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Volumn 26, Issue 2, 2012, Pages 421-426

From peptides and proteins to micro-structure mechanics and rheological properties of fibril systems

Author keywords

Fibril; Micro mechanics; Peptide; Protein; Rheology

Indexed keywords


EID: 80052738136     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2010.11.019     Document Type: Article
Times cited : (23)

References (42)
  • 6
    • 44449138916 scopus 로고    scopus 로고
    • Peptides are building blocks of heat-induced fibrillar protein aggregates of ß-lactoglobulin formed at pH 2
    • Akkermans C., Venema P., van der Goot A.J., Gruppen H., Bakx E.J., Boom R.M., et al. Peptides are building blocks of heat-induced fibrillar protein aggregates of ß-lactoglobulin formed at pH 2. Biomacromolecules 2008, 9(5):1474-1479.
    • (2008) Biomacromolecules , vol.9 , Issue.5 , pp. 1474-1479
    • Akkermans, C.1    Venema, P.2    van der Goot, A.J.3    Gruppen, H.4    Bakx, E.J.5    Boom, R.M.6
  • 9
    • 0001417865 scopus 로고    scopus 로고
    • Static and dynamic scattering of b-lactoglobulin aggregates formed after heat-induced denaturation at pH 2
    • Aymard P., Nicolai T., Durand D., Clark A.H. Static and dynamic scattering of b-lactoglobulin aggregates formed after heat-induced denaturation at pH 2. Macromolecules 1999, 32(8):2542-2552.
    • (1999) Macromolecules , vol.32 , Issue.8 , pp. 2542-2552
    • Aymard, P.1    Nicolai, T.2    Durand, D.3    Clark, A.H.4
  • 10
    • 33947694371 scopus 로고    scopus 로고
    • Heat-induced whey protein isolate fibrils: conversion, hydrolysis, and disulphide bond formation
    • Bolder S.G., Vasbinder A., Sagis L.M.C., van der Linden E. Heat-induced whey protein isolate fibrils: conversion, hydrolysis, and disulphide bond formation. International Dairy Journal 2007, 17:846-853.
    • (2007) International Dairy Journal , vol.17 , pp. 846-853
    • Bolder, S.G.1    Vasbinder, A.2    Sagis, L.M.C.3    van der Linden, E.4
  • 11
    • 0007177844 scopus 로고
    • Scaling properties in polymer physics
    • Cornell University Press, Ithaka (New York), P.G. De Gennes (Ed.)
    • De Gennes P.G. Scaling properties in polymer physics. Scaling concepts in polymer physics 1979, 223-230. Cornell University Press, Ithaka (New York). P.G. De Gennes (Ed.).
    • (1979) Scaling concepts in polymer physics , pp. 223-230
    • De Gennes, P.G.1
  • 12
    • 16344365621 scopus 로고    scopus 로고
    • Gel formation of peptides produced by extensive enzymatic hydrolysis of b-lactoglobulin
    • Doucet D., Foegeding E.A. Gel formation of peptides produced by extensive enzymatic hydrolysis of b-lactoglobulin. Biomacromolecules 2005, 6(2):1140-1148.
    • (2005) Biomacromolecules , vol.6 , Issue.2 , pp. 1140-1148
    • Doucet, D.1    Foegeding, E.A.2
  • 14
    • 0034914095 scopus 로고    scopus 로고
    • Molecular self-assembly of partially hydrolysed alpha-lactalbumin resulting in strong gels with a novel microstructure
    • Ipsen R., Otte J., Qvist K.B. Molecular self-assembly of partially hydrolysed alpha-lactalbumin resulting in strong gels with a novel microstructure. Journal of Dairy Research 2001, 68(2):277-286.
    • (2001) Journal of Dairy Research , vol.68 , Issue.2 , pp. 277-286
    • Ipsen, R.1    Otte, J.2    Qvist, K.B.3
  • 15
    • 80052693828 scopus 로고
    • Etude Par La Birefringence Decoulement De La Gelification De La Gelatine Et De Ses Interactions Avec Dautres Substances Organiques
    • Joly M. Etude Par La Birefringence Decoulement De La Gelification De La Gelatine Et De Ses Interactions Avec Dautres Substances Organiques. Bulletin De La Societe De Chimie Biologique 1949, 31(1):105-107.
