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Volumn 118, Issue 4, 2014, Pages 921-930

Electrostatic unfolding and interactions of albumin driven by pH changes: A molecular dynamics study

Author keywords

[No Author keywords available]

Indexed keywords

BIOCOMPATIBILITY; BIOLOGICAL MATERIALS; CONFORMATIONS; DENATURATION; ELECTROSTATICS; MOLECULAR DYNAMICS;

EID: 84893442580     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp409936v     Document Type: Article
Times cited : (148)

References (60)
  • 1
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of Novel Biomaterials through Molecular Self-Assembly
    • Zhang, S. G. Fabrication of Novel Biomaterials through Molecular Self-Assembly Nat. Biotechnol. 2003, 21 (10) 1171-1178
    • (2003) Nat. Biotechnol. , vol.21 , Issue.10 , pp. 1171-1178
    • Zhang, S.G.1
  • 2
    • 33745135423 scopus 로고    scopus 로고
    • Hydrogels in Biology and Medicine: From Molecular Principles to Bionanotechnology
    • Peppas, N. A.; Hilt, J. Z.; Khademhosseini, A.; Langer, R. Hydrogels in Biology and Medicine: From Molecular Principles to Bionanotechnology Adv. Mater. 2006, 18 (11) 1345-1360
    • (2006) Adv. Mater. , vol.18 , Issue.11 , pp. 1345-1360
    • Peppas, N.A.1    Hilt, J.Z.2    Khademhosseini, A.3    Langer, R.4
  • 4
    • 0028227096 scopus 로고
    • Structure of Serum-Albumin
    • Carter, D. C.; Ho, J. X. Structure of Serum-Albumin Adv. Protein Chem. 1994, 45, 153-203
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 6
    • 78650749876 scopus 로고    scopus 로고
    • Effects of pH on Aggregation Kinetics of the Repeat Domain of a Functional Amyloid, Pmel17
    • Pfefferkorn, C. M.; McGlinchey, R. P.; Lee, J. C. Effects of pH on Aggregation Kinetics of the Repeat Domain of a Functional Amyloid, Pmel17 Proc. Natl. Acad. Sci. U.S.A. 2010, 107 (50) 21447-21452
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , Issue.50 , pp. 21447-21452
    • Pfefferkorn, C.M.1    McGlinchey, R.P.2    Lee, J.C.3
  • 7
    • 84856094279 scopus 로고    scopus 로고
    • Amyloid Fibrillation in Native and Chemically-Modified Forms of Carbonic Anhydrase II: Role of Surface Hydrophobicity
    • Es-haghi, A.; Shariatizi, S.; Ebrahim-Habibi, A.; Nemat-Gorgani, M. Amyloid Fibrillation in Native and Chemically-Modified Forms of Carbonic Anhydrase II: Role of Surface Hydrophobicity Biochim. Biophys. Acta, Proteins Proteomics 2012, 1824 (3) 468-477
    • (2012) Biochim. Biophys. Acta, Proteins Proteomics , vol.1824 , Issue.3 , pp. 468-477
    • Es-Haghi, A.1    Shariatizi, S.2    Ebrahim-Habibi, A.3    Nemat-Gorgani, M.4
  • 10
    • 0016287438 scopus 로고
    • Coupling of Dyes to Biopolymers by Sensitized Photooxidation - Affinity Labeling of a Binding-Site in Bovine Serum-Albumin
    • Brandt, J.; Fredriks, M.; Andersson, L. O. Coupling of Dyes to Biopolymers by Sensitized Photooxidation-Affinity Labeling of a Binding-Site in Bovine Serum-Albumin Biochemistry 1974, 13 (23) 4758-4764
    • (1974) Biochemistry , vol.13 , Issue.23 , pp. 4758-4764
    • Brandt, J.1    Fredriks, M.2    Andersson, L.O.3
  • 11
    • 0037308418 scopus 로고    scopus 로고
    • Characterizing a Drug's Primary Binding Site on Albumin
    • Day, Y. S. N.; Myszka, D. G. Characterizing a Drug's Primary Binding Site on Albumin J. Pharm. Sci. 2003, 92 (2) 333-343
    • (2003) J. Pharm. Sci. , vol.92 , Issue.2 , pp. 333-343
    • Day, Y.S.N.1    Myszka, D.G.2
  • 12
    • 0025968147 scopus 로고
