메뉴 건너뛰기




Volumn 32, Issue 10, 2016, Pages 2492-2499

Freeze-Thaw Cycling Induced Isotropic-Nematic Coexistence of Amyloid Fibrils Suspensions

Author keywords

[No Author keywords available]

Indexed keywords

ASPECT RATIO; CRYSTAL STRUCTURE; FREEZING; GLYCOPROTEINS; LIQUIDS; METASTABLE PHASES; SUSPENSIONS (FLUIDS); THAWING;

EID: 84961221268     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/acs.langmuir.6b00276     Document Type: Article
Times cited : (22)

References (49)
  • 1
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C. A.; Poirier, M. A. Protein aggregation and neurodegenerative disease Nat. Med. 2004, 10 (7) S10-S17 10.1038/nm1066
    • (2004) Nat. Med. , vol.10 , Issue.7 , pp. S10-S17
    • Ross, C.A.1    Poirier, M.A.2
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F.; Dobson, C. M. Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 2006, 75, 333-366 10.1146/annurev.biochem.75.101304.123901
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 36048941372 scopus 로고    scopus 로고
    • Peptide fibrillization
    • Hamley, I. W. Peptide fibrillization Angew. Chem., Int. Ed. 2007, 46 (43) 8128-8147 10.1002/anie.200700861
    • (2007) Angew. Chem., Int. Ed. , vol.46 , Issue.43 , pp. 8128-8147
    • Hamley, I.W.1
  • 5
    • 1242310516 scopus 로고    scopus 로고
    • Mesoscopic properties of semiflexible amyloid fibrils
    • Sagis, L. M. C.; Veerman, C.; van der Linden, E. Mesoscopic properties of semiflexible amyloid fibrils Langmuir 2004, 20 (3) 924-927 10.1021/la035390s
    • (2004) Langmuir , vol.20 , Issue.3 , pp. 924-927
    • Sagis, L.M.C.1    Veerman, C.2    Van Der Linden, E.3
  • 6
    • 34047234694 scopus 로고    scopus 로고
    • Formation of amyloid-like fibrils by ovalbumin and related proteins under conditions relevant to food processing
    • Pearce, F. G.; Mackintosh, S. H.; Gerrard, J. A. Formation of amyloid-like fibrils by ovalbumin and related proteins under conditions relevant to food processing J. Agric. Food Chem. 2007, 55 (2) 318-322 10.1021/jf062154p
    • (2007) J. Agric. Food Chem. , vol.55 , Issue.2 , pp. 318-322
    • Pearce, F.G.1    Mackintosh, S.H.2    Gerrard, J.A.3
  • 7
    • 84870904145 scopus 로고    scopus 로고
    • Self-Assembly of Ovalbumin into Amyloid and Non-Amyloid Fibrils
    • Lara, C.; Gourdin-Bertin, S.; Adamcik, J.; Bolisetty, S.; Mezzenga, R. Self-Assembly of Ovalbumin into Amyloid and Non-Amyloid Fibrils Biomacromolecules 2012, 13 (12) 4213-4221 10.1021/bm301481v
    • (2012) Biomacromolecules , vol.13 , Issue.12 , pp. 4213-4221
    • Lara, C.1    Gourdin-Bertin, S.2    Adamcik, J.3    Bolisetty, S.4    Mezzenga, R.5
  • 8
    • 3042673992 scopus 로고    scopus 로고
    • A highly amyloidogenic region of hen lysozyme
    • Frare, E.; de Laureto, P. P.; Zurdo, J.; Dobson, C. M.; Fontana, A. A highly amyloidogenic region of hen lysozyme J. Mol. Biol. 2004, 340 (5) 1153-1165 10.1016/j.jmb.2004.05.056
    • (2004) J. Mol. Biol. , vol.340 , Issue.5 , pp. 1153-1165
    • Frare, E.1    De Laureto, P.P.2    Zurdo, J.3    Dobson, C.M.4    Fontana, A.5
