메뉴 건너뛰기




Volumn 39, Issue 6, 2010, Pages 1007-1017

Irreversible gelation of thermally unfolded proteins: Structural and mechanical properties of lysozyme aggregates

Author keywords

Gelation; Percolation; Protein aggregation; Thermal irreversibility; Unfolding

Indexed keywords


EID: 77952099647     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-009-0503-4     Document Type: Article
Times cited : (21)

References (52)
  • 1
    • 11244340520 scopus 로고    scopus 로고
    • Thermally induced fibrillar aggregation of hen egg white lysozyme
    • DOI 10.1529/biophysj.104.048819
    • LN Arnaudov R de Vries 2005 Thermally induced fibrillar aggregation of hen egg white lysozyme Biophys J 88 1 515 526 10.1529/biophysj.104.048819 15489299 (Pubitemid 40070697)
    • (2005) Biophysical Journal , vol.88 , Issue.1 , pp. 515-526
    • Arnaudov, L.N.1    De Vries, R.2
  • 2
    • 0036037356 scopus 로고    scopus 로고
    • Unfolding and aggregation during the thermal denaturation of streptokinase
    • DOI 10.1046/j.1432-1033.2002.03107.x
    • AI Azuaga CM Dobson PL Mateo F Conejero-Lara 2002 Unfolding and aggregation during the thermal denaturation of streptokinase Eur J Biochem 269 4121 4133 10.1046/j.1432-1033.2002.03107.x 12180989 (Pubitemid 34994907)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.16 , pp. 4121-4133
    • Azuaga, A.I.1    Dobson, C.M.2    Mateo, P.L.3    Conejero-Lara, F.4
  • 4
    • 0000012892 scopus 로고
    • Dsc studies on the denaturation and aggregation of serum albumins
    • 10.1016/0040-6031(92)80263-V
    • G Barone C Giancola A Verdoliva 1992 Dsc studies on the denaturation and aggregation of serum albumins Thermochim Acta 199 197 205 10.1016/0040-6031(92) 80263-V
    • (1992) Thermochim Acta , vol.199 , pp. 197-205
    • Barone, G.1    Giancola, C.2    Verdoliva, A.3
  • 5
    • 2642562735 scopus 로고    scopus 로고
    • Influence of the ionic strength on the heat-induced aggregation of the globular protein β-lactoglobulin at pH 7
    • DOI 10.1016/j.ijbiomac.2003.11.003, PII S0141813003001442
    • K Baussay CL Bon T Nicolai D Durand J-P Busnel 2004 Influence of the ionic strength on the heat-induced aggregation of the globular protein b-lactoglobulin at ph 7 Int J Biol Macromol 34 21 28 10.1016/j.ijbiomac.2003.11. 003 15178005 (Pubitemid 38721181)
    • (2004) International Journal of Biological Macromolecules , vol.34 , Issue.1-2 , pp. 21-28
    • Baussay, K.1    Le Bon, C.2    Nicolai, T.3    Durand, D.4    Busnel, J.-P.5
  • 6
    • 0028751624 scopus 로고
    • Transputer-based upgrading of a differential scanning calorimeter
    • 10.1088/0957-0233/5/12/004
    • D Bulone LG Fornili SL Fornili M Lapis PL San Biagio 1994 Transputer-based upgrading of a differential scanning calorimeter Meas Sci Technol 5 1443 1447 10.1088/0957-0233/5/12/004
    • (1994) Meas Sci Technol , vol.5 , pp. 1443-1447
    • Bulone, D.1    Fornili, L.G.2    Fornili, S.L.3    Lapis, M.4    San Biagio, P.L.5
  • 7
    • 1642452936 scopus 로고    scopus 로고
    • Formation of amyloid fibrils from fully reduced hen egg white lysozyme
