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Volumn 24, Issue 19, 2012, Pages

Phase diagrams and kinetics of phase transitions in protein solutions

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL FUNCTIONS; CONDENSED PHASIS; CRYSTAL NUCLEI; FOLDED STATE; INDUSTRIAL PROCESSS; KINETICS OF NUCLEATION; KINETICS OF PHASE TRANSITIONS; LIQUID DROPLETS; LIQUID-LIQUID SEPARATION; MESOSCOPICS; NUCLEATION PROCESS; PATHOLOGICAL CONDITIONS; PHYSICAL PROCESS; PROTEIN CLUSTERS; PROTEIN CRYSTAL NUCLEATION; PROTEIN SOLUTION; SOLID AGGREGATES; SOLUTION THERMODYNAMICS; SPINODALS; TWO-STEP MECHANISMS;

EID: 84860171103     PISSN: 09538984     EISSN: 1361648X     Source Type: Journal    
DOI: 10.1088/0953-8984/24/19/193101     Document Type: Review
Times cited : (62)

References (148)
  • 3
    • 0031570336 scopus 로고    scopus 로고
    • Amyloid fibril formation and protein misassembly: A structural quest for insights into amyloid and priori diseases
    • Kelly J W 1997 Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases Structure 5 595600 (Pubitemid 27236259)
    • (1997) Structure , vol.5 , Issue.5 , pp. 595-600
    • Kelly, J.W.1
  • 5
    • 0014149925 scopus 로고
    • Pathogenesis of hemolytic anemia in homozygous hemoglobin C disease
    • 10.1172/JCI105670 0021-9738
    • Charache S, Conley C L, Waugh D F, Ugoretz R J and Spurrell J R 1967 Pathogenesis of hemolytic anemia in homozygous hemoglobin C disease J. Clin. Invest. 46 1795811
    • (1967) J. Clin. Invest. , vol.46 , Issue.11 , pp. 1795-1811
    • Charache, S.1    Conley, C.L.2    Waugh, D.F.3    Ugoretz, R.J.4    Spurrell, J.R.5
  • 6
    • 0021996069 scopus 로고
    • Ligand state of intraerythrocytic circulating HbC crystals in homozygote CC patients
    • Hirsch R E, Raventos-Suarez C, Olson J A and Nagel R L 1985 Ligand state of intraerythrocytic circulating HbC crystals in homozygote CC patients Blood 66 7757 (Pubitemid 15242457)
    • (1985) Blood , vol.66 , Issue.4 , pp. 775-777
    • Hirsch, R.E.1    Raventos-Suarez, C.2    Olson, J.A.3    Nagel, R.L.4
  • 8
    • 34848813177 scopus 로고    scopus 로고
    • Sickle-cell haemoglobin polymerization: Is it the primary pathogenic event of sickle-cell anaemia?
    • DOI 10.1111/j.1365-2141.2007.06794.x
    • Vekilov P 2007 Sickle-cell haemoglobin polymerisation: is it the primary pathogenic event of sickle-cell anaemia? Br. J. Haematol. 139 17384 (Pubitemid 47493095)
    • (2007) British Journal of Haematology , vol.139 , Issue.2 , pp. 173-184
    • Vekilov, P.G.1
  • 11
    • 0032054714 scopus 로고    scopus 로고
    • The role of assembly in insulin's biosynthesis
    • DOI 10.1016/S0959-440X(98)80037-7
    • Dodson G and Steiner D 1998 The role of assembly in insulins biosynthesis Curr. Opin. Struct. Biol. 8 18994 (Pubitemid 28221050)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.2 , pp. 189-194
    • Dodson, G.1    Steiner, D.2
  • 13
    • 0030565978 scopus 로고    scopus 로고
    • Protein crystal growth in microgravity review of large scale temperature induction method
    • 10.1016/0022-0248(96)00325-9 0022-0248
    • Long M L, Bishop J B, Nagabhushan T L, Reichert P, Smith G D and DeLucas L J 1996 Protein crystal growth in microgravity review of large scale temperature induction method J. Cryst. Growth 168 23343
    • (1996) J. Cryst. Growth , vol.168 , Issue.1-4 , pp. 233-243
    • Long, M.L.1    Bishop, J.B.2    Nagabhushan, T.L.3    Reichert, P.4    Smith, G.D.5    Delucas, L.J.6
  • 17
    • 27744516079 scopus 로고    scopus 로고
    • Insulin particle formation in supersaturated aqueous solutions of poly(ethylene glycol)
    • DOI 10.1529/biophysj.105.062802
    • Bromberg L, Rashba-Step J and Scott T 2005 Insulin particle formation in supersaturated aqueous solutions of poly(ethylene glycol) Biophys. J. 89 342433 (Pubitemid 41636097)
    • (2005) Biophysical Journal , vol.89 , Issue.5 , pp. 3424-3433
    • Bromberg, L.1    Rashba-Step, J.2    Scott, T.3
  • 20
    • 37549059193 scopus 로고    scopus 로고
    • What determines the rate of growth of crystals from solution?