  • 9
    • 79955863547 scopus 로고    scopus 로고
    • General Self-Assembly Mechanism Converting Hydrolyzed Globular Proteins into Giant Multistranded Amyloid Ribbons
    • Lara, C.; Adamcik, J.; Jordens, S.; Mezzenga, R. General Self-Assembly Mechanism Converting Hydrolyzed Globular Proteins Into Giant Multistranded Amyloid Ribbons Biomacromolecules 2011, 12 (5) 1868-1875 10.1021/bm200216u
    • (2011) Biomacromolecules , vol.12 , Issue.5 , pp. 1868-1875
    • Lara, C.1    Adamcik, J.2    Jordens, S.3    Mezzenga, R.4
  • 10
    • 0037108179 scopus 로고    scopus 로고
    • Conformational prerequisites for alpha-lactalbumin fibrillation
    • Goers, J.; Permyakov, S. E.; Permyakov, E. A.; Uversky, V. N.; Fink, A. L. Conformational prerequisites for alpha-lactalbumin fibrillation Biochemistry 2002, 41 (41) 12546-12551 10.1021/bi0262698
    • (2002) Biochemistry , vol.41 , Issue.41 , pp. 12546-12551
    • Goers, J.1    Permyakov, S.E.2    Permyakov, E.A.3    Uversky, V.N.4    Fink, A.L.5
  • 11
    • 0037126101 scopus 로고    scopus 로고
    • Novel amyloid fibrillar networks derived from a globular protein: Beta-lactoglobulin
    • Gosal, W. S.; Clark, A. H.; Pudney, P. D. A.; Ross-Murphy, S. B. Novel amyloid fibrillar networks derived from a globular protein: beta-lactoglobulin Langmuir 2002, 18 (19) 7174-7181 10.1021/la025531a
    • (2002) Langmuir , vol.18 , Issue.19 , pp. 7174-7181
    • Gosal, W.S.1    Clark, A.H.2    Pudney, P.D.A.3    Ross-Murphy, S.B.4
  • 12
    • 52649129277 scopus 로고    scopus 로고
    • Structure of heat-induced beta-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate
    • Jung, J. M.; Savin, G.; Pouzot, M.; Schmitt, C.; Mezzenga, R. Structure of heat-induced beta-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate Biomacromolecules 2008, 9 (9) 2477-2486 10.1021/bm800502j
    • (2008) Biomacromolecules , vol.9 , Issue.9 , pp. 2477-2486
    • Jung, J.M.1    Savin, G.2    Pouzot, M.3    Schmitt, C.4    Mezzenga, R.5
  • 13
    • 73649116661 scopus 로고    scopus 로고
    • Liquid Crystalline Phase Behavior of Protein Fibers in Water: Experiments versus Theory
    • Jung, J. M.; Mezzenga, R. Liquid Crystalline Phase Behavior of Protein Fibers in Water: Experiments versus Theory Langmuir 2010, 26 (1) 504-514 10.1021/la9021432
    • (2010) Langmuir , vol.26 , Issue.1 , pp. 504-514
    • Jung, J.M.1    Mezzenga, R.2
  • 14
    • 77955230701 scopus 로고    scopus 로고
    • Understanding amyloid aggregation by statistical analysis of atomic force microscopy images
    • Adamcik, J.; Jung, J. M.; Flakowski, J.; De Los Rios, P.; Dietler, G.; Mezzenga, R. Understanding amyloid aggregation by statistical analysis of atomic force microscopy images Nat. Nanotechnol. 2010, 5 (6) 423-428 10.1038/nnano.2010.59
    • (2010) Nat. Nanotechnol. , vol.5 , Issue.6 , pp. 423-428
    • Adamcik, J.1    Jung, J.M.2    Flakowski, J.3    De Los Rios, P.4    Dietler, G.5    Mezzenga, R.6
  • 15
    • 77954279639 scopus 로고    scopus 로고
    • Effects of Charge Double Layer and Colloidal Aggregation on the Isotropic-Nematic Transition of Protein Fibers in Water
