Emrick, T.; Rotello, V. M. Control of protein structure and function through surface recognition by tailored nanoparticle scaffolds J. Am. Chem. Soc. 2004, 126 (3) 739-743
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.3 , pp. 739-743
    • Hong, R.1    Fischer, N.O.2    Verma, A.3    Goodman, C.M.4    Emrick, T.5    Rotello, V.M.6
  • 55
    • 0034705635 scopus 로고    scopus 로고
    • Pore size distributions of cation-exchange adsorbents determined by inverse size-exclusion chromatography
    • DePhillips, P.; Lenhoff, A. M. Pore size distributions of cation-exchange adsorbents determined by inverse size-exclusion chromatography J. Chromatogr. A 2000, 883 (1) 39-54
    • (2000) J. Chromatogr. A , vol.883 , Issue.1 , pp. 39-54
    • Dephillips, P.1    Lenhoff, A.M.2
  • 56
    • 84855269204 scopus 로고    scopus 로고
    • Applications of isothermal titration calorimetry in pure and applied research - Survey of the literature from 2010
    • Ghai, R.; Falconer, R. J.; Collins, B. M. Applications of isothermal titration calorimetry in pure and applied research - survey of the literature from 2010 J. Mol. Recognit. 2012, 25 (1) 32-52
    • (2012) J. Mol. Recognit. , vol.25 , Issue.1 , pp. 32-52
    • Ghai, R.1    Falconer, R.J.2    Collins, B.M.3
  • 57
    • 84881243456 scopus 로고    scopus 로고
    • Structural and biophysical characterization of the interactions between the death domain of fas receptor and calmodulin
    • Fernandez, T. F.; Samal, A. B.; Bedwell, G. J.; Chen, Y.; Saad, J. S. Structural and biophysical characterization of the interactions between the death domain of fas receptor and calmodulin J. Biol. Chem. 2013, 288 (30) 21898-21908
    • (2013) J. Biol. Chem. , vol.288 , Issue.30 , pp. 21898-21908
    • Fernandez, T.F.1    Samal, A.B.2    Bedwell, G.J.3    Chen, Y.4    Saad, J.S.5
  • 58
    • 84866279744 scopus 로고    scopus 로고
    • Structural basis for entropy-driven cellulose binding by a type-A cellulose-binding module (CBM) and bacterial expansin
    • Georgelis, N.; Yennawar, N. H.; Cosgrove, D. J. Structural basis for entropy-driven cellulose binding by a type-A cellulose-binding module (CBM) and bacterial expansin Proc. Natl. Acad. Sci. U. S. A. 2012, 109 (37) 14830-14835
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , Issue.37 , pp. 14830-14835
    • Georgelis, N.1    Yennawar, N.H.2    Cosgrove, D.J.3
  • 59
    • 48249102785 scopus 로고    scopus 로고
    • Calorimetry and thermodynamics in drug design
    • Chaires, J. B. Calorimetry and thermodynamics in drug design Annu. Rev. Biophys. 2008, 37 (1) 135-151
    • (2008) Annu. Rev. Biophys. , vol.37 , Issue.1 , pp. 135-151
    • Chaires, J.B.1
  • 60
    • 12044254701 scopus 로고
    • A direct measure of the contribution of solvent reorganization to the enthalpy of binding
    • Chervenak, M. C.; Toone, E. J. A direct measure of the contribution of solvent reorganization to the enthalpy of binding J. Am. Chem. Soc. 1994, 116 (23) 10533-10539
    • (1994) J. Am. Chem. Soc. , vol.116 , Issue.23 , pp. 10533-10539
    • Chervenak, M.C.1    Toone, E.J.2
  • 61
    • 0027305948 scopus 로고
    • Contribution of hydration to protein folding thermodynamics: I. The enthalpy of hydration
    • Makhatadze, G. I.; Privalov, P. L. Contribution of hydration to protein folding thermodynamics: I. The enthalpy of hydration J. Mol. Biol. 1993, 232 (2) 639-659
    • (1993) J. Mol. Biol. , vol.232 , Issue.2 , pp. 639-659
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 62
    • 0027250627 scopus 로고
    • Contribution of hydration to protein folding thermodynamics: II. The entropy and Gibbs energy of hydration
    • Privalov, P. L.; Makhatadze, G. I. Contribution of hydration to protein folding thermodynamics: II. The entropy and Gibbs energy of hydration J. Mol. Biol. 1993, 232 (2) 660-679
    • (1993) J. Mol. Biol. , vol.232 , Issue.2 , pp. 660-679
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 66