    • 10.1021/cg070427i 1528-7483
    • Vekilov P G 2007 What determines the rate of growth of crystals from solution? Cryst. Growth Des. 7 2796810
    • (2007) Cryst. Growth Des. , vol.7 , Issue.12 , pp. 2796-2810
    • Vekilov, P.G.1
  • 21
    • 77958095167 scopus 로고    scopus 로고
    • Phase transitions of folded proteins
    • 10.1039/c0sm00215a 1744-683X
    • Vekilov P G 2010 Phase transitions of folded proteins Soft Matter 6 525472
    • (2010) Soft Matter , vol.6 , Issue.21 , pp. 5254-5272
    • Vekilov, P.G.1
  • 22
    • 38349042010 scopus 로고    scopus 로고
    • Protein phase behavior in aqueous solutions: Crystallization, liquidliquid phase separation, gels, and aggregates
    • 10.1529/biophysj.107.116152 0006-3495
    • Dumetz A C, Chockla A M, Kaler E W and Lenhoff A M 2008 Protein phase behavior in aqueous solutions: crystallization, liquidliquid phase separation, gels, and aggregates Biophys. J. 94 57083
    • (2008) Biophys. J. , vol.94 , Issue.2 , pp. 570-583
    • Dumetz, A.C.1    Chockla, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 24
    • 0035942984 scopus 로고    scopus 로고
    • Cloud-point temperatures for lysozyme in electrolyte solutions: Effect of salt type, salt concentration and pH
    • DOI 10.1016/S0301-4622(01)00173-9, PII S0301462201001739
    • Grigsby J J, Blanch H W and Prausnitz J M 2001 Cloud-point temperatures for lysozyme in electrolyte solutions: effect of salt type, salt concentration and pH Biophys. Chem. 91 23143 (Pubitemid 32707879)
    • (2001) Biophysical Chemistry , vol.91 , Issue.3 , pp. 231-243
    • Grigsby, J.J.1    Blanch, H.W.2    Prausnitz, J.M.3
  • 27
    • 24144467366 scopus 로고    scopus 로고
    • Light-scattering studies of protein solutions: Role of hydration in weak protein-protein interactions
    • DOI 10.1529/biophysj.105.065284
    • Paliwal A, Asthagiri D, Abras D, Lenhoff A M and Paulaitis M E 2005 Light-scattering studies of protein solutions: role of hydration in weak proteinprotein interactions Biophys. J. 89 156473 (Pubitemid 41233514)
    • (2005) Biophysical Journal , vol.89 , Issue.3 , pp. 1564-1573
    • Paliwal, A.1    Asthagiri, D.2    Abras, D.3    Lenhoff, A.M.4    Paulaitis, M.E.5
  • 28
    • 0030834854 scopus 로고    scopus 로고
    • Interactions of lysozyme in concentrated electrolyte solutions from dynamic light-scattering measurements
    • Kuehner D E, Heyer C, Ramsch C, Fornefeld U M, Blanch H W and Prausnitz J M 1997 Interactions of lysozyme in concentrated electrolyte solutions from dynamic light-scattering measurements Biophys. J. 73 321124 (Pubitemid 27525784)
    • (1997) Biophysical Journal , vol.73 , Issue.6 , pp. 3211-3224
    • Kuehner, D.E.1    Heyer, C.2    Ramsch, C.3    Fornefeld, U.M.4    Blanch, H.W.5    Prausnitz, J.M.6
  • 29
    • 33751000441 scopus 로고    scopus 로고
    • Searching for silver bullets: An alternative strategy for crystallizing macromolecules
    • DOI 10.1016/j.jsb.2006.09.006, PII S1047847706002899
    • McPherson A and Cudney B 2006 Searching for silver bullets: an alternative strategy for crystallizing macromolecules J. Struct. Biol. 156 387406 (Pubitemid 44751480)
    • (2006) Journal of Structural Biology , vol.156 , Issue.3 , pp. 387-406
    • McPherson, A.1    Cudney, B.2
  • 30
    • 34548427923 scopus 로고    scopus 로고
    • Patterns of protein-protein interactions in salt solutions and implications for protein crystallization
    • DOI 10.1110/ps.072957907
    • Dumetz A C, Snellinger-OBrien A M, Kaler E W and Lenhoff A M 2007 Patterns of proteinprotein interactions in salt solutions and implications for protein crystallization Protein Sci. 16 186777 (Pubitemid 47367109)
    • (2007) Protein Science , vol.16 , Issue.9 , pp. 1867-1877
    • Dumetz, A.C.1    Snellinger-O'Brien, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 31
    • 0031768735 scopus 로고    scopus 로고
    • Protein interactions in solution characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen
    • Velev O D, Kaler E W and Lenhoff A M 1998 Protein interactions in solution characterized by light and neutron scattering: comparison of lysozyme and chemotrypsinogen Biophys. J. 75 268297 (Pubitemid 28548940)
    • (1998) Biophysical Journal , vol.75 , Issue.6 , pp. 2682-2697
    • Velev, O.D.1    Kaler, E.W.2    Lenhoff, A.M.3
  • 32
    • 33646110105 scopus 로고    scopus 로고
    • The van der Waals interaction between protein molecules in an electrolyte solution
    • 10.1063/1.1634955 0021-9606
    • Song X Y and Zhao X F 2004 The van der Waals interaction between protein molecules in an electrolyte solution J. Chem. Phys. 120 20059
    • (2004) J. Chem. Phys. , vol.120 , Issue.4 , pp. 2005-2009
    • Song, X.Y.1    Zhao, X.F.2
  • 33
    • 0029540627 scopus 로고
    • Interaction in undersaturated and supersaturated lysozyme solutions: Static and dynamic light scattering results
    • 10.1063/1.469891 0021-9606
    • Muschol M and Rosenberger F 1995 Interaction in undersaturated and supersaturated lysozyme solutions: static and dynamic light scattering results J. Chem. Phys. 103 1042432
    • (1995) J. Chem. Phys. , vol.103 , Issue.24 , pp. 10424-10432
    • Muschol, M.1    Rosenberger, F.2
  • 34