    • Mezzenga, R.; Jung, J. M.; Adamcik, J. Effects of Charge Double Layer and Colloidal Aggregation on the Isotropic-Nematic Transition of Protein Fibers in Water Langmuir 2010, 26 (13) 10401-10405 10.1021/la101636r
    • (2010) Langmuir , vol.26 , Issue.13 , pp. 10401-10405
    • Mezzenga, R.1    Jung, J.M.2    Adamcik, J.3
  • 16
    • 84867441784 scopus 로고    scopus 로고
    • Gelation, Phase Behavior, and Dynamics of beta-Lactoglobulin Amyloid Fibrils at Varying Concentrations and Ionic Strengths
    • Bolisetty, S.; Harnau, L.; Jung, J. M.; Mezzenga, R. Gelation, Phase Behavior, and Dynamics of beta-Lactoglobulin Amyloid Fibrils at Varying Concentrations and Ionic Strengths Biomacromolecules 2012, 13 (10) 3241-3252 10.1021/bm301005w
    • (2012) Biomacromolecules , vol.13 , Issue.10 , pp. 3241-3252
    • Bolisetty, S.1    Harnau, L.2    Jung, J.M.3    Mezzenga, R.4
  • 17
    • 84878709366 scopus 로고    scopus 로고
    • Non-equilibrium nature of two-dimensional isotropic and nematic coexistence in amyloid fibrils at liquid interfaces
    • Jordens, S.; Isa, L.; Usov, I.; Mezzenga, R. Non-equilibrium nature of two-dimensional isotropic and nematic coexistence in amyloid fibrils at liquid interfaces Nat. Commun. 2013, 4, 1917 10.1038/ncomms2911
    • (2013) Nat. Commun. , vol.4 , pp. 1917
    • Jordens, S.1    Isa, L.2    Usov, I.3    Mezzenga, R.4
  • 18
    • 84908313432 scopus 로고    scopus 로고
    • Re-entrant isotropic-nematic phase behavior in polymer-depleted amyloid fibrils
    • Zhao, J. G.; Li, C. X.; Mezzenga, R. Re-entrant isotropic-nematic phase behavior in polymer-depleted amyloid fibrils J. Phys.: Condens. Matter 2014, 26 (46) 464112 10.1088/0953-8984/26/46/464112
    • (2014) J. Phys.: Condens. Matter , vol.26 , Issue.46
    • Zhao, J.G.1    Li, C.X.2    Mezzenga, R.3
  • 19
    • 84971301149 scopus 로고
    • The effects of shape on the interaction of colloidal particles
    • Onsager, L. The effects of shape on the interaction of colloidal particles Ann. N. Y. Acad. Sci. 1949, 51 (4) 627-659 10.1111/j.1749-6632.1949.tb27296.x
    • (1949) Ann. N. Y. Acad. Sci. , vol.51 , Issue.4 , pp. 627-659
    • Onsager, L.1
  • 20
    • 33747298984 scopus 로고
    • Liquid crystalline substances from virusinfected plants
    • Bawden, F. C.; Pirie, N. W.; Bernal, J. D.; Fankuchen, I. Liquid crystalline substances from virusinfected plants Nature 1936, 138, 1051-1052 10.1038/1381051a0
    • (1936) Nature , vol.138 , pp. 1051-1052
    • Bawden, F.C.1    Pirie, N.W.2    Bernal, J.D.3    Fankuchen, I.4
  • 21
    • 33846799850 scopus 로고    scopus 로고
    • Isotropic to nematic liquid crystalline phase transition of F-actin varies from continuous to first order
    • Viamontes, J.; Oakes, P. W.; Tang, J. X. Isotropic to nematic liquid crystalline phase transition of F-actin varies from continuous to first order Phys. Rev. Lett. 2006, 97 (11) 118103 10.1103/PhysRevLett.97.118103
    • (2006) Phys. Rev. Lett. , vol.97 , Issue.11
    • Viamontes, J.1    Oakes, P.W.2    Tang, J.X.3