    • Locations of the 3 Primary Binding-Sites for Long-Chain Fatty-Acids on Bovine Serum-Albumin
    • Hamilton, J. A.; Era, S.; Bhamidipati, S. P.; Reed, R. G. Locations of the 3 Primary Binding-Sites for Long-Chain Fatty-Acids on Bovine Serum-Albumin Proc. Natl. Acad. Sci. U.S.A. 1991, 88 (6) 2051-2054
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , Issue.6 , pp. 2051-2054
    • Hamilton, J.A.1    Era, S.2    Bhamidipati, S.P.3    Reed, R.G.4
  • 13
    • 0035066321 scopus 로고    scopus 로고
    • Differential Binding of IgG and IgA Antibodies to Antigenic Determinants of Bovine Serum Albumin
    • Hilger, C.; Grigioni, F.; De Beaufort, C.; Michel, G.; Freilinger, J.; Hentges, F. Differential Binding of IgG and IgA Antibodies to Antigenic Determinants of Bovine Serum Albumin Clin. Exp. Immunol. 2001, 123 (3) 387-394
    • (2001) Clin. Exp. Immunol. , vol.123 , Issue.3 , pp. 387-394
    • Hilger, C.1    Grigioni, F.2    De Beaufort, C.3    Michel, G.4    Freilinger, J.5    Hentges, F.6
  • 16
    • 0030926737 scopus 로고    scopus 로고
    • Structural Transitions of Human Serum Albumin: An Investigation Using Electrophoretic Techniques
    • Gianazza, E.; Galliano, M.; Miller, I. Structural Transitions of Human Serum Albumin: An Investigation Using Electrophoretic Techniques Electrophoresis 1997, 18 (5) 695-700
    • (1997) Electrophoresis , vol.18 , Issue.5 , pp. 695-700
    • Gianazza, E.1    Galliano, M.2    Miller, I.3
  • 17
    • 0030979596 scopus 로고    scopus 로고
    • DSC Studies on Bovine Serum Albumin Denaturation - Effects of Ionic Strength and SDS Concentration
    • Giancola, C.; DeSena, C.; Fessas, D.; Graziano, G.; Barone, G. DSC Studies on Bovine Serum Albumin Denaturation-Effects of Ionic Strength and SDS Concentration Int. J. Biol. Macromol. 1997, 20 (3) 193-204
    • (1997) Int. J. Biol. Macromol. , vol.20 , Issue.3 , pp. 193-204
    • Giancola, C.1    Desena, C.2    Fessas, D.3    Graziano, G.4    Barone, G.5
  • 18
    • 0344444642 scopus 로고    scopus 로고
    • Impact of Glycerol on Thermostability and Heat-Induced Gelation of Bovine Serum Albumin
    • Baier, S. K.; Decker, E. A.; McClements, D. J. Impact of Glycerol on Thermostability and Heat-Induced Gelation of Bovine Serum Albumin Food Hydrocolloids 2004, 18 (1) 91-100
    • (2004) Food Hydrocolloids , vol.18 , Issue.1 , pp. 91-100
    • Baier, S.K.1    Decker, E.A.2    McClements, D.J.3
  • 19
    • 0348226844 scopus 로고    scopus 로고
    • Combined Influence of NaCl and Sucrose on Heat-Induced Gelation of Bovine Serum Albumin
    • Baier, S. K.; McClements, D. J. Combined Influence of NaCl and Sucrose on Heat-Induced Gelation of Bovine Serum Albumin J. Agric. Food Chem. 2003, 51 (27) 8107-8112
    • (2003) J. Agric. Food Chem. , vol.51 , Issue.27 , pp. 8107-8112
    • Baier, S.K.1    McClements, D.J.2
  • 20
    • 0035187378 scopus 로고    scopus 로고
    • Globular Protein Gelation - Theory and Experiment
    • Clark, A. H.; Kavanagh, G. M.; Ross-Murphy, S. B. Globular Protein Gelation-Theory and Experiment Food Hydrocolloids 2001, 15 (4-6) 383-400
    • (2001) Food Hydrocolloids , vol.15 , Issue.46 , pp. 383-400
    • Clark, A.H.1    Kavanagh, G.M.2    Ross-Murphy, S.B.3
  • 22
    • 0348236986 scopus 로고    scopus 로고
    • Effect of Copper, Iron, Zinc and Magnesium Ions on Bovine Serum Albumin Gelation
    • Haque, Z. Z.; Aryana, K. J. Effect of Copper, Iron, Zinc and Magnesium Ions on Bovine Serum Albumin Gelation Food Sci. Technol. Res. 2002, 8 (1) 1-3
    • (2002) Food Sci. Technol. Res. , vol.8 , Issue.1 , pp. 1-3