    • 0030002671 scopus 로고    scopus 로고
    • Electrostatic proteinprotein interactions: Comparison of point-dipole and finite-length dipole potentials of mean force
    • 10.1006/jcis.1996.0031 0021-9797
    • Coen C J, Newman J, Blanch H W and Prausnitz J M 1996 Electrostatic proteinprotein interactions: comparison of point-dipole and finite-length dipole potentials of mean force J. Colloid Interface Sci. 177 2769
    • (1996) J. Colloid Interface Sci. , vol.177 , Issue.1 , pp. 276-279
    • Coen, C.J.1    Newman, J.2    Blanch, H.W.3    Prausnitz, J.M.4
  • 36
    • 0023430928 scopus 로고
    • Binary liquid phase separation and critical phenomena in a protein water solution
    • 10.1073/pnas.84.20.7079 0027-8424
    • Thomson J A, Schurtenberger P, Thurston G M and Benedek G B 1987 Binary liquid phase separation and critical phenomena in a protein water solution Proc. Natl Acad. Sci. USA 84 707983
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , Issue.20 , pp. 7079-7083
    • Thomson, J.A.1    Schurtenberger, P.2    Thurston, G.M.3    Benedek, G.B.4
  • 37
    • 8344242992 scopus 로고    scopus 로고
    • Smooth transition from metastability to instability in phase separating protein solutions
    • 10.1063/1.1792156 0021-9606
    • Shah M, Galkin O and Vekilov P G 2004 Smooth transition from metastability to instability in phase separating protein solutions J. Chem. Phys. 121 750512
    • (2004) J. Chem. Phys. , vol.121 , Issue.15 , pp. 7505-7512
    • Shah, M.1    Galkin, O.2    Vekilov, P.G.3
  • 38
    • 0031559476 scopus 로고    scopus 로고
    • Liquid-liquid phase separation in supersaturated lysozyme solutions and associated precipitate formation/crystallization
    • Muschol M and Rosenberger F 1997 Liquidliquid phase separation in supersaturated lysozyme solutions and associated precipitate formation/crystallization J. Chem. Phys. 107 195362 (Pubitemid 127568868)
    • (1997) Journal of Chemical Physics , vol.107 , Issue.6 , pp. 1953-1962
    • Muschol, M.1    Rosenberger, F.2
  • 40
    • 0344408851 scopus 로고    scopus 로고
    • Thermodynamic functions of concentrated protein solutions from phase equilibria
    • 10.1021/jp0278317 1520-6106 B
    • Petsev D N, Wu X, Galkin O and Vekilov P G 2003 Thermodynamic functions of concentrated protein solutions from phase equilibria J. Phys. Chem. B 107 39216
    • (2003) J. Phys. Chem. , vol.107 , Issue.16 , pp. 3921-3926
    • Petsev, D.N.1    Wu, X.2    Galkin, O.3    Vekilov, P.G.4
  • 42
    • 0033216548 scopus 로고    scopus 로고
    • The role of long range forces in the phase behavior of colloids and proteins
    • 10.1209/epl/i1999-00485-9 0295-5075 332
    • Noro M G, Kern N and Frenkel D 1999 The role of long range forces in the phase behavior of colloids and proteins Eurpophys. Lett. 48 3328
    • (1999) Eurpophys. Lett. , vol.48 , Issue.3 , pp. 332-338
    • Noro, M.G.1    Kern, N.2    Frenkel, D.3
  • 43
    • 0000854412 scopus 로고    scopus 로고
    • Phase behaviour of a simple model of globular proteins
    • 10.1063/1.479243 0021-9606
    • Sear R P 1999 Phase behaviour of a simple model of globular proteins J. Chem. Phys. 111 48006
    • (1999) J. Chem. Phys. , vol.111 , Issue.10 , pp. 4800-4806
    • Sear, R.P.1
  • 44
    • 0037263109 scopus 로고    scopus 로고
    • Ergodic and non-ergodic phase transitions in globular protein suspensions
    • Kulkarni A M, Dixit N M and Zukoski C F 2003 Ergodic and non-ergodic phase transitions in globular protein suspensions Faraday Discuss. 123 3750 (Pubitemid 38328303)
    • (2003) Faraday Discussions , vol.123 , pp. 37-50
    • Kulkarni, A.M.1    Dixit, N.M.2    Zukoski, C.F.3
  • 45
    • 3242889183 scopus 로고    scopus 로고
    • Effect of the range of attractive interactions on crystallization, metastable phase transition, and percolation in colloidal dispersions
    • 10.1103/PhysRevE.68.011403 1063-651X E 011403
    • Fu D, Li Y and Wu J 2003 Effect of the range of attractive interactions on crystallization, metastable phase transition, and percolation in colloidal dispersions Phys. Rev. E 68 011403
    • (2003) Phys. Rev. , vol.68 , Issue.1
    • Fu, D.1    Li, Y.2    Wu, J.3
  • 52
    • 1542375225 scopus 로고    scopus 로고
    • Liquid-Liquid Phase Separation in Hemoglobins: Distinct Aggregation Mechanisms of the β6 Mutants
    • Chen Q, Vekilov P G, Nagel R L and Hirsch R E 2004 Liquidliquid separation in hemoglobins: distinct aggregation mechanisms of the β6 mutants Biophys. J. 86 170212 (Pubitemid 38295605)
    • (2004) Biophysical Journal , vol.86 , Issue.3 , pp. 1702-1712
    • Chen, Q.1    Vekilov, P.G.2    Nagel, R.L.3    Hirsch, R.E.4
  • 53
    • 34547894189 scopus 로고    scopus 로고
    • Three frontiers in the thermodynamics of protein solutions
    • 10.1351/pac200779081435 0033-4545
    • Prausnitz J and Foose L 2007 Three frontiers in the thermodynamics of protein solutions Pure Appl. Chem. 79 143544
    • (2007) Pure Appl. Chem. , vol.79 , Issue.8 , pp. 1435-1444
    • Prausnitz, J.1    Foose, L.2
  • 54
    • 0024745871 scopus 로고
    • The price of lost freedom: Entropy of bimolecular complex formation
    • 10.1093/protein/3.1.1 1741-0126
    • Finkelstein A and Janin J 1989 The price of lost freedom: entropy of bimolecular complex formation Protein Eng. 3 110