    • DOI 10.1110/ps.03183404
    • A Cao D Hu L Lai 2004 Formation of amyloid fibrils from fully reduced hen egg white lysozyme Protein Sci 13 319 324 10.1110/ps.03183404 14718651 (Pubitemid 38124952)
    • (2004) Protein Science , vol.13 , Issue.2 , pp. 319-324
    • Cao, A.1    Hu, D.2    Lai, L.3
  • 8
    • 36048943585 scopus 로고    scopus 로고
    • Large size fibrillar bundles of the Alzheimer amyloid β-protein
    • DOI 10.1007/s00249-007-0164-0, Proceedings of the XVIII Congress of the Italian Society of Pure and Applied Biophysics (SIBPA), Palermo, Sicily, September 2006
    • R Carrotta J Barthès A Longo V Martorana M Manno G Portale PL San Biagio 2007 Large size fibrillar bundles of the Alzheimer amyloid β-protein Eur Biophys J 36 701 709 10.1007/s00249-007-0164-0 17492436 (Pubitemid 350092521)
    • (2007) European Biophysics Journal , vol.36 , Issue.7 , pp. 701-709
    • Carrotta, R.1    Barthes, J.2    Longo, A.3    Martorana, V.4    Manno, M.5    Portale, G.6    San Biagio, P.L.7
  • 9
    • 65649087063 scopus 로고    scopus 로고
    • Protein stability modulated by a conformational effector: Effects of trifluoroethanol on bovine serum albumin
    • 10.1039/b818687a
    • R Carrotta M Manno FM Giordano A Longo G Portale V Martorana PL San Biagio 2009 Protein stability modulated by a conformational effector: effects of trifluoroethanol on bovine serum albumin Phys Chem Phys 11 4007 4018 10.1039/b818687a
    • (2009) Phys Chem Phys , vol.11 , pp. 4007-4018
    • Carrotta, R.1    Manno, M.2    Giordano, F.M.3    Longo, A.4    Portale, G.5    Martorana, V.6    San Biagio, P.L.7
  • 10
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F Chiti CM Dobson 2006 Protein misfolding, functi nal amyloid, and human disease Annu Rev Biochem 75 333 366 10.1146/annurev.biochem.75.101304.123901 16756495 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 11
    • 0035187378 scopus 로고    scopus 로고
    • Globular protein gelation - Theory and experiment
    • DOI 10.1016/S0268-005X(01)00042-X, PII S0268005X0100042X
    • A Clark G Kavanagh S Ross-Murphy 2001 Globular protein gelation-theory and experiment Food Hydrocolloids 15 383 400 10.1016/S0268-005X(01)00042-X (Pubitemid 33086066)
    • (2001) Food Hydrocolloids , vol.15 , Issue.4-6 , pp. 383-400
    • Clark, A.H.1    Kavanagh, G.M.2    Ross-Murphy, S.B.3
  • 12
    • 4243569535 scopus 로고
    • Denaturation versus pH of lysozyme and biosynthetic human growth hormone by differential scanning calorimetry and circular dichroism: A comparative study
    • 10.1016/0040-6031(92)80138-M
    • P Claudy JM Létoffé A Bayol MC Bonnet JC Maurizot 1992 Denaturation versus pH of lysozyme and biosynthetic human growth hormone by differential scanning calorimetry and circular dichroism: a comparative study Thermochim Acta 207 227 237 10.1016/0040-6031(92)80138-M
    • (1992) Thermochim Acta , vol.207 , pp. 227-237
    • Claudy, P.1    Létoffé, J.M.2    Bayol, A.3    Bonnet, M.C.4    Maurizot, J.C.5
  • 13