    • Haque, Z.Z.1    Aryana, K.J.2
  • 23
    • 0000523319 scopus 로고
    • Alpha-Lactalbumin Enhances the Gelation Properties of Bovine Serum-Albumin
    • Matsudomi, N.; Oshita, T.; Kobayashi, K.; Kinsella, J. E. Alpha-Lactalbumin Enhances the Gelation Properties of Bovine Serum-Albumin J. Agric. Food Chem. 1993, 41 (7) 1053-1057
    • (1993) J. Agric. Food Chem. , vol.41 , Issue.7 , pp. 1053-1057
    • Matsudomi, N.1    Oshita, T.2    Kobayashi, K.3    Kinsella, J.E.4
  • 24
    • 0026023953 scopus 로고
    • Gelation of Bovine Serum-Albumin and Beta-Lactoglobulin - Effects of pH, Salts and Thiol Reagents
    • Matsudomi, N.; Rector, D.; Kinsella, J. E. Gelation of Bovine Serum-Albumin and Beta-Lactoglobulin-Effects of pH, Salts and Thiol Reagents Food Chem. 1991, 40 (1) 55-69
    • (1991) Food Chem. , vol.40 , Issue.1 , pp. 55-69
    • Matsudomi, N.1    Rector, D.2    Kinsella, J.E.3
  • 26
    • 0026649396 scopus 로고
    • Gelation of Globular-Proteins - Effect of Ph and Ionic-Strength on the Critical Concentration for Gel Formation - A Simple-Model and Its Application to Beta-Lactoglobulin Heat-Induced Gelation
    • Renard, D.; Lefebvre, J. Gelation of Globular-Proteins-Effect of Ph and Ionic-Strength on the Critical Concentration for Gel Formation-a Simple-Model and Its Application to Beta-Lactoglobulin Heat-Induced Gelation Int. J. Biol. Macromol. 1992, 14 (5) 287-291
    • (1992) Int. J. Biol. Macromol. , vol.14 , Issue.5 , pp. 287-291
    • Renard, D.1    Lefebvre, J.2
  • 28
    • 84982017762 scopus 로고
    • Physical and Biochemical-Characterization of Albunex, a New Ultrasound Contrast Agent Consisting of Air-Filled Albumin Microspheres Suspended in a Solution of Human Albumin
    • Christiansen, C.; Kryvi, H.; Sontum, P. C.; Skotland, T. Physical and Biochemical-Characterization of Albunex, a New Ultrasound Contrast Agent Consisting of Air-Filled Albumin Microspheres Suspended in a Solution of Human Albumin Biotechnol. Appl. Biochem. 1994, 19, 307-320
    • (1994) Biotechnol. Appl. Biochem. , vol.19 , pp. 307-320
    • Christiansen, C.1    Kryvi, H.2    Sontum, P.C.3    Skotland, T.4
  • 29
    • 0028236545 scopus 로고
    • Lack of an Immune-Response to Albunex(R), a New Ultrasound Contrast Agent Based on Air-Filled Albumin Microspheres
    • Christiansen, C.; Vebner, A. J.; Muan, B.; Vik, H.; Haider, T.; Nicolaysen, H.; Skotland, T. Lack of an Immune-Response to Albunex(R), a New Ultrasound Contrast Agent Based on Air-Filled Albumin Microspheres Int. Arch. Allergy Imm 1994, 104 (4) 372-378
    • (1994) Int. Arch. Allergy Imm , vol.104 , Issue.4 , pp. 372-378
    • Christiansen, C.1    Vebner, A.J.2    Muan, B.3    Vik, H.4    Haider, T.5    Nicolaysen, H.6    Skotland, T.7
  • 30
    • 22144498118 scopus 로고    scopus 로고
    • Radical Cross-Linked Albumin Microspheres as Potential Drug Delivery Systems: Preparation and in Vitro Studies
    • Iemma, F.; Spizzirri, U. G.; Puoci, F.; Muzzalupo, R.; Trombino, S.; Picci, N. Radical Cross-Linked Albumin Microspheres as Potential Drug Delivery Systems: Preparation and in Vitro Studies Drug Delivery 2005, 12 (4) 229-234
    • (2005) Drug Delivery , vol.12 , Issue.4 , pp. 229-234
    • Iemma, F.1    Spizzirri, U.G.2    Puoci, F.3    Muzzalupo, R.4    Trombino, S.5    Picci, N.6
  • 31
    • 0025811220 scopus 로고
    • Localized Rifampicin Albumin Microspheres
    • Pande, S.; Vyas, S. P.; Dixit, V. K. Localized Rifampicin Albumin Microspheres J. Microencapsulation 1991, 8 (1) 87-93