    • (1989) Protein Eng. , vol.3 , Issue.1 , pp. 1-10
    • Finkelstein, A.1    Janin, J.2
  • 55
    • 0028360307 scopus 로고
    • The contribution of vibrational entropy to molecular association. The dimerization of insulin
    • DOI 10.1006/jmbi.1994.1300
    • Tidor B and Karplus M 1994 The contribution of vibrational entropy to molecular association. The dimerization of insulin J. Mol. Biol. 238 40514 (Pubitemid 24154720)
    • (1994) Journal of Molecular Biology , vol.238 , Issue.3 , pp. 405-414
    • Tidor, B.1    Karplus, M.2
  • 57
    • 0030214216 scopus 로고    scopus 로고
    • Enthalpy of crystallization of hen egg-white lysozyme
    • DOI 10.1016/0022-0248(96)00180-7, PII S0022024896001807
    • Schall C, Arnold E and Wiencek J M 1996 Enthalpy of crystallization of hen egg white lysozyme J. Cryst. Growth 165 293302 (Pubitemid 126360857)
    • (1996) Journal of Crystal Growth , vol.165 , Issue.3 , pp. 293-298
    • Schall, C.A.1    Arnold, E.2    Wiencek, J.M.3
  • 58
    • 0034634336 scopus 로고    scopus 로고
    • Molecular-level thermodynamic and kinetic parameters for the self-assembly of apoferritin molecules into crystals
    • 10.1006/jmbi.2000.4171 0022-2836
    • Yau S-T, Petsev D N, Thomas B R and Vekilov P G 2000 Molecular-level thermodynamic and kinetic parameters for the self-assembly of apoferritin molecules into crystals J. Mol. Biol. 303 66778
    • (2000) J. Mol. Biol. , vol.303 , Issue.5 , pp. 667-678
    • Yau, S.-T.1    Petsev, D.N.2    Thomas, B.R.3    Vekilov, P.G.4
  • 59
    • 0035501930 scopus 로고    scopus 로고
    • Temperature-independent solubility and interactions between apoferritin monomers and dimers in solution
    • DOI 10.1016/S0022-0248(01)01095-8, PII S0022024801010958
    • Petsev D N, Thomas B R, Yau S-T, Tsekova D, Nanev C, Wilson W W and Vekilov P G 2001 Temperature-independent solubility and interactions between apoferritin monomers and dimers in solution J. Cryst. Growth 232 219 (Pubitemid 32768302)
    • (2001) Journal of Crystal Growth , vol.232 , Issue.1-4 , pp. 21-29
    • Petsev, D.N.1    Thomas, B.R.2    Yau, S.-T.3    Tsekova, D.4    Nanev, C.5    William Wilson, W.6    Vekilov, P.G.7
  • 62
    • 8344281751 scopus 로고    scopus 로고
    • Monte Carlo study of phase separation in aqueous protein solutions
    • Lomakin A, Asherie N and Benedek G B 1996 Monte Carlo study of phase separation in aqueous protein solutions J. Chem. Phys. 104 164656 (Pubitemid 126747367)
    • (1996) Journal of Chemical Physics , vol.104 , Issue.4 , pp. 1646-1656
    • Lomakin, A.1    Asherie, N.2    Benedek, G.B.3
  • 65
    • 0345412741 scopus 로고    scopus 로고
    • Thermodynamics of the Hydrophobicity in Crystallization of Insulin
    • Bergeron L, Filobelo L, Galkin O and Vekilov P G 2003 Thermodynamics of the hydrophobicity in crystallization of insulin Biophys. J. 85 393542 (Pubitemid 37490302)
    • (2003) Biophysical Journal , vol.85 , Issue.6 , pp. 3935-3942
    • Bergeron, L.1    Filobelo, L.F.2    Galkin, O.3    Vekilov, P.G.4
  • 66
    • 0034082815 scopus 로고    scopus 로고
    • Interactions and aggregation of apoferritin molecules in solution: Effects of added electrolytes
    • Petsev D N, Thomas B R, Yau S-T and Vekilov P G 2000 Interactions and aggregation of apoferritin molecules in solution: effects of added electrolytes Biophys. J. 78 20609 (Pubitemid 30183600)
    • (2000) Biophysical Journal , vol.78 , Issue.4 , pp. 2060-2069
    • Petsev, D.N.1    Thomas, B.R.2    Yau, S.-T.3    Vekilov, P.G.4
  • 68
    • 0038446327 scopus 로고    scopus 로고
    • How to keep dry in water
    • DOI 10.1038/423025a
    • Ball P 2003 Chemical physics: how to keep dry in water Nature 423 256 (Pubitemid 36569570)
    • (2003) Nature , vol.423 , Issue.6935 , pp. 25-26
    • Ball, P.1
  • 69
    • 2342527858 scopus 로고    scopus 로고
    • Dynamics of water in biological recognition
    • 10.1021/cr020689l 0009-2665
    • Pal S K and Zewail A H 2004 Dynamics of water in biological recognition Chem. Rev. 104 2099124
    • (2004) Chem. Rev. , vol.104 , Issue.4 , pp. 2099-2124
    • Pal, S.K.1    Zewail, A.H.2
  • 70
    • 0344553294 scopus 로고    scopus 로고
    • Dynamics of water near a protein surface
    • 10.1021/jp030943t 1520-6106 B
    • Bhattacharyya S M, Wang Z-G and Zewail A H 2003 Dynamics of water near a protein surface J. Phys. Chem. B 107 1321828
    • (2003) J. Phys. Chem. , vol.107 , Issue.47 , pp. 13218-13228
    • Bhattacharyya, S.M.1    Wang, Z.-G.2    Zewail, A.H.3
  • 75
    • 0028228418 scopus 로고
    • The entropic cost of bound water in crystals and biomolecules
    • Dunitz J D 1994 The entropic cost of bound water in crystals and biomolecules Science 264 670 (Pubitemid 24186849)
    • (1994) Science , vol.264 , Issue.5159 , pp. 670
    • Dunitz, J.D.1
  • 76
    • 0000067621 scopus 로고
    • The growth of crystals and equilibrium structure of their surfaces
    • 10.1098/rsta.1951.0006 1364-503X A
    • Burton W K, Cabrera N and Frank F C 1951 The growth of crystals and equilibrium structure of their surfaces Phil. Trans. R. Soc. A 243 299360
    • (1951) Phil. Trans. R. Soc. , vol.243 , Issue.866 , pp. 299-360