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • DOI 10.1021/bi00483a001
    • KA Dill 1990 Dominant forces in protein folding Biochemistry 29 31 7133 7155 10.1021/bi00483a001 2207096 (Pubitemid 20230041)
    • (1990) Biochemistry , vol.29 , Issue.31 , pp. 7133-7155
    • Dill, K.A.1
  • 14
    • 77956742997 scopus 로고
    • Protein gels
    • 10.1016/S0065-3233(08)60004-2 18884345
    • JD Ferry 1948 Protein gels Adv Protein Chem 4 1 78 10.1016/S0065-3233(08) 60004-2 18884345
    • (1948) Adv Protein Chem , vol.4 , pp. 1-78
    • Ferry, J.D.1
  • 18
    • 0001121864 scopus 로고    scopus 로고
    • Rapid evolution of reversible denaturation and elevated melting temperature in a microbial haloalkane dehalogenase
    • 10.1002/1615-4169(200108)343:6/7<607::AID-ADSC607>3.0.CO;2-M
    • KA Gray TH Richardson K Kretz JM Short F Bartnek R Knowles L Kan P Swanson DE Robertson 2001 Rapid evolution of reversible denaturation and elevated melting temperature in a microbial haloalkane dehalogenase Adv Synth Catal 343 607 617 10.1002/1615-4169(200108)343:6/7<607::AID-ADSC607>3.0. CO;2-M
    • (2001) Adv Synth Catal , vol.343 , pp. 607-617
    • Gray, K.A.1    Richardson, T.H.2    Kretz, K.3    Short, J.M.4    Bartnek, F.5    Knowles, R.6    Kan, L.7    Swanson, P.8    Robertson, D.E.9
  • 19
    • 34547647893 scopus 로고    scopus 로고
    • Evidence of a two-stage thermal denaturation process in lysozyme: A Raman scattering and differential scanning calorimetry investigation
    • 10.1063/1.2139087
    • A Hedoux R Ionov J-F Willart A Lerbret F Affouard Y Guinet M Descamps D Prevost L Paccou F Danede 2006 Evidence of a two-stage thermal denaturation process in lysozyme: a Raman scattering and differential scanning calorimetry investigation J Chem Phys 124 014703 10.1063/1.2139087
    • (2006) J Chem Phys , vol.124 , pp. 014703
    • Hedoux, A.1    Ionov, R.2    Willart, J.-F.3    Lerbret, A.4    Affouard, F.5    Guinet, Y.6    Descamps, M.7    Prevost, D.8    Paccou, L.9    Danede, F.10
  • 20
    • 84998379089 scopus 로고
    • Protein flexibil ty and functional properties of heat-denatured ovalbumin and lysozyme
    • A Kato K Fujimoto N Matsudomi K Kobayashi 1986 Protein flexibility and functional properties of heat-denatured ovalbumin and lysozyme Agric Biol Chem 50 417 420
    • (1986) Agric Biol Chem , vol.50 , pp. 417-420
    • Kato, A.1    Fujimoto, K.2    Matsudomi, N.3    Kobayashi, K.4
  • 21
    • 0034647438 scopus 로고    scopus 로고
    • Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain
    • 10.1006/jmbi.2000.3862 10884350
    • M Krebs D Wilkins E Chung M Pitkeathly A Chamberlain J Zurdo C Robinson C Dobson 2000 Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain J Mol Biol 300 541 549 10.1006/jmbi.2000.3862 10884350
    • (2000) J Mol Biol , vol.300 , pp. 541-549
    • Krebs, M.1    Wilkins, D.2    Chung, E.3    Pitkeathly, M.4    Chamberlain, A.5    Zurdo, J.6    Robinson, C.7    Dobson, C.8
  • 22
    • 33846839238 scopus 로고    scopus 로고
    • Protein particulates: Another generic form of protein aggregation?