  • 22
    • 0037171195 scopus 로고    scopus 로고
    • Outstanding magnetic properties of nematic suspensions of goethite (alpha-FeOOH) nanorods
    • Lemaire, B. J.; Davidson, P.; Ferre, J.; Jamet, J. P.; Panine, P.; Dozov, I.; Jolivet, J. P. Outstanding magnetic properties of nematic suspensions of goethite (alpha-FeOOH) nanorods Phys. Rev. Lett. 2002, 88 (12) 125507 10.1103/PhysRevLett.88.125507
    • (2002) Phys. Rev. Lett. , vol.88 , Issue.12
    • Lemaire, B.J.1    Davidson, P.2    Ferre, J.3    Jamet, J.P.4    Panine, P.5    Dozov, I.6    Jolivet, J.P.7
  • 23
    • 33748097006 scopus 로고
    • Ordered Phases in Concentrated DNA Solutions
    • Rill, R. L.; Strzelecka, T. E.; Davidson, M. W.; Vanwinkle, D. H. Ordered Phases in Concentrated DNA Solutions Phys. A 1991, 176 (1) 87-116 10.1016/0378-4371(91)90435-F
    • (1991) Phys. A , vol.176 , Issue.1 , pp. 87-116
    • Rill, R.L.1    Strzelecka, T.E.2    Davidson, M.W.3    Vanwinkle, D.H.4
  • 24
    • 84875939276 scopus 로고    scopus 로고
    • The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions
    • Mezzenga, R.; Fischer, P. The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions Rep. Prog. Phys. 2013, 76 (4) 046601 10.1088/0034-4885/76/4/046601
    • (2013) Rep. Prog. Phys. , vol.76 , Issue.4
    • Mezzenga, R.1    Fischer, P.2
  • 25
    • 34547534138 scopus 로고    scopus 로고
    • Vibrational and relaxational properties of crystalline and amorphous ices
    • Johari, G. P.; Andersson, O. Vibrational and relaxational properties of crystalline and amorphous ices Thermochim. Acta 2007, 461 (1-2) 14-43 10.1016/j.tca.2007.03.011
    • (2007) Thermochim. Acta , vol.461 , Issue.1-2 , pp. 14-43
    • Johari, G.P.1    Andersson, O.2
  • 26
    • 0031558386 scopus 로고    scopus 로고
    • Natural convection, solute trapping, and channel formation during solidification of saltwater
    • Worster, M. G.; Wettlaufer, J. S. Natural convection, solute trapping, and channel formation during solidification of saltwater J. Phys. Chem. B 1997, 101 (32) 6132-6136 10.1021/jp9632448
    • (1997) J. Phys. Chem. B , vol.101 , Issue.32 , pp. 6132-6136
    • Worster, M.G.1    Wettlaufer, J.S.2
  • 27
    • 0018859760 scopus 로고
    • Concentration of Impurities by Progressive Freezing
    • Halde, R. Concentration of Impurities by Progressive Freezing Water Res. 1980, 14 (6) 575-580 10.1016/0043-1354(80)90115-3
    • (1980) Water Res. , vol.14 , Issue.6 , pp. 575-580
    • Halde, R.1
  • 28
    • 84888369881 scopus 로고    scopus 로고
    • Ice-templating, freeze casting: Beyond materials processing
    • Deville, S. Ice-templating, freeze casting: Beyond materials processing J. Mater. Res. 2013, 28 (17) 2202-2219 10.1557/jmr.2013.105
    • (2013) J. Mater. Res. , vol.28 , Issue.17 , pp. 2202-2219
    • Deville, S.1
  • 29
    • 31544472632 scopus 로고    scopus 로고
    • Freezing as a path to build complex composites
    • Deville, S.; Saiz, E.; Nalla, R. K.; Tomsia, A. P. Freezing as a path to build complex composites Science 2006, 311 (5760) 515-518 10.1126/science.1120937