    • Burton, W.K.1    Cabrera, N.2    Frank, F.C.3
  • 77
    • 11944255842 scopus 로고
    • Direct determination of site and kink energeis of vicinal Si(001)
    • 10.1103/PhysRevLett.65.1913 0031-9007
    • Swartzentruber B S, Mo Y-W, Kariotis R, Lagally M G and Webb M B 1990 Direct determination of site and kink energeis of vicinal Si(001) Phys. Rev. Lett. 65 19136
    • (1990) Phys. Rev. Lett. , vol.65 , Issue.15 , pp. 1913-1916
    • Swartzentruber, B.S.1    Mo, Y.-W.2    Kariotis, R.3    Lagally, M.G.4    Webb, M.B.5
  • 78
    • 0030258696 scopus 로고    scopus 로고
    • Step fluctuations on Pt(111) surfaces
    • DOI 10.1016/0039-6028(96)00823-0
    • Giesen M, Schulze Icking-Konert G, Stapel D and Ibach H 1996 Step fluctuations on Pt(111) surfaces Surf. Sci. 366 22938 (Pubitemid 126385589)
    • (1996) Surface Science , vol.366 , Issue.2 , pp. 229-238
    • Giesen, M.1    Icking-Konert, G.S.2    Stapel, D.3    Ibach, H.4
  • 79
    • 0000239702 scopus 로고
    • Step dynamics on Au(110) studied with a high-temperature, high-speed scanning tunneling microscope
    • 10.1103/PhysRevLett.71.3517 0031-9007
    • Kuipers L, Hoogeman M and Frenken J 1993 Step dynamics on Au(110) studied with a high-temperature, high-speed scanning tunneling microscope Phys. Rev. Lett. 71 351720
    • (1993) Phys. Rev. Lett. , vol.71 , Issue.21 , pp. 3517-3520
    • Kuipers, L.1    Hoogeman, M.2    Frenken, J.3
  • 81
    • 1842555070 scopus 로고    scopus 로고
    • Rational protein crystallization by mutational surface engineering
    • DOI 10.1016/j.str.2004.03.008, PII S0969212604000887
    • Derewenda Z 2004 Rational protein crystallization by mutational surface engineering Structure (Camb) 12 52935 (Pubitemid 38447156)
    • (2004) Structure , vol.12 , Issue.4 , pp. 529-535
    • Derewenda, Z.S.1
  • 82
    • 33644874674 scopus 로고    scopus 로고
    • Entropy and surface engineering in protein crystallization
    • 10.1107/S0907444905035237 0907-4449 D
    • Derewenda Z S and Vekilov P G 2006 Entropy and surface engineering in protein crystallization Acta Crystallogr. D 62 11624
    • (2006) Acta Crystallogr. , vol.62 , Issue.1 , pp. 116-124
    • Derewenda, Z.S.1    Vekilov, P.G.2
  • 85
    • 4344698577 scopus 로고    scopus 로고
    • The use of recombinant methods and molecular engineering in protein crystallization
    • DOI 10.1016/j.ymeth.2004.03.024, PII S1046202304001173
    • Derewenda Z 2004 The use of recombinant methods and molecular engineering in protein crystallization Methods 34 35463 (Pubitemid 39119819)
    • (2004) Methods , vol.34 , Issue.3 , pp. 354-363
    • Derewenda, Z.S.1
  • 86
    • 0024036988 scopus 로고
    • Systematic studies on the crystallization of lysozyme. Determination and use of phase diagrams
    • 10.1016/0022-0248(88)90302-8 0022-0248
    • Ataka M and Asai M 1988 Systematic studies on the crystallization of lysozyme. Determination and use of phase diagrams J. Cryst. Growth 90 8693
    • (1988) J. Cryst. Growth , vol.90 , Issue.1-3 , pp. 86-93
    • Ataka, M.1    Asai, M.2
  • 87
    • 0024035827 scopus 로고
    • The solubility of hen-egg-white lysozyme
    • 10.1016/0022-0248(88)90303-X 0022-0248
    • Howard S B, Twigg P J, Baird J K and Meehan E J 1988 The solubility of hen-egg-white lysozyme J. Cryst. Growth 90 94104
    • (1988) J. Cryst. Growth , vol.90 , Issue.1-3 , pp. 94-104
    • Howard, S.B.1    Twigg, P.J.2    Baird, J.K.3    Meehan, E.J.4
  • 93
    • 36849108755 scopus 로고
    • On the statistical mechanics of nucleation theory
    • 10.1063/1.1727620 0021-9606
    • Lothe J and Pound G M 1966 On the statistical mechanics of nucleation theory J. Chem. Phys. 45 6304
    • (1966) J. Chem. Phys. , vol.45 , Issue.2 , pp. 630-634
    • Lothe, J.1    Pound, G.M.2
  • 94
  • 95
    • 0033513864 scopus 로고    scopus 로고
    • In situ atomic force microscopy studies of surface morphology, growth kinetics, defect structure and dissolution in macromolecular crystallization
    • 10.1016/S0022-0248(98)00823-9 0022-0248
    • Malkin A J, Kuznetsov Y G and McPherson A 1999 In situ atomic force microscopy studies of surface morphology, growth kinetics, defect structure and dissolution in macromolecular crystallization J. Cryst. Growth 196 47188
    • (1999) J. Cryst. Growth , vol.196 , Issue.2-4 , pp. 471-488
    • Malkin, A.J.1    Kuznetsov, Y.G.2    McPherson, A.3
  • 96
    • 0000015259 scopus 로고    scopus 로고
    • Effects of convective solute and impurity transport in protein crystal growth
    • Vekilov P G, Thomas B R and Rosenberger F 1998 Effects of convective solute and impurity transport on protein crystal growth J. Phys. Chem. B 102 520816 (Pubitemid 128576748)
    • (1998) Journal of Physical Chemistry B , vol.102 , Issue.26 , pp. 5208-5216
    • Vekilov, P.G.1    Thomas, B.R.2    Rosenberger, F.3
  • 97
    • 0003056570 scopus 로고
    • Theory of new phase formation: Cavitation
    • Zeldovich Y B 1943 Theory of new phase formation: cavitation Acta Physicochim. URSS 18 122
    • (1943) Acta Physicochim. URSS , vol.18 , pp. 1-22
    • Zeldovich, Y.B.1
  • 100
    • 0034639421 scopus 로고    scopus 로고
    • Are nucleation kinetics of protein crystals similar to those of liquid droplets?