    • DOI 10.1529/biophysj.106.094342
    • MRH Krebs GL Devlin AM Donald 2007 Protein particulates: another generic form of protein aggregation Biophys J 92 1336 1342 10.1529/biophysj.106.094342 17114226 (Pubitemid 46203194)
    • (2007) Biophysical Journal , vol.92 , Issue.4 , pp. 1336-1342
    • Krebs, M.R.H.1    Devlin, G.L.2    Donald, A.M.3
  • 23
    • 0034616839 scopus 로고    scopus 로고
    • Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: Implications for amyloid fibril formation and materials science
    • DOI 10.1021/ja9937831
    • HA Lashuel SR LaBrenz L Woo LC Serpell JW Kelly 2000 Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: implications for amyloid fibril formation and materials science J Am Chem Soc 122 5262 5277 10.1021/ja9937831 (Pubitemid 30395258)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.22 , pp. 5262-5277
    • Lashuel, H.A.1    LaBrenz, S.R.2    Woo, L.3    Serpell, L.C.4    Kelly, J.W.5
  • 25
    • 4143063021 scopus 로고    scopus 로고
    • Thermodynamic instability in supersaturated lysozyme solutions: Effect of salt and role of concentration fluctuations
    • 10.1103/PhysRevE.68.011904
    • M Manno C Xiao D Bulone V Martorana PL San Biagio 2003 Thermodynamic instability in supersaturated lysozyme solutions: effect of salt and role of concentration fluctuations Phys Rev E 68 011904 10.1103/PhysRevE.68.011904
    • (2003) Phys Rev e , vol.68 , pp. 011904
    • Manno, M.1    Xiao, C.2    Bulone, D.3    Martorana, V.4    San Biagio, P.L.5
  • 26
    • 0043161935 scopus 로고    scopus 로고
    • Conformational changes involved in thermal aggregation processes of bovine serum albumin
    • DOI 10.1016/S0301-4622(03)00153-4
    • V Militello V Vetri M Leone 2003 Conformational changes involved in thermal aggregation processes of bovine serum albumin Biophys Chem 105 133 141 10.1016/S0301-4622(03)00153-4 12932585 (Pubitemid 36970268)
    • (2003) Biophysical Chemistry , vol.105 , Issue.1 , pp. 133-141
    • Militello, V.1    Vetri, V.2    Leone, M.3
  • 27
    • 0002976987 scopus 로고
    • Thermally induced changes in egg white proteins
    • 10.1021/jf00102a004
    • Y Mine T Noutomi N Haga 1990 Thermally induced changes in egg white proteins J Agric Food Chem 38 2122 2125 10.1021/jf00102a004
    • (1990) J Agric Food Chem , vol.38 , pp. 2122-2125
    • Mine, Y.1    Noutomi, T.2    Haga, N.3
  • 28
    • 0031559476 scopus 로고    scopus 로고
    • Liquid-liquid phase separation in supersaturated lysozyme solution and associated precipitate formation/crystallization
    • 10.1063/1.474547
    • M Muschol F Rosenberger 1997 Liquid-liquid phase separation in supersaturated lysozyme solution and associated precipitate formation/ crystallization Chem Phys 107 1953 1962 10.1063/1.474547
    • (1997) J Chem Phys , vol.107 , pp. 1953-1962
    • Muschol, M.1    Rosenberger, F.2
  • 29
    • 62949238920 scopus 로고    scopus 로고
    • Pre-aggregates characterization and viscoelastic studies of BSA cold gels induced by metal ions
    • doi:10.1007/s00249-008-0389-6
    • Navarra G, Giacomazza D, Leone M, Militello V, San Biagio PL (2009) Pre-aggregates characterization and viscoelastic studies of BSA cold gels induced by metal ions. Eur Biophys J doi: 10.1007/s00249-008-0389-6
    • (2009) Eur Biophys J
    • Navarra, G.1    Giacomazza, D.2    Leone, M.3    Militello, V.4    San Biagio, P.L.5
  • 30
    • 0039300582 scopus 로고