    • (2006) Science , vol.311 , Issue.5760 , pp. 515-518
    • Deville, S.1    Saiz, E.2    Nalla, R.K.3    Tomsia, A.P.4
  • 30
    • 78651063967 scopus 로고    scopus 로고
    • Controlled freezing and freeze drying: A versatile route for porous and micro-/nano-structured materials
    • Qian, L.; Zhang, H. F. Controlled freezing and freeze drying: a versatile route for porous and micro-/nano-structured materials J. Chem. Technol. Biotechnol. 2011, 86 (2) 172-184 10.1002/jctb.2495
    • (2011) J. Chem. Technol. Biotechnol. , vol.86 , Issue.2 , pp. 172-184
    • Qian, L.1    Zhang, H.F.2
  • 31
    • 35748979712 scopus 로고    scopus 로고
    • Protein stability during freezing: Separation of stresses and mechanisms of protein stabilization
    • Bhatnagar, B. S.; Bogner, R. H.; Pikal, M. J. Protein stability during freezing: Separation of stresses and mechanisms of protein stabilization Pharm. Dev. Technol. 2007, 12 (5) 505-523 10.1080/10837450701481157
    • (2007) Pharm. Dev. Technol. , vol.12 , Issue.5 , pp. 505-523
    • Bhatnagar, B.S.1    Bogner, R.H.2    Pikal, M.J.3
  • 32
    • 84862194929 scopus 로고    scopus 로고
    • Frozen polymerization for aligned porous structures with enhanced mechanical stability, conductivity, and as stationary phase for HPLC
    • Barrow, M.; Eltmimi, A.; Ahmed, A.; Myers, P.; Zhang, H. F. Frozen polymerization for aligned porous structures with enhanced mechanical stability, conductivity, and as stationary phase for HPLC J. Mater. Chem. 2012, 22 (23) 11615-11620 10.1039/c2jm31425h
    • (2012) J. Mater. Chem. , vol.22 , Issue.23 , pp. 11615-11620
    • Barrow, M.1    Eltmimi, A.2    Ahmed, A.3    Myers, P.4    Zhang, H.F.5
  • 33
    • 37549062170 scopus 로고    scopus 로고
    • Ice-templating of core/shell microgel fibers through 'Bricks-and-Mortar' assembly
    • Shi, Q. H.; An, Z. S.; Tsung, C. K.; Liang, H. J.; Zheng, N. F.; Hawker, C. J.; Stucky, G. D. Ice-templating of core/shell microgel fibers through 'Bricks-and-Mortar' assembly Adv. Mater. 2007, 19 (24) 4539-4543 10.1002/adma.200700819
    • (2007) Adv. Mater. , vol.19 , Issue.24 , pp. 4539-4543
    • Shi, Q.H.1    An, Z.S.2    Tsung, C.K.3    Liang, H.J.4    Zheng, N.F.5    Hawker, C.J.6    Stucky, G.D.7
  • 34
    • 80055012527 scopus 로고    scopus 로고
    • Assembly of Colloidal Nanoparticles Directed by the Microstructures of Polycrystalline Ice
    • Shen, X. S.; Chen, L. Y.; Li, D. H.; Zhu, L. F.; Wang, H.; Liu, C. C.; Wang, Y.; Xiong, Q. H.; Chen, H. Y. Assembly of Colloidal Nanoparticles Directed by the Microstructures of Polycrystalline Ice ACS Nano 2011, 5 (10) 8426-8433 10.1021/nn203399z
    • (2011) ACS Nano , vol.5 , Issue.10 , pp. 8426-8433
    • Shen, X.S.1    Chen, L.Y.2    Li, D.H.3    Zhu, L.F.4    Wang, H.5    Liu, C.C.6    Wang, Y.7    Xiong, Q.H.8    Chen, H.Y.9
  • 35
    • 26944467652 scopus 로고    scopus 로고
    • Polymer hollow particles with controllable holes in their surfaces
    • Im, S. H.; Jeong, U. Y.; Xia, Y. N. Polymer hollow particles with controllable holes in their surfaces Nat. Mater. 2005, 4 (9) 671-675 10.1038/nmat1448