    • DOI 10.1021/ja9930869
    • Galkin O and Vekilov P G 2000 Are nucleation kinetics of protein crystals similar to those of liquid droplets? J. Am. Chem. Soc. 122 15663 (Pubitemid 30054100)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.1 , pp. 156-163
    • Galkin, O.1    Vekilov, P.G.2
  • 101
    • 0000063775 scopus 로고
    • On the equilibrium of heterogeneous substances
    • Gibbs J W 1876 On the equilibrium of heterogeneous substances Trans. Connect. Acad. Sci. 3 108248
    • (1876) Trans. Connect. Acad. Sci. , vol.3 , pp. 108-248
    • Gibbs, J.W.1
  • 102
    • 0000063775 scopus 로고
    • On the equilibrium of heterogeneous substances
    • Gibbs J W 1878 On the equilibrium of heterogeneous substances Trans. Connect. Acad. Sci. 16 343524
    • (1878) Trans. Connect. Acad. Sci. , vol.16 , pp. 343-524
    • Gibbs, J.W.1
  • 103
    • 35949034972 scopus 로고
    • Theory of dynamic critical phenomena
    • 10.1103/RevModPhys.49.435 0034-6861
    • Hohenberg P C and Halperin B I 1977 Theory of dynamic critical phenomena Rev. Mod. Phys. 49 43579
    • (1977) Rev. Mod. Phys. , vol.49 , Issue.3 , pp. 435-479
    • Hohenberg, P.C.1    Halperin, B.I.2
  • 105
    • 33746012315 scopus 로고
    • Free energy of a nonuniform system. I. Interfacial free energy
    • 10.1063/1.1744102 0021-9606
    • Cahn J W and Hilliard J E 1958 Free energy of a nonuniform system. I. Interfacial free energy J. Chem. Phys. 28 25867
    • (1958) J. Chem. Phys. , vol.28 , Issue.2 , pp. 258-267
    • Cahn, J.W.1    Hilliard, J.E.2
  • 106
    • 0000828166 scopus 로고
    • Kinetics of nucleation in near-critical fluids
    • 10.1103/PhysRevA.21.948 0556-2791 A
    • Langer J S and Schwartz A J 1980 Kinetics of nucleation in near-critical fluids Phys. Rev. A 21 94858
    • (1980) Phys. Rev. , vol.21 , Issue.3 , pp. 948-958
    • Langer, J.S.1    Schwartz, A.J.2
  • 107
    • 0028483006 scopus 로고
    • Density, thermal expansivity, viscosity and refractive index of lysozyme solutions at crystal growth concentrations
    • 10.1016/0022-0248(94)90111-2 0022-0248
    • Fredericks W J, Hammonds M C, Howard S B and Rosenberger F 1994 Density, thermal expansivity, viscosity and refractive index of lysozyme solutions at crystal growth concentrations J. Cryst. Growth 141 18392
    • (1994) J. Cryst. Growth , vol.141 , Issue.1-2 , pp. 183-192
    • Fredericks, W.J.1    Hammonds, M.C.2    Howard, S.B.3    Rosenberger, F.4
  • 108
    • 41349092701 scopus 로고    scopus 로고
    • Evidence for the surface-diffusion mechanism of solution crystallization from molecular-level observations with ferritin
    • DOI 10.1103/PhysRevE.66.021606, 021606
    • Chen K and Vekilov P G 2002 Evidence for the surface diffusion mechanism of solution crystallization from molecular-level observations with ferritin Phys. Rev. E 66 021606 (Pubitemid 40618659)
    • (2002) Physical Review E - Statistical, Nonlinear, and Soft Matter Physics , vol.66 , Issue.2
    • Chen, K.1    Vekilov, P.G.2
  • 111
    • 0000540719 scopus 로고    scopus 로고
    • Direct determination of the nucleation rate of protein crystals
    • 10.1021/jp992786x 1520-6106
    • Galkin O and Vekilov P G 1999 Direct determination of the nucleation rate of protein crystals J. Phys. Chem. 103 1096571
    • (1999) J. Phys. Chem. , vol.103 , Issue.49 , pp. 10965-10971
    • Galkin, O.1    Vekilov, P.G.2
  • 112
    • 0037470883 scopus 로고    scopus 로고
    • On the methods of determination of homogeneous nucleation rates of protein crystals
    • DOI 10.1016/S0927-7757(02)00423-5, PII S0927775702004235
    • Vekilov P G and Galkin O 2003 On the methods of determination of homogeneous nucleation rates of protein crystals Colloids Surf. A 215 12530 (Pubitemid 36344046)
    • (2003) Colloids and Surfaces A: Physicochemical and Engineering Aspects , vol.215 , Issue.1-3 , pp. 125-130
    • Vekilov, P.G.1    Galkin, O.2
  • 113
    • 22844433290 scopus 로고    scopus 로고
    • Spinodal for the solution-to-crystal phase transformation
    • DOI 10.1063/1.1943413, 014904
    • Filobelo L F, Galkin O and Vekilov P G 2005 Spinodal for the solution-to-crystal phase transformation J. Chem. Phys. 123 014904 (Pubitemid 41037078)
    • (2005) Journal of Chemical Physics , vol.123 , Issue.1 , pp. 1-7
    • Filobelo, L.F.1    Galkin, O.2    Vekilov, P.G.3
  • 114
    • 0347308440 scopus 로고    scopus 로고
    • Measurement and modeling of protein crystal nucleation kinetics
    • 10.1021/cg025504i 1528-7483
    • Bhamidi V, Varanasi S and Schall C A 2002 Measurement and modeling of protein crystal nucleation kinetics Cryst. Growth Des. 2 395400
    • (2002) Cryst. Growth Des. , vol.2 , Issue.5 , pp. 395-400
    • Bhamidi, V.1    Varanasi, S.2    Schall, C.A.3
  • 115
    • 0001782795 scopus 로고    scopus 로고
    • Nucleation of First-Order Phase Transitions
    • Oxtoby D W 1998 Nucleation of first order phase transitions Acc. Chem. Res. 31 917 (Pubitemid 128474581)
    • (1998) Accounts of Chemical Research , vol.31 , Issue.2 , pp. 91-97
    • Oxtoby, D.W.1
  • 116
    • 0013306867 scopus 로고
    • Homogeneous nucleation: Theory and experiment
    • 10.1088/0953-8984/4/38/001 0953-8984
    • Oxtoby D W 1992 Homogeneous nucleation: theory and experiment J. Phys.: Condens. Matter 4 762750
    • (1992) J. Phys.: Condens. Matter , vol.4 , Issue.38 , pp. 7627-7650
    • Oxtoby, D.W.1
  • 117
    • 0001511066 scopus 로고
    • A general relation between the nucleation work and the size of the nucleus in multicomponent nucleation
    • 10.1063/1.466859 0021-9606
    • Oxtoby D W and Kashchiev D 1994 A general relation between the nucleation work and the size of the nucleus in multicomponent nucleation J. Chem. Phys. 100 766571