    • (1949) Bulletin De La Societe De Chimie Biologique , vol.31 , Issue.1 , pp. 105-107
    • Joly, M.1
  • 16
    • 5244345265 scopus 로고
    • Etude Par La Birefringence Decoulement De La Denaturation Thermique De La Serumalbumine
    • Joly M., Barbu E. Etude Par La Birefringence Decoulement De La Denaturation Thermique De La Serumalbumine. Bulletin De La Societe De Chimie Biologique 1949, 31(11-1):1642-1655.
    • (1949) Bulletin De La Societe De Chimie Biologique , vol.31 , Issue.1-11 , pp. 1642-1655
    • Joly, M.1    Barbu, E.2
  • 17
    • 80052740942 scopus 로고
    • L'Action Des Electrolytes Sur Lagregation De La Serumalbumine - Etude Par La Birefringence Decoulement
    • Joly M., Barbu E. l'Action Des Electrolytes Sur Lagregation De La Serumalbumine - Etude Par La Birefringence Decoulement. Bulletin De La Societe De Chimie Biologique 1950, 32(11-1):849-850.
    • (1950) Bulletin De La Societe De Chimie Biologique , vol.32 , Issue.1-11 , pp. 849-850
    • Joly, M.1    Barbu, E.2
  • 18
    • 0037126110 scopus 로고    scopus 로고
    • All gelatin networks: 2. The master curve for elasticity
    • Joly-Duhamel C., Hellio D., Ajdari A., Djabourov M. All gelatin networks: 2. The master curve for elasticity. Langmuir 2002, 18(19):7158-7166.
    • (2002) Langmuir , vol.18 , Issue.19 , pp. 7158-7166
    • Joly-Duhamel, C.1    Hellio, D.2    Ajdari, A.3    Djabourov, M.4
  • 21
    • 0032487960 scopus 로고    scopus 로고
    • Nonlinear dynamics - jamming is not just cool any more
    • Liu A.J., Nagel S.R. Nonlinear dynamics - jamming is not just cool any more. Nature 1998, 396(6706):21-22.
    • (1998) Nature , vol.396 , Issue.6706 , pp. 21-22
    • Liu, A.J.1    Nagel, S.R.2
  • 22
    • 33646088595 scopus 로고    scopus 로고
    • Probing the pressure-temperature stability of amyloid fibrils provides new insights into their molecular properties
    • Meersman F., Dobson C.M. Probing the pressure-temperature stability of amyloid fibrils provides new insights into their molecular properties. Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics 2006, 1764(3):452-460.
    • (2006) Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics , vol.1764 , Issue.3 , pp. 452-460
    • Meersman, F.1    Dobson, C.M.2
  • 23
    • 33846562360 scopus 로고    scopus 로고
    • Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion
    • Mishra R., Sorgjerd K., Nystrom S., Nordigarden A., Yu Y.-C., Hammarstrom P. Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion. Journal of Molecular Biology 2007, 366(3):1029-1044.
    • (2007) Journal of Molecular Biology , vol.366 , Issue.3 , pp. 1029-1044
    • Mishra, R.1    Sorgjerd, K.2    Nystrom, S.3    Nordigarden, A.4    Yu, Y.-C.5    Hammarstrom, P.6
  • 24
    • 4244197773 scopus 로고    scopus 로고
    • Tube diameter in tightly entangled solutions of semiflexible polymers
    • Morse D.C. Tube diameter in tightly entangled solutions of semiflexible polymers. Physical Review E 2001, 63(3):031502.
    • (2001) Physical Review E , vol.63 , Issue.3 , pp. 031502
    • Morse, D.C.1
  • 26
    • 33751575369 scopus 로고
    • The statistics and dynamics of confined or entangled stiff polymers
    • Odijk T. The statistics and dynamics of confined or entangled stiff polymers. Macromolecules 1983, 16(8):1340-1344.
    • (1983) Macromolecules , vol.16 , Issue.8 , pp. 1340-1344
    • Odijk, T.1
  • 27
    • 0001631058 scopus 로고    scopus 로고
    • The random contact equation and its implications for (Colloidal) rods in packings, suspensions, and anisotropic powders