    • (2005) Nat. Mater. , vol.4 , Issue.9 , pp. 671-675
    • Im, S.H.1    Jeong, U.Y.2    Xia, Y.N.3
  • 36
    • 37049250697 scopus 로고
    • Concentration by Freeze-Thaw
    • Gibor, A. Concentration by Freeze-Thaw Science 1961, 133 (344) 193-194 10.1126/science.133.3447.193
    • (1961) Science , vol.133 , Issue.344 , pp. 193-194
    • Gibor, A.1
  • 37
    • 84860678240 scopus 로고    scopus 로고
    • Solvent freeze out crystallization of lysozyme from a lysozyme-ovalbumin mixture
    • Borbon, V. D.; Ulrich, J. Solvent freeze out crystallization of lysozyme from a lysozyme-ovalbumin mixture Cryst. Res. Technol. 2012, 47 (5) 541-547 10.1002/crat.201200073
    • (2012) Cryst. Res. Technol. , vol.47 , Issue.5 , pp. 541-547
    • Borbon, V.D.1    Ulrich, J.2
  • 38
    • 0014004365 scopus 로고
    • Polysomes Extracted from Escherichia Coli by Freeze-Thaw-Lysozyme Lysis
    • Ron, E. Z.; Kohler, R. E.; Davis, B. D. Polysomes Extracted from Escherichia Coli by Freeze-Thaw-Lysozyme Lysis Science 1966, 153 (3740) 1119-1120 10.1126/science.153.3740.1119
    • (1966) Science , vol.153 , Issue.3740 , pp. 1119-1120
    • Ron, E.Z.1    Kohler, R.E.2    Davis, B.D.3
  • 39
    • 33847298955 scopus 로고    scopus 로고
    • Ice-templated porous alumina structures
    • Deville, S.; Saiz, E.; Tomsia, A. P. Ice-templated porous alumina structures Acta Mater. 2007, 55 (6) 1965-1974 10.1016/j.actamat.2006.11.003
    • (2007) Acta Mater. , vol.55 , Issue.6 , pp. 1965-1974
    • Deville, S.1    Saiz, E.2    Tomsia, A.P.3
  • 40
    • 84924370659 scopus 로고    scopus 로고
    • FiberApp: An Open-Source Software for Tracking and Analyzing Polymers, Filaments, Biomacromolecules, and Fibrous Objects
    • Usov, I.; Mezzenga, R. FiberApp: An Open-Source Software for Tracking and Analyzing Polymers, Filaments, Biomacromolecules, and Fibrous Objects Macromolecules 2015, 48 (5) 1269-1280 10.1021/ma502264c
    • (2015) Macromolecules , vol.48 , Issue.5 , pp. 1269-1280
    • Usov, I.1    Mezzenga, R.2
  • 41
    • 0344394335 scopus 로고    scopus 로고
    • Multiple steps during the formation of beta-lactoglobulin fibrils
    • Arnaudov, L. N.; de Vries, R.; Ippel, H.; van Mierlo, C. P. M. Multiple steps during the formation of beta-lactoglobulin fibrils Biomacromolecules 2003, 4 (6) 1614-1622 10.1021/bm034096b
    • (2003) Biomacromolecules , vol.4 , Issue.6 , pp. 1614-1622
    • Arnaudov, L.N.1    De Vries, R.2    Ippel, H.3    Van Mierlo, C.P.M.4
  • 42
    • 84899775084 scopus 로고    scopus 로고
    • Controlled ice nucleation in the field of freeze-drying: Fundamentals and technology review
    • Geidobler, R.; Winter, G. Controlled ice nucleation in the field of freeze-drying: Fundamentals and technology review Eur. J. Pharm. Biopharm. 2013, 85 (2) 214-222 10.1016/j.ejpb.2013.04.014
    • (2013) Eur. J. Pharm. Biopharm. , vol.85 , Issue.2 , pp. 214-222
    • Geidobler, R.1    Winter, G.2
  • 43
    • 67651202371 scopus 로고    scopus 로고
    • Freezing-Induced Phase Separation and Spatial Microheterogeneity in Protein Solutions