    • Optimization approaches to thermally induced egg white lysozyme gel
    • S Nayakawa R Nakamura 1986 Optimization approaches to thermally induced egg white lysozyme gel Agric Biol Chem 50 2039 2046
    • (1986) Agric Biol Chem , vol.50 , pp. 2039-2046
    • Nayakawa, S.1    Nakamura, R.2
  • 31
    • 0002503424 scopus 로고    scopus 로고
    • Scattering properties and modelling of aggregating and gelling systems
    • Brown W (ed) Clarendon Press, Oxford
    • Nicolai T, Durand D, Gimel J-C (1996) Scattering properties and modelling of aggregating and gelling systems. In: Brown W (ed) Light scattering: principles and development. Clarendon Press, Oxford
    • (1996) Light Scattering: Principles and Development
    • Nicolai, T.1    Durand, D.2    Gimel, J.-C.3
  • 32
    • 0032940179 scopus 로고    scopus 로고
    • Kinetic study on thermal denaturation of hen egg-white lysozyme involving precipitation
    • DOI 10.1016/S1389-1723(99)89013-6
    • D Nohara A Mizutani T Sakai 1999 Kinetic study on thermal denaturation of hen egg-white lysozyme involving precipitation J Biosci Bioeng 87 199 205 10.1016/S1389-1723(99)89013-6 16232451 (Pubitemid 29173416)
    • (1999) Journal of Bioscience and Bioengineering , vol.87 , Issue.2 , pp. 199-205
    • Nohara, D.1    Mizutani, A.2    Sakai, T.3
  • 33
    • 0016505899 scopus 로고
    • The stability of globular proteins
    • 10.3109/10409237509102551 238787
    • CN Pace 1975 The stability of globular proteins CRC Crit Rev Biochem 3 1 43 10.3109/10409237509102551 238787
    • (1975) CRC Crit Rev Biochem , vol.3 , pp. 1-43
    • Pace, C.N.1
  • 34
    • 1542680924 scopus 로고    scopus 로고
    • Heat induced aggregation and gelation of casein submicelles
    • DOI 10.1016/j.idairyj.2003.09.003, PII S0958694603002218
    • M Panouille T Nicolai D Durand 2004 Heat induced aggregation and gelation of casein submicelles Int Dairy J 14 297 303 10.1016/j.idairyj.2003.09.003 (Pubitemid 38345652)
    • (2004) International Dairy Journal , vol.14 , Issue.4 , pp. 297-303
    • Panouille, M.1    Nicolai, T.2    Durand, D.3
  • 35
    • 12744259081 scopus 로고
    • Small-angle scattering from precipitates: Analysis by use of a polydisperse hard-sphere model
    • 10.1103/PhysRevB.47.657
    • JS Pedersen 1993 Small-angle scattering from precipitates: analysis by use of a polydisperse hard-sphere model Phys Rev B 47 657 665 10.1103/PhysRevB.47.657
    • (1993) Phys Rev B , vol.47 , pp. 657-665
    • Pedersen, J.S.1
  • 36
    • 0034276092 scopus 로고    scopus 로고
    • Protein crystallization: Scaling of charge and salt concentration in lysozyme solutions
    • 10.1088/0953-8984/12/35/103
    • WCK Poon SU Egelhaaf PA Beales A Salonen L Sawyer 2000 Protein crystallization: scaling of charge and salt concentration in lysozyme solutions J Phys Condens Matter 12 L569 L574 10.1088/0953-8984/12/35/103
    • (2000) J Phys Condens Matter , vol.12
    • Poon, W.C.K.1    Egelhaaf, S.U.2    Beales, P.A.3    Salonen, A.4    Sawyer, L.5
  • 37
    • 33846185994 scopus 로고    scopus 로고
    • Comparison of the effects of 2,2,2-trifluoroethanol on peptide and protein structure and function
    • DOI 10.1016/j.jsb.2006.07.008, PII S1047847706002188
    • JF Povey CM Smales SJ Hassard MJ Howard 2007 Comparison of the effects of 2,2,2-trifluoroethanol on peptide and protein structure and function J Struct Biol 157 329 338 10.1016/j.jsb.2006.07.008 16979904 (Pubitemid 46109329)