    • Philipse A.P. The random contact equation and its implications for (Colloidal) rods in packings, suspensions, and anisotropic powders. Langmuir 1996, 12(5):1127-1133.
    • (1996) Langmuir , vol.12 , Issue.5 , pp. 1127-1133
    • Philipse, A.P.1
  • 30
    • 0032488529 scopus 로고    scopus 로고
    • On the density and structure formation in gels and clusters of colloidal rods and fibers
    • Philipse A.P., Wierenga A.M. On the density and structure formation in gels and clusters of colloidal rods and fibers. Langmuir 1998, 14(1):49-54.
    • (1998) Langmuir , vol.14 , Issue.1 , pp. 49-54
    • Philipse, A.P.1    Wierenga, A.M.2
  • 31
    • 17044440175 scopus 로고    scopus 로고
    • Measuring the length distribution of a fibril system: a flow birefringence technique applied to amyloid fibrils
    • Rogers S.S., Venema P., Sagis L.M.C., van der Linden E., Donald A.M. Measuring the length distribution of a fibril system: a flow birefringence technique applied to amyloid fibrils. Macromolecules 2005, 38(7):2948-2958.
    • (2005) Macromolecules , vol.38 , Issue.7 , pp. 2948-2958
    • Rogers, S.S.1    Venema, P.2    Sagis, L.M.C.3    van der Linden, E.4    Donald, A.M.5
  • 33
  • 35
    • 27144550792 scopus 로고    scopus 로고
    • Elasticity due to semiflexible protein assemblies near the critical gel concentration and beyond
    • van der Linden E., Parker A. Elasticity due to semiflexible protein assemblies near the critical gel concentration and beyond. Langmuir 2005, 21(21):9792-9794.
    • (2005) Langmuir , vol.21 , Issue.21 , pp. 9792-9794
    • van der Linden, E.1    Parker, A.2
  • 36
    • 34548843934 scopus 로고    scopus 로고
    • Similarities in self-assembly of proteins and surfactants: an attempt to bridge the gap
    • The Royal Society of Chemistry, Cambridge UK
    • van der Linden E., Venema P. Similarities in self-assembly of proteins and surfactants: an attempt to bridge the gap. Food colloids. Self-assembly and material science 2007, 57-67. The Royal Society of Chemistry, Cambridge UK.
    • (2007) Food colloids. Self-assembly and material science , pp. 57-67
    • van der Linden, E.1    Venema, P.2
  • 39
    • 0036054901 scopus 로고    scopus 로고
    • Effect of electrostatic interactions on the percolation concentration of fibrillar ß-lactoglobulin gels
    • Veerman C., Ruis H.G.M., Sagis L.M.C., van der Linden E. Effect of electrostatic interactions on the percolation concentration of fibrillar ß-lactoglobulin gels. Biomacromolecules 2002, 3(4):869-873.
    • (2002) Biomacromolecules , vol.3 , Issue.4 , pp. 869-873
    • Veerman, C.1    Ruis, H.G.M.2    Sagis, L.M.C.3    van der Linden, E.4
  • 40
    • 0037941389 scopus 로고    scopus 로고
    • Gels at extremely low weight fractions (0.07%) formed by irreversible self-assembly of proteins
    • Veerman C., Sagis L.M.C., van der Linden E. Gels at extremely low weight fractions (0.07%) formed by irreversible self-assembly of proteins. Macromolecular Bioscience 2003, 3(5):243-247.
    • (2003) Macromolecular Bioscience , vol.3 , Issue.5 , pp. 243-247
    • Veerman, C.1    Sagis, L.M.C.2    van der Linden, E.3
  • 41
    • 31144446814 scopus 로고    scopus 로고
    • The effect of shear flow on the percolation concentration of fibrillar protein assemblies
    • Veerman C., Sagis L.M.C., Venema P., van der Linden E. The effect of shear flow on the percolation concentration of fibrillar protein assemblies. Journal of Rheology 2005, 49(2):355-368.
    • (2005) Journal of Rheology , vol.49 , Issue.2 , pp. 355-368
    • Veerman, C.1    Sagis, L.M.C.2    Venema, P.3    van der Linden, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.