    • Dong, J. P.; Hubel, A.; Bischof, J. C.; Aksan, A. Freezing-Induced Phase Separation and Spatial Microheterogeneity in Protein Solutions J. Phys. Chem. B 2009, 113 (30) 10081-10087 10.1021/jp809710d
    • (2009) J. Phys. Chem. B , vol.113 , Issue.30 , pp. 10081-10087
    • Dong, J.P.1    Hubel, A.2    Bischof, J.C.3    Aksan, A.4
  • 44
    • 33845213536 scopus 로고    scopus 로고
    • The formation of nematic liquid crystal phases by hen lysozyme amyloid fibrils
    • Corrigan, A. M.; Muller, C.; Krebs, M. R. H. The formation of nematic liquid crystal phases by hen lysozyme amyloid fibrils J. Am. Chem. Soc. 2006, 128 (46) 14740-14741 10.1021/ja064455l
    • (2006) J. Am. Chem. Soc. , vol.128 , Issue.46 , pp. 14740-14741
    • Corrigan, A.M.1    Muller, C.2    Krebs, M.R.H.3
  • 45
    • 0033586786 scopus 로고    scopus 로고
    • Protein formulation and lyophilization cycle design: Prevention of damage due to freeze-concentration induced phase separation
    • Heller, M. C.; Carpenter, J. F.; Randolph, T. W. Protein formulation and lyophilization cycle design: Prevention of damage due to freeze-concentration induced phase separation Biotechnol. Bioeng. 1999, 63 (2) 166-174 10.1002/(SICI)1097-0290(19990420)63:2<166::AID-BIT5>3.0.CO;2-H
    • (1999) Biotechnol. Bioeng. , vol.63 , Issue.2 , pp. 166-174
    • Heller, M.C.1    Carpenter, J.F.2    Randolph, T.W.3
  • 46
    • 0002429374 scopus 로고
    • Phase Equilibria in Solutions of Rod-Like Particles
    • Flory, P. J. Phase Equilibria in Solutions of Rod-Like Particles Proc. R. Soc. London, Ser. A 1956, 234 (1196) 73-89 10.1098/rspa.1956.0016
    • (1956) Proc. R. Soc. London, Ser. A , vol.234 , Issue.1196 , pp. 73-89
    • Flory, P.J.1
  • 47
    • 36549091493 scopus 로고
    • On the Isotropic-Liquid Crystal Phase-Separation in a Solution of Rodlike Particles of Different Lengths
    • Lekkerkerker, H. N. W.; Coulon, P.; Vanderhaegen, R.; Deblieck, R. On the Isotropic-Liquid Crystal Phase-Separation in a Solution of Rodlike Particles of Different Lengths J. Chem. Phys. 1984, 80 (7) 3427-3433 10.1063/1.447098
    • (1984) J. Chem. Phys. , vol.80 , Issue.7 , pp. 3427-3433
    • Lekkerkerker, H.N.W.1    Coulon, P.2    Vanderhaegen, R.3    Deblieck, R.4
  • 48
    • 0000676841 scopus 로고
    • Phase-Transitions in Lyotropic Colloidal and Polymer Liquid-Crystals
    • Vroege, G. J.; Lekkerkerker, H. N. W. Phase-Transitions in Lyotropic Colloidal and Polymer Liquid-Crystals Rep. Prog. Phys. 1992, 55 (8) 1241-1309 10.1088/0034-4885/55/8/003
    • (1992) Rep. Prog. Phys. , vol.55 , Issue.8 , pp. 1241-1309
    • Vroege, G.J.1    Lekkerkerker, H.N.W.2
  • 49
    • 0142020867 scopus 로고    scopus 로고
    • Isotropic-nematic phase behavior of length-polydisperse hard rods
    • Wensink, H. H.; Vroege, G. J. Isotropic-nematic phase behavior of length-polydisperse hard rods J. Chem. Phys. 2003, 119 (13) 6868-6882 10.1063/1.1599277
    • (2003) J. Chem. Phys. , vol.119 , Issue.13 , pp. 6868-6882
    • Wensink, H.H.1    Vroege, G.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.