    • (2007) Journal of Structural Biology , vol.157 , Issue.2 , pp. 329-338
    • Povey, J.F.1    Smales, C.M.2    Hassard, S.J.3    Howard, M.J.4
  • 38
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • 10.1016/S0065-3233(08)60460-X 44431
    • PL Privalov 1979 Stability of proteins: small globular proteins Adv Protein Chem 33 167 241 10.1016/S0065-3233(08)60460-X 44431
    • (1979) Adv Protein Chem , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 40
    • 35248824245 scopus 로고    scopus 로고
    • Viscoelasticity and Stokes-Einstein relation in repulsive and attractive colloidal glasses
    • DOI 10.1063/1.2772628
    • AM Puertas C De Michele F Sciortino P Tartaglia E Zaccarelli 2007 Viscoelasticity and Stokes-Einstein relation in repulsive and attractive colloidal glasses J Chem Phys 127 144906 10.1063/1.2772628 17935438 (Pubitemid 47569047)
    • (2007) Journal of Chemical Physics , vol.127 , Issue.14 , pp. 144906
    • Puertas, A.M.1    De Michele, C.2    Sciortino, F.3    Tartaglia, P.4    Zaccarelli, E.5
  • 41
    • 36148939558 scopus 로고    scopus 로고
    • Investigation of the phase behavior of an embedded charge protein model through molecular simulation
    • DOI 10.1021/jp075455q
    • TW Rosch JR Errington 2007 Investigation of the phase behavior of an embedded charge protein model through molecular simulation J Phys Chem B 111 12591 12598 10.1021/jp075455q 17929863 (Pubitemid 350103376)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.43 , pp. 12591-12598
    • Rosch, T.W.1    Errington, J.R.2
  • 42
    • 0344252790 scopus 로고
    • A theory of the linear viscoelastic properties of dilute solutions of coiling polymers
    • 10.1063/1.1699180
    • PEJ Rouse 1953 A theory of the linear viscoelastic properties of dilute solutions of coiling polymers J Chem Phys 21 1272 1280 10.1063/1.1699180
    • (1953) J Chem Phys , vol.21 , pp. 1272-1280
    • Rouse, P.E.J.1
  • 43
    • 0000197747 scopus 로고    scopus 로고
    • Rheology of suspensions of weakly attractive particles: Approach to gelation
    • 10.1122/1.550966
    • CJ Rueb CF Zukoski 1998 Rheology of suspensions of weakly attractive particles: approach to gelation J Rheol 42 1451 1476 10.1122/1.550966
    • (1998) J Rheol , vol.42 , pp. 1451-1476
    • Rueb, C.J.1    Zukoski, C.F.2
  • 44
    • 0038199766 scopus 로고
    • Differential scanning calorimetric study of the interactions of some stabilizing amino acids and oligopeptides with hen egg white lysozyme
    • 10.1039/ft9959102101
    • B Sabulal N Kishore 1995 Differential scanning calorimetric study of the interactions of some stabilizing amino acids and oligopeptides with hen egg white lysozyme J Chem Soc Faraday Trans 91 14 2101 2106 10.1039/ft9959102101
    • (1995) J Chem Soc Faraday Trans , vol.91 , Issue.14 , pp. 2101-2106
    • Sabulal, B.1    Kishore, N.2
  • 45
    • 0037072012 scopus 로고    scopus 로고
    • The endothermic effects during denaturation of lysozyme by temperature modulated calorimetry and an intermediate reaction equilibrium
    • DOI 10.1021/jp025587d
    • G Salvetti E Tombari L Mikheeva GP Johari 2002 The endothermic effects during denaturation of lysozyme by temperature modulated calorimetry and an intermediate reaction equilibrium J Phys Chem B 106 6081 6087 10.1021/jp025587d (Pubitemid 35281855)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.23 , pp. 6081-6087
    • Salvetti, G.1    Tombari, E.2    Mikheeva, L.3    Johari, G.P.4