    • (1994) J. Chem. Phys. , vol.100 , Issue.10 , pp. 7665-7671
    • Oxtoby, D.W.1    Kashchiev, D.2
  • 118
    • 36749114484 scopus 로고
    • On the relation between nucleation work, nucleus size, and nucleation rate
    • 10.1063/1.442808 0021-9606
    • Kashchiev D 1982 On the relation between nucleation work, nucleus size, and nucleation rate J. Chem. Phys. 76 5098102
    • (1982) J. Chem. Phys. , vol.76 , Issue.10 , pp. 5098-5102
    • Kashchiev, D.1
  • 121
    • 84860149303 scopus 로고    scopus 로고
    • Kinetics of phase transition in protein solutions on microscopic and mesoscopic length scales
    • Filobelo L 2005 Kinetics of phase transition in protein solutions on microscopic and mesoscopic length scales Chemical and Biomolecular Engineering (Houston: University of Houston) p 174
    • (2005) Chemical and Biomolecular Engineering , pp. 174
    • Filobelo, L.1
  • 122
    • 18744399040 scopus 로고    scopus 로고
    • Nucleation of ordered solid phases of proteins via a disordered high-density state: Phenomenological approach
    • DOI 10.1063/1.1887168, 174905
    • Pan W, Kolomeisky A B and Vekilov P G 2005 Nucleation of ordered solid phases of protein via a disordered high-density state: phenomenological approach J. Chem. Phys. 122 174905 (Pubitemid 40666002)
    • (2005) Journal of Chemical Physics , vol.122 , Issue.17 , pp. 1-7
    • Pan, W.1    Kolomeisky, A.B.2    Vekilov, P.G.3
  • 123
    • 4143146536 scopus 로고    scopus 로고
    • Dense liquid precursor for the nucleation of ordered solid phases from solution
    • DOI 10.1021/cg049977w
    • Vekilov P G 2004 Dense liquid precursor for the nucleation of ordered solid phases from solution Cryst. Growth Des. 4 67185 (Pubitemid 39091291)
    • (2004) Crystal Growth and Design , vol.4 , Issue.4 , pp. 671-685
    • Vekilov, P.G.1
  • 124
    • 0001052492 scopus 로고    scopus 로고
    • Crystal nucleation in the presence of a metastable critical point
    • DOI 10.1063/1.476554, PII S0021960698513256
    • Talanquer V and Oxtoby D W 1998 Crystal nucleation in the presence of a metastable critical point J. Chem. Phys. 109 2237 (Pubitemid 128678819)
    • (1998) Journal of Chemical Physics , vol.109 , Issue.1 , pp. 223-227
    • Talanquer, V.1    Oxtoby, D.W.2
  • 125
    • 4243965364 scopus 로고    scopus 로고
    • Coil-globule transition in gas-liquid nucleation of polar fluids
    • ten Wolde P R, Oxtoby D W and Frenkel D 1998 Coil-globule transition in gasliquid nucleation of polar fluids Phys. Rev. Lett. 81 36958 (Pubitemid 128629592)
    • (1998) Physical Review Letters , vol.81 , Issue.17 , pp. 3695-3698
    • Ten Wolde, P.R.1    Oxtoby, D.W.2    Frenkel, D.3
  • 128
    • 33846016196 scopus 로고    scopus 로고
    • Metastable mesoscopic clusters in solutions of sickle-cell hemoglobin
    • DOI 10.1529/biophysj.106.094854
    • Pan W, Galkin O, Filobelo L, Nagel R L and Vekilov P G 2007 Metastable mesoscopic clusters in solutions of sickle cell hemoglobin Biophys. J. 92 26777 (Pubitemid 46048434)
    • (2007) Biophysical Journal , vol.92 , Issue.1 , pp. 267-277
    • Pan, W.1    Galkin, O.2    Filobelo, L.3    Nagel, R.L.4    Vekilov, P.G.5
  • 130
    • 33846016337 scopus 로고
    • Excess scattered-light intensity fluctuations from hemoglobin
    • 10.1103/PhysRevLett.32.37 0031-9007
    • Uzgiris E E and Golibersuch D C 1974 Excess scattered-light intensity fluctuations from hemoglobin Phys. Rev. Lett. 32 3740
    • (1974) Phys. Rev. Lett. , vol.32 , Issue.2 , pp. 37-40
    • Uzgiris, E.E.1    Golibersuch, D.C.2
  • 131
    • 19244365097 scopus 로고    scopus 로고
    • Equilibrium cluster phases and low-density arrested disordered states: The role of short-range attraction and long-range repulsion
    • 10.1103/PhysRevLett.93.055701 0031-9007 055701
    • Sciortino F, Mossa S, Zaccarelli E and Tartaglia P 2004 Equilibrium cluster phases and low-density arrested disordered states: the role of short-range attraction and long-range repulsion Phys. Rev. Lett. 93 055701
    • (2004) Phys. Rev. Lett. , vol.93 , Issue.5
    • Sciortino, F.1    Mossa, S.2    Zaccarelli, E.3    Tartaglia, P.4
  • 132
    • 0035969723 scopus 로고    scopus 로고
    • Anomalously large equilibrium clusters of colloids
    • DOI 10.1021/jp011646w
    • Groenewold J and Kegel W K 2001 Anomalously large equilibrium clusters of colloids J. Phys. Chem. B 105 117029 (Pubitemid 35338403)
    • (2001) Journal of Physical Chemistry B , vol.105 , Issue.47 , pp. 11702-11709
    • Groenewold, J.1    Kegel, W.K.2
  • 133
    • 23044513923 scopus 로고    scopus 로고
    • Cluster formation in two-Yukawa fluids
    • DOI 10.1063/1.1830433, 044507
    • Liu Y, Chen W-R and Chen S-H 2005 Cluster formation in two-Yukawa fluids J. Chem. Phys. 122 044507 (Pubitemid 41055355)
    • (2005) Journal of Chemical Physics , vol.122 , Issue.4 , pp. 1-13
    • Liu, Y.1    Chen, W.-R.2    Chen, S.-H.3
  • 134
    • 10044228437 scopus 로고    scopus 로고
    • Ground-state clusters for short-range attractive and long-range repulsive potentials
    • 10.1021/la048554t 0743-7463
    • Mossa S, Sciortino F, Tartaglia P and Zaccarelli E 2004 Ground-state clusters for short-range attractive and long-range repulsive potentials Langmuir 20 1075663
    • (2004) Langmuir , vol.20 , Issue.24 , pp. 10756-10763
    • Mossa, S.1    Sciortino, F.2    Tartaglia, P.3    Zaccarelli, E.4
  • 135
    • 9644259209 scopus 로고    scopus 로고
    • Equilibrium cluster formation in concentrated protein solutions and colloids
    • DOI 10.1038/nature03109
    • Stradner A, Sedgwick H, Cardinaux F, Poon W C K, Egelhaaf S U and Schurtenberger P 2004 Equilibrium cluster formation in concentrated protein solutions and colloids Nature 432 4925 (Pubitemid 39576527)