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • Chandler, D. Interfaces and the driving force of hydrophobic assembly Nature 2005, 437 (7059) 640-647
    • (2005) Nature , vol.437 , Issue.7059 , pp. 640-647
    • Chandler, D.1
  • 67
    • 0011960339 scopus 로고    scopus 로고
    • Hydrophobicity at small and large length scales
    • Lum, K.; Chandler, D.; Weeks, J. D. Hydrophobicity at small and large length scales J. Phys. Chem. B 1999, 103 (22) 4570-4577
    • (1999) J. Phys. Chem. B , vol.103 , Issue.22 , pp. 4570-4577
    • Lum, K.1    Chandler, D.2    Weeks, J.D.3
  • 68
    • 22144481993 scopus 로고    scopus 로고
    • Hydrophobic hydration from small to large lengthscales: Understanding and manipulating the crossover
    • Rajamani, S.; Truskett, T. M.; Garde, S. Hydrophobic hydration from small to large lengthscales: Understanding and manipulating the crossover Proc. Natl. Acad. Sci. U. S. A. 2005, 102 (27) 9475-9480
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.27 , pp. 9475-9480
    • Rajamani, S.1    Truskett, T.M.2    Garde, S.3
  • 69
    • 0035815522 scopus 로고    scopus 로고
    • Microcalorimetric studies of the interaction mechanisms between proteins and Q-Sepharose at pH near the isoelectric point (pI): Effects of NaCl concentration, pH value, and temperature
    • Lin, F.-Y.; Chen, C.-S.; Chen, W.-Y.; Yamamoto, S. Microcalorimetric studies of the interaction mechanisms between proteins and Q-Sepharose at pH near the isoelectric point (pI): Effects of NaCl concentration, pH value, and temperature J. Chromatogr. A 2001, 912 (2) 281-289
    • (2001) J. Chromatogr. A , vol.912 , Issue.2 , pp. 281-289
    • Lin, F.-Y.1    Chen, C.-S.2    Chen, W.-Y.3    Yamamoto, S.4
  • 70
    • 0035880579 scopus 로고    scopus 로고
    • Microcalorimetric studies on the interaction mechanism between proteins and hydrophobic solid surfaces in hydrophobic interaction chromatography: Effects of salts, hydrophobicity of the sorbent, and structure of the protein
    • Lin, F.-Y.; Chen, W.-Y.; Hearn, M. T. Microcalorimetric studies on the interaction mechanism between proteins and hydrophobic solid surfaces in hydrophobic interaction chromatography: effects of salts, hydrophobicity of the sorbent, and structure of the protein Anal. Chem. 2001, 73 (16) 3875-3883
    • (2001) Anal. Chem. , vol.73 , Issue.16 , pp. 3875-3883
    • Lin, F.-Y.1    Chen, W.-Y.2    Hearn, M.T.3
  • 71
    • 0034000234 scopus 로고    scopus 로고
    • Microcalorimetric studies of interactions between proteins and hydrophobic ligands in hydrophobic interaction chromatography: Effects of ligand chain length, density and the amount of bound protein
    • Lin, F. Y.; Chen, W. Y.; Ruaan, R. C.; Huang, H. M. Microcalorimetric studies of interactions between proteins and hydrophobic ligands in hydrophobic interaction chromatography: effects of ligand chain length, density and the amount of bound protein J. Chromatogr. A 2000, 872 (1-2) 37-47
    • (2000) J. Chromatogr. A , vol.872 , Issue.12 , pp. 37-47
    • Lin, F.Y.1    Chen, W.Y.2    Ruaan, R.C.3    Huang, H.M.4
  • 72
    • 0026548062 scopus 로고
    • Effects of stationary phase ligand density on high-performance ion-exchange chromatography of proteins
    • Wu, D.; Walters, R. R. Effects of stationary phase ligand density on high-performance ion-exchange chromatography of proteins J. Chromatogr. A 1992, 598 (1) 7-13
    • (1992) J. Chromatogr. A , vol.598 , Issue.1 , pp. 7-13
    • Wu, D.1    Walters, R.R.2
  • 73
    • 33645057678 scopus 로고    scopus 로고
    • Hexamer peptide affinity resins that bind the Fc region of human immunoglobulin G
    • Yang, H.; Gurgel, P. V.; Carbonell, R. G. Hexamer peptide affinity resins that bind the Fc region of human immunoglobulin G J. Pept. Res. 2005, 66, 120-137
    • (2005) J. Pept. Res. , vol.66 , pp. 120-137
    • Yang, H.1    Gurgel, P.V.2    Carbonell, R.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.