  • 46
    • 0001189246 scopus 로고
    • The physical chemistry of insulin. I. Hydrogen ion titration curve of zinc-free insulin
    • 10.1021/ja01637a035
    • C Tanford J Epstein 1954 The physical chemistry of insulin. I. Hydrogen ion titration curve of zinc-free insulin J Am Chem Soc 76 2163 2169 10.1021/ja01637a035
    • (1954) J Am Chem Soc , vol.76 , pp. 2163-2169
    • Tanford, C.1    Epstein, J.2
  • 47
    • 0030806177 scopus 로고    scopus 로고
    • Enhancement of protein crystal nucleation by critical density fluctuations
    • DOI 10.1126/science.277.5334.1975
    • PR ten Wolde D Frenkel 1997 Enhancement of protein crystal nucleation by critical density fluctuations Science 277 1975 1978 10.1126/science.277.5334. 1975 9302288 (Pubitemid 27449135)
    • (1997) Science , vol.277 , Issue.5334 , pp. 1975-1978
    • Ten Wolde, P.R.1    Frenkel, D.2
  • 48
    • 33244490300 scopus 로고    scopus 로고
    • Effect of heat-treatment on the physico-chemical properties of egg white proteins: A kinetic study
    • DOI 10.1016/j.jfoodeng.2005.04.019, PII S0260877405002542
    • I van der Plancken A Van Loey ME Hendrickx 2006 Effect of heat-treatment on the physico-chemical properties of egg white proteins: a kinetic study J Food Eng 75 316 326 10.1016/j.jfoodeng.2005.04.019 (Pubitemid 43277422)
    • (2006) Journal of Food Engineering , vol.75 , Issue.3 , pp. 316-326
    • Van Der Plancken, I.1    Van Loey, A.2    Hendrickx, M.E.3
  • 49
    • 35748957119 scopus 로고    scopus 로고
    • Thermal aggregation of bovine serum albumin at different pH: Comparison with human serum albumin
    • DOI 10.1007/s00249-007-0196-5, Proceedings of the XVIII Congress of the Italian Society of Pure and Applied Biophysics (SIBPA), Palermo, Sicily, September 2006
    • V Vetri F Librizzi M Leone V Militello 2007 Thermal aggregation of bovine serum albumin at different pH: comparison with human serum albumin Eur Biophys J 36 717 725 10.1007/s00249-007-0196-5 17624524 (Pubitemid 350092526)
    • (2007) European Biophysics Journal , vol.36 , Issue.7 , pp. 717-725
    • Vetri, V.1    Librizzi, F.2    Leone, M.3    Militello, V.4
  • 50
    • 0022694827 scopus 로고
    • ANALYSIS OF LINEAR VISCOELASTICITY OF A CROSSLINKING POLYMER AT THE GEL POINT.
    • DOI 10.1122/1.549853
    • HH Winter F Chambon 1986 Analysis of linear viscoelasticity of a crosslinking polymer at the gel point J Rheol 30 367 382 10.1122/1.549853 (Pubitemid 16535398)
    • (1986) Journal of Rheology , vol.30 , Issue.2 , pp. 367-382
    • Winter H.Henning1    Chambon Francois2
  • 51
    • 33750369218 scopus 로고    scopus 로고
    • Thermoreversible protein hydrogel as cell scaffold
    • DOI 10.1021/bm0605560
    • H Yan A Saiani JE Gough AF Miller 2006 Thermoreversible protein hydrogel as cell scaffold Biomacromolecules 7 2776 2782 10.1021/bm0605560 17025352 (Pubitemid 44615260)
    • (2006) Biomacromolecules , vol.7 , Issue.10 , pp. 2776-2782
    • Yan, H.1    Saiani, A.2    Gough, J.E.3    Miller, A.F.4
  • 52
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of novel biomaterials through molecular self-assembly
    • DOI 10.1038/nbt874
    • S Zhang 2003 Fabrication of novel biomaterials through molecular self-assembly Nat Biotechnol 21 1171 1178 10.1038/nbt874 14520402 (Pubitemid 37186173)
    • (2003) Nature Biotechnology , vol.21 , Issue.10 , pp. 1171-1178
    • Zhang, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.