    • (1991) J. Microencapsulation , vol.8 , Issue.1 , pp. 87-93
    • Pande, S.1    Vyas, S.P.2    Dixit, V.K.3
  • 32
    • 0027228389 scopus 로고
    • Albumin Microspheres as a Drug-Delivery System - Relation among Turbidity Ratio, Degree of Cross-Linking, and Drug-Release
    • Rubino, O. P.; Kowalsky, R.; Swarbrick, J. Albumin Microspheres as a Drug-Delivery System-Relation among Turbidity Ratio, Degree of Cross-Linking, and Drug-Release Pharm. Res. 1993, 10 (7) 1059-1065
    • (1993) Pharm. Res. , vol.10 , Issue.7 , pp. 1059-1065
    • Rubino, O.P.1    Kowalsky, R.2    Swarbrick, J.3
  • 33
    • 35348926358 scopus 로고    scopus 로고
    • Antitumor Effect of an Injectable in-Situ Forming Drug Delivery System Composed of a Novel Tissue Adhesive Containing Doxorubicin Hydrochloride
    • Kakinoki, S.; Taguchi, T. Antitumor Effect of an Injectable in-Situ Forming Drug Delivery System Composed of a Novel Tissue Adhesive Containing Doxorubicin Hydrochloride Eur. J. Pharm. Biopharm. 2007, 67 (3) 676-681
    • (2007) Eur. J. Pharm. Biopharm. , vol.67 , Issue.3 , pp. 676-681
    • Kakinoki, S.1    Taguchi, T.2
  • 34
    • 11244313250 scopus 로고    scopus 로고
    • Spherical Hydrophilic Microparticles Obtained by the Radical Copolymerisation of Functionalised Bovine Serum Albumin
    • Iemma, F.; Spizzirri, U.; Muzzalupo, R.; Puoci, F.; Trombino, S.; Picci, N. Spherical Hydrophilic Microparticles Obtained by the Radical Copolymerisation of Functionalised Bovine Serum Albumin Colloid Polym. Sci. 2004, 283 (3) 250-256
    • (2004) Colloid Polym. Sci. , vol.283 , Issue.3 , pp. 250-256
    • Iemma, F.1    Spizzirri, U.2    Muzzalupo, R.3    Puoci, F.4    Trombino, S.5    Picci, N.6
  • 36
    • 77449113345 scopus 로고    scopus 로고
    • Photopolymerizable Hydrogels Made from Polymer-Conjugated Albumin for Affinity-Based Drug Delivery
    • Oss-Ronen, L.; Seliktar, D. Photopolymerizable Hydrogels Made from Polymer-Conjugated Albumin for Affinity-Based Drug Delivery Adv. Biomater. 2010, 12 (1-2) 45-52
    • (2010) Adv. Biomater. , vol.12 , Issue.12 , pp. 45-52
    • Oss-Ronen, L.1    Seliktar, D.2
  • 37
    • 56349119329 scopus 로고    scopus 로고
    • About the Albumin Structure in Solution: Cigar Expanded Form versus Heart Normal Shape
    • Leggio, C.; Galantini, L.; Pavel, N. V. About the Albumin Structure in Solution: Cigar Expanded Form versus Heart Normal Shape Phys. Chem. Chem. Phys. 2008, 10 (45) 6741-6750
    • (2008) Phys. Chem. Chem. Phys. , vol.10 , Issue.45 , pp. 6741-6750
    • Leggio, C.1    Galantini, L.2    Pavel, N.V.3
  • 38
    • 0025046965 scopus 로고
    • Differential Scanning Calorimetric Studies on Bovine Serum-Albumin 0.1. Effects of pH and Ionic-Strength
    • Yamasaki, M.; Yano, H.; Aoki, K. Differential Scanning Calorimetric Studies on Bovine Serum-Albumin 0.1. Effects of pH and Ionic-Strength Int. J. Biol. Macromol. 1990, 12 (4) 263-268
    • (1990) Int. J. Biol. Macromol. , vol.12 , Issue.4 , pp. 263-268
    • Yamasaki, M.1    Yano, H.2    Aoki, K.3
  • 40
    • 0029633168 scopus 로고
    • Gromacs - A Message-Passing Parallel Molecular-Dynamics Implementation
    • Berendsen, H. J. C.; Vanderspoel, D.; Vandrunen, R. Gromacs-a Message-Passing Parallel Molecular-Dynamics Implementation Comput. Phys. Commun. 1995, 91 (1-3) 43-56
    • (1995) Comput. Phys. Commun. , vol.91 , Issue.13 , pp. 43-56
    • Berendsen, H.J.C.1    Vanderspoel, D.2    Vandrunen, R.3
  • 41
