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Volumn 57, Issue 3, 2013, Pages 1003-1022

Shear and dilatational linear and nonlinear subphase controlled interfacial rheology of β-lactoglobulin fibrils and their derivatives

Author keywords

lactoglobulin fibrils; Amyloid fibrils; Dilatational rheology; Interfacial rheology; LAOS; Pendant drop tensiometry; Rheological fingerprint; SAOS

Indexed keywords

AMYLOID FIBRIL; DILATATIONAL RHEOLOGY; INTERFACIAL RHEOLOGY; LACTOGLOBULIN; LAOS; PENDANT DROP TENSIOMETRY; RHEOLOGICAL FINGERPRINT; SAOS;

EID: 84877289006     PISSN: 01486055     EISSN: None     Source Type: Journal    
DOI: 10.1122/1.4802051     Document Type: Article
Times cited : (110)

References (43)
  • 1
    • 77955230701 scopus 로고    scopus 로고
    • Understanding amyloid aggregation by statistical analysis of atomic force microscopy images
    • 10.1038/nnano.2010.59
    • Adamcik, J., J. M. Jung, J. Flakowski, P. De Los Rios, G. Dietler, and R. Mezzenga, Understanding amyloid aggregation by statistical analysis of atomic force microscopy images., Nat. Nanotechnol. 5, 423-428 (2010). 10.1038/nnano.2010.59
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 423-428
    • Adamcik, J.1    Jung, J.M.2    Flakowski, J.3    De Los Rios, P.4    Dietler, G.5    Mezzenga, R.6
  • 2
    • 43749085625 scopus 로고    scopus 로고
    • Formation of fibrillar whey protein aggregates: Influence of heat and shear treatment, and resulting rheology
    • 10.1016/j.foodhyd.2007.07.001
    • Akkermans, C., A. J. van der Goot, P. Venema, E. van der Linden, and R. M. Boom, Formation of fibrillar whey protein aggregates: Influence of heat and shear treatment, and resulting rheology., Food Hydrocolloids 22, 1315-1325 (2008). 10.1016/j.foodhyd.2007.07.001
    • (2008) Food Hydrocolloids , vol.22 , pp. 1315-1325
    • Akkermans, C.1    Van Der Goot, A.J.2    Venema, P.3    Van Der Linden, E.4    Boom, R.M.5
  • 3
    • 79952408560 scopus 로고    scopus 로고
    • On the measurement of the surface pressure in langmuir films with finite shear elasticity
    • 10.1039/c0sm01213k
    • Aumaitre, E., D. Vella, and P. Cicuta, On the measurement of the surface pressure in langmuir films with finite shear elasticity., Soft Matter 7, 2530-2537 (2011). 10.1039/c0sm01213k
    • (2011) Soft Matter , vol.7 , pp. 2530-2537
    • Aumaitre, E.1    Vella, D.2    Cicuta, P.3
  • 4
    • 0343058964 scopus 로고    scopus 로고
    • Viscoelastic properties of triacylglycerol/water interfaces covered by proteins
    • 10.1016/0927-7757(96)03533-9
    • Benjamins, J., A. Cagna, and E. Lucassen-Reynders, Viscoelastic properties of triacylglycerol/water interfaces covered by proteins., Colloids Surf., A 114, 245-254 (1996). 10.1016/0927-7757(96)03533-9
    • (1996) Colloids Surf., A , vol.114 , pp. 245-254
    • Benjamins, J.1    Cagna, A.2    Lucassen-Reynders, E.3
  • 5
    • 33746577383 scopus 로고    scopus 로고
    • Compression/expansion rheology of oil/water interfaces with adsorbed proteins. Comparison with the air/water surface
    • 10.1021/la060441h
    • Benjamins, J., J. Lyklema, and E. Lucassen-Reynders, Compression/ expansion rheology of oil/water interfaces with adsorbed proteins. Comparison with the air/water surface., Langmuir 22, 6181-6188 (2006). 10.1021/la060441h
    • (2006) Langmuir , vol.22 , pp. 6181-6188
    • Benjamins, J.1    Lyklema, J.2    Lucassen-Reynders, E.3
  • 6
    • 78651367537 scopus 로고    scopus 로고
    • Snapshots of fibrillation and aggregation kinetics in multistranded amyloid β-lactoglobulin fibrils
    • 10.1039/c0sm00502a