    • (2004) Nature , vol.432 , Issue.7016 , pp. 492-495
    • Stradner, A.1    Sedgwick, H.2    Cardinaux, F.3    Poon, W.C.K.4    Egelhaaf, S.U.5    Schurtenberger, P.6
  • 136
    • 77953148643 scopus 로고    scopus 로고
    • The origin of anomalous mesoscopic phases in protein solutions
    • 10.1021/jp100617w 1520-6106 B
    • Pan W, Vekilov P G and Lubchenko V 2010 The origin of anomalous mesoscopic phases in protein solutions J. Phys. Chem. B 114 762030
    • (2010) J. Phys. Chem. , vol.114 , Issue.22 , pp. 7620-7630
    • Pan, W.1    Vekilov, P.G.2    Lubchenko, V.3
  • 137
    • 0030806177 scopus 로고    scopus 로고
    • Enhancement of protein crystal nucleation by critical density fluctuations
    • DOI 10.1126/science.277.5334.1975
    • ten Wolde P R and Frenkel D 1997 Enhancement of protein crystal nucleation by critical density fluctuations Science 277 19758 (Pubitemid 27449135)
    • (1997) Science , vol.277 , Issue.5334 , pp. 1975-1978
    • Ten Wolde, P.R.1    Frenkel, D.2
  • 138
    • 0037961013 scopus 로고    scopus 로고
    • Metastable states and the kinetics of colloid phase separation
    • Soga K G, Melrose J M and Ball R C 1999 Metastable states and the kinetics of colloid phase separation J. Chem. Phys. 110 22808 (Pubitemid 129615076)
    • (1999) Journal of Chemical Physics , vol.110 , Issue.4 , pp. 2280-2288
    • Soga, K.G.1    Melrose, J.R.2    Ball, R.C.3
  • 139
    • 0037153184 scopus 로고    scopus 로고
    • Materials chemistry: Crystals in a flash
    • DOI 10.1038/420277a
    • Oxtoby D W 2002 Crystals in a flash Nature 420 2778 (Pubitemid 35398171)
    • (2002) Nature , vol.420 , Issue.6913 , pp. 277-278
    • Oxtoby, D.W.1
  • 140
    • 0037171856 scopus 로고    scopus 로고
    • Insights into phase transition kinetics from colloid science
    • DOI 10.1038/416811a
    • Anderson V J and Lekkerkerker H N W 2002 Insights into phase transition kinetics from colloid science Nature 416 8115 (Pubitemid 34453731)
    • (2002) Nature , vol.416 , Issue.6883 , pp. 811-815
    • Anderson, V.J.1    Lekkerkerker, H.N.W.2
  • 141
    • 18144382316 scopus 로고    scopus 로고
    • Strong dc electric field applied to supersaturated aqueous glycine solution induces nucleation of the γ polymorph
    • DOI 10.1103/PhysRevLett.94.145503, 145503
    • Aber J E, Arnold S and Garetz B A 2005 Strong dc electric field applied to supersaturated aqueous glycine solution induces nucleation of the polymorph Phys. Rev. Lett. 94 145503 (Pubitemid 40620424)
    • (2005) Physical Review Letters , vol.94 , Issue.14 , pp. 1-4
    • Aber, J.E.1    Arnold, S.2    Garetz, B.A.3    Myerson, A.S.4
  • 142
    • 4243283850 scopus 로고    scopus 로고
    • Polarization switching of crystal structure in the nonphotochemical light-induced nucleation of supersaturated aqueous glycine solutions
    • 10.1103/PhysRevLett.89.175501 0031-9007 175501
    • Garetz B, Matic J and Myerson A 2002 Polarization switching of crystal structure in the nonphotochemical light-induced nucleation of supersaturated aqueous glycine solutions Phys. Rev. Lett. 89 175501
    • (2002) Phys. Rev. Lett. , vol.89 , Issue.17
    • Garetz, B.1    Matic, J.2    Myerson, A.3
  • 143
    • 3042630018 scopus 로고    scopus 로고
    • The effect of seed preparation on the chirality of the secondary nuclei
    • DOI 10.1016/j.ces.2004.04.014, PII S0009250904002374
    • Qian R Y and Botsaris G D 2004 The effect of seed preparation on the chirality of the secondary nuclei Chem. Eng. Sci. 59 284152 (Pubitemid 38814598)
    • (2004) Chemical Engineering Science , vol.59 , Issue.14 , pp. 2841-2852
    • Qian, R.-Y.1    Botsaris, G.D.2
  • 144
    • 0035502093 scopus 로고    scopus 로고
    • The liquid protein phase in crystallization: A case study - Intact immunoglobulins
    • DOI 10.1016/S0022-0248(01)01058-2, PII S0022024801010582
    • Kuznetsov Y G, Malkin A J and McPherson A 2001 The liquid protein phase in crystallization: a case study intact immunoglobins J. Cryst. Growth 232 309 (Pubitemid 32768303)
    • (2001) Journal of Crystal Growth , vol.232 , Issue.1-4 , pp. 30-39
    • Kuznetsov, Y.G.1    Malkin, A.J.2    McPherson, A.3
  • 146
    • 34547700385 scopus 로고    scopus 로고
    • Two-step mechanism of homogeneous nucleation of sickle cell hemoglobin polymers
    • DOI 10.1529/biophysj.106.103705
    • Galkin O, Pan W, Filobelo L, Hirsch R E, Nagel R L and Vekilov P G 2007 Two-step mechanism of homogeneous nucleation of sickle cell hemoglobin polymers Biophys. J. 93 90213 (Pubitemid 47219782)
    • (2007) Biophysical Journal , vol.93 , Issue.3 , pp. 902-913
    • Galkin, O.1    Pan, W.2    Filobelo, L.3    Hirsch, R.E.4    Nagel, R.L.5    Vekilov, P.G.6
  • 147
    • 0026260016 scopus 로고
    • The solubility of the tetragonal form of hen egg white lysozyme from pH 4.0 to 5.4
    • 10.1016/0022-0248(91)90043-5 0022-0248
    • Cacioppo E and Pusey M L 1991 The solubility of the tetragonal form of hen egg white lysozyme from pH 4.0 to 5.4. J. Cryst. Growth 114 28692
    • (1991) J. Cryst. Growth , vol.114 , Issue.3 , pp. 286-292
    • Cacioppo, E.1    Pusey, M.L.2
  • 148
    • 0002268479 scopus 로고
    • Preliminary x-ray data for some new crystalline forms of - Lactoglobulin and hen-egg-white lysozyme
    • 10.1107/S0365110X59000238 0365-110X B
    • Steinrauf L K 1959 Preliminary x-ray data for some new crystalline forms of - lactoglobulin and hen-egg-white lysozyme Acta Crystallogr. B 12 779
    • (1959) Acta Crystallogr. , vol.12 , Issue.1 , pp. 77-79
    • Steinrauf, L.K.1


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