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess, B.; Kutzner, C.; van der Spoel, D.; Lindahl, E. GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, And Scalable Molecular Simulation J. Chem. Theory Comput. 2008, 4 (3) 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , Issue.3 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 42
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A Package for Molecular Simulation and Trajectory Analysis
    • Lindahl, E.; Hess, B.; Van Der Spoel, D. GROMACS 3.0: A Package for Molecular Simulation and Trajectory Analysis J. Mol. Model. 2001, 7 (8) 306-317
    • (2001) J. Mol. Model. , vol.7 , Issue.8 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 44
    • 79951681330 scopus 로고    scopus 로고
    • CpHModels-3.0. Remote homology Modeling Using Structure Guided Profile Sequence Alignment and Double-Sided Baseline Corrected Scoring Scheme
    • Nielsen, M.; Lundegaard, C.; Lund, O.; Petersen, T. N., CpHModels-3.0. Remote homology Modeling Using Structure Guided Profile Sequence Alignment and Double-Sided Baseline Corrected Scoring Scheme. Abstract at the CASP8 Conference 2008, 193.
    • (2008) Abstract at the CASP8 Conference , pp. 193
    • Nielsen, M.1    Lundegaard, C.2    Lund, O.3    Petersen, T.N.4
  • 45
    • 77954293798 scopus 로고    scopus 로고
    • CPHmodels-3.0 - Remote Homology Modeling Using Structure Guided Sequence Profiles
    • Nielsen, M.; Lundegaard, C.; Lund, O.; Petersen, T. N., CPHmodels-3.0-Remote Homology Modeling Using Structure Guided Sequence Profiles. Nucleic Acids Res. 2010, 38.
    • (2010) Nucleic Acids Res. , vol.38
    • Nielsen, M.1    Lundegaard, C.2    Lund, O.3    Petersen, T.N.4
  • 46
    • 84866661019 scopus 로고    scopus 로고
    • Structures of Bovine, Equine and Leporine Serum Albumin
    • Bujacz, A. Structures of Bovine, Equine and Leporine Serum Albumin Acta Crystallogr., Sect. D: Biol. Crystallogr. 2012, 68, 1278-1289
    • (2012) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.68 , pp. 1278-1289
    • Bujacz, A.1
  • 47
    • 0029912748 scopus 로고    scopus 로고
    • Development and Testing of the OPLS All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids
    • Jorgensen, W. L.; Maxwell, D. S.; TiradoRives, J. Development and Testing of the OPLS All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids J. Am. Chem. Soc. 1996, 118 (45) 11225-11236
    • (1996) J. Am. Chem. Soc. , vol.118 , Issue.45 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tiradorives, J.3
  • 48
    • 52349088763 scopus 로고    scopus 로고
    • FAMBE-pH: A Fast and Accurate Method to Compute the Total Solvation Free Energies of Proteins
    • Vorobjev, Y. N.; Vila, J. A.; Scheraga, H. A. FAMBE-pH: A Fast and Accurate Method to Compute the Total Solvation Free Energies of Proteins J. Phys. Chem. B 2008, 112 (35) 11122-11136
    • (2008) J. Phys. Chem. B , vol.112 , Issue.35 , pp. 11122-11136
    • Vorobjev, Y.N.1    Vila, J.A.2    Scheraga, H.A.3
  • 50
    • 3242887525 scopus 로고    scopus 로고
    • STRIDE: A Web Server for Secondary Structure Assignment from Known Atomic Coordinates of Proteins
    • Heinig, M.; Frishman, D. STRIDE: A Web Server for Secondary Structure Assignment from Known Atomic Coordinates of Proteins Nucleic Acids Res. 2004, 32, W500-W502
    • (2004) Nucleic Acids Res. , vol.32
    • Heinig, M.1    Frishman, D.2
  • 51
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of Nanosystems: Application to Microtubules and the Ribosome