    • Bolisetty, S., J. Adamcik, and R. Mezzenga, Snapshots of fibrillation and aggregation kinetics in multistranded amyloid β-lactoglobulin fibrils., Soft Matter 7, 493-499 (2011). 10.1039/c0sm00502a
    • (2011) Soft Matter , vol.7 , pp. 493-499
    • Bolisetty, S.1    Adamcik, J.2    Mezzenga, R.3
  • 7
    • 0344541703 scopus 로고    scopus 로고
    • An interfacial stress rheometer to study rheological transitions in monolayers at the air water interface
    • 10.1021/la980465r
    • Brooks, C. F., G. G. Fuller, C. W. Frank, and C. R. Robertson, An interfacial stress rheometer to study rheological transitions in monolayers at the air water interface., Langmuir 15, 2450-2459 (1999). 10.1021/la980465r
    • (1999) Langmuir , vol.15 , pp. 2450-2459
    • Brooks, C.F.1    Fuller, G.G.2    Frank, C.W.3    Robertson, C.R.4
  • 8
    • 0037453525 scopus 로고    scopus 로고
    • Dilatational rheology of bsa conformers at the air/water interface
    • 10.1021/la020720e
    • Cascào Pereira, L. G., O. Théodoly, H. W. Blanch, and C. J. Radke, Dilatational rheology of bsa conformers at the air/water interface., Langmuir 19, 2349-2356 (2003). 10.1021/la020720e
    • (2003) Langmuir , vol.19 , pp. 2349-2356
    • Cascào Pereira, L.G.1    Théodoly, O.2    Blanch, H.W.3    Radke, C.J.4
  • 9
    • 84855680604 scopus 로고    scopus 로고
    • Deformation modes of complex fluid interfaces
    • 10.1039/c1sm05263b
    • Erni, P., Deformation modes of complex fluid interfaces., Soft Matter 7, 7586-7600 (2011). 10.1039/c1sm05263b
    • (2011) Soft Matter , vol.7 , pp. 7586-7600
    • Erni, P.1
  • 10
    • 84861352737 scopus 로고    scopus 로고
    • Nonlinear viscoelasticity and shear localization at complex fluid interfaces
    • 10.1021/la301023k
    • Erni, P., and A. Parker, Nonlinear viscoelasticity and shear localization at complex fluid interfaces., Langmuir 28, 7757-7767 (2012). 10.1021/la301023k
    • (2012) Langmuir , vol.28 , pp. 7757-7767
    • Erni, P.1    Parker, A.2
  • 11
    • 0344945668 scopus 로고    scopus 로고
    • Stress and strain-controlled measurements of interfacial shear viscosity and viscoelasticity at liquid/liquid and gas/liquid interfaces
    • 10.1063/1.1614433
    • Erni, P., P. Fischer, E. J. Windhab, V. Kusnezov, H. Stettin, and J. Läuger, Stress and strain-controlled measurements of interfacial shear viscosity and viscoelasticity at liquid/liquid and gas/liquid interfaces., Rev. Sci. Instrum. 74, 4916-4924 (2003). 10.1063/1.1614433
    • (2003) Rev. Sci. Instrum. , vol.74 , pp. 4916-4924
    • Erni, P.1    Fischer, P.2    Windhab, E.J.3    Kusnezov, V.4    Stettin, H.5    Läuger, J.6
  • 12
    • 56049098182 scopus 로고    scopus 로고
    • New measures for characterizing nonlinear viscoelasticity in large amplitude oscillatory shear
    • 10.1122/1.2970095
    • Ewoldt, R. H., A. E. Hosoi, and G. H. McKinley, New measures for characterizing nonlinear viscoelasticity in large amplitude oscillatory shear., J. Rheol. 52, 1427-1458 (2008). 10.1122/1.2970095
    • (2008) J. Rheol. , vol.52 , pp. 1427-1458
    • Ewoldt, R.H.1    Hosoi, A.E.2    McKinley, G.H.3
  • 13
    • 34248139762 scopus 로고    scopus 로고
    • Rheological fingerprinting of gastropod pedal mucus and synthetic complex fluids for biomimicking adhesive locomotion
    • 10.1039/b615546d
    • Ewoldt, R. H., C. Clasen, A. E. Hosoi, and G. H. McKinley, Rheological fingerprinting of gastropod pedal mucus and synthetic complex fluids for biomimicking adhesive locomotion., Soft Matter 3, 634-643 (2007). 10.1039/b615546d
    • (2007) Soft Matter , vol.