    • Baker, N. A.; Sept, D.; Joseph, S.; Holst, M. J.; McCammon, J. A. Electrostatics of Nanosystems: Application to Microtubules and the Ribosome Proc. Natl. Acad. Sci. U.S.A. 2001, 98 (18) 10037-10041
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , Issue.18 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 54
    • 0033062612 scopus 로고    scopus 로고
    • Crystal Structure of Human Serum Albumin at 2.5 Angstrom Resolution
    • Sugio, S.; Kashima, A.; Mochizuki, S.; Noda, M.; Kobayashi, K. Crystal Structure of Human Serum Albumin at 2.5 Angstrom Resolution Protein Eng. 1999, 12 (6) 439-446
    • (1999) Protein Eng. , vol.12 , Issue.6 , pp. 439-446
    • Sugio, S.1    Kashima, A.2    Mochizuki, S.3    Noda, M.4    Kobayashi, K.5
  • 55
    • 80052811746 scopus 로고    scopus 로고
    • Advances in Implicit Models of Water Solvent to Compute Conformational Free Energy and Molecular Dynamics of Proteins at Constant pH
    • Vorobjev, Y. N. Advances in Implicit Models of Water Solvent to Compute Conformational Free Energy and Molecular Dynamics of Proteins at Constant pH Adv. Protein Chem. Struct. Biol. 2011, 85, 281-322
    • (2011) Adv. Protein Chem. Struct. Biol. , vol.85 , pp. 281-322
    • Vorobjev, Y.N.1
  • 56
    • 33846591083 scopus 로고    scopus 로고
    • Effective Charge of Bovine Serum Albumin Determined by Electrophoresis NMR
    • Bohme, U.; Scheler, U. Effective Charge of Bovine Serum Albumin Determined by Electrophoresis NMR Chem. Phys. Lett. 2007, 435, 342-345
    • (2007) Chem. Phys. Lett. , vol.435 , pp. 342-345
    • Bohme, U.1    Scheler, U.2
  • 57
    • 0345872684 scopus 로고
    • The Reversible Expansion of Bovine Serum Albumin in Acid Solutions
    • Tanford, C.; Buzzell, J. G.; Rands, D. G.; Swanson, S. A. The Reversible Expansion of Bovine Serum Albumin in Acid Solutions J. Am. Chem. Soc. 1955, 77 (24) 6421-6428
    • (1955) J. Am. Chem. Soc. , vol.77 , Issue.24 , pp. 6421-6428
    • Tanford, C.1    Buzzell, J.G.2    Rands, D.G.3    Swanson, S.A.4
  • 58
    • 0017409567 scopus 로고
    • Physical and Binding Properties of Large Fragments of Human-Serum Albumin
    • Geisow, M. J.; Beaven, G. H. Physical and Binding Properties of Large Fragments of Human-Serum Albumin Biochem. J. 1977, 163 (3) 477-484
    • (1977) Biochem. J. , vol.163 , Issue.3 , pp. 477-484
    • Geisow, M.J.1    Beaven, G.H.2
  • 59
    • 0022651532 scopus 로고
    • Direct Evidence for the Involvement of Domain-III in the N-F Transition of Bovine Serum-Albumin
    • Khan, M. Y. Direct Evidence for the Involvement of Domain-III in the N-F Transition of Bovine Serum-Albumin Biochem. J. 1986, 236 (1) 307-310
    • (1986) Biochem. J. , vol.236 , Issue.1 , pp. 307-310
    • Khan, M.Y.1
  • 60
    • 0028113997 scopus 로고
    • Reversed-Phase Chromatography of Synthetic Amphipathic Alpha-Helical Peptides as a Model for Ligand/Receptor Interactions Effect of Changing Hydrophobic Environment on the Relative Hydrophilicity/Hydrophobicity of Amino-Acid Side-Chains
    • Sereda, T. J.; Mant, C. T.; Sonnichsen, F. D.; Hodges, R. S. Reversed-Phase Chromatography of Synthetic Amphipathic Alpha-Helical Peptides as a Model for Ligand/Receptor Interactions Effect of Changing Hydrophobic Environment on the Relative Hydrophilicity/Hydrophobicity of Amino-Acid Side-Chains J. Chromatogr. A 1994, 676 (1) 139-153
    • (1994) J. Chromatogr. A , vol.676 , Issue.1 , pp. 139-153
    • Sereda, T.J.1    Mant, C.T.2    Sonnichsen, F.D.3    Hodges, R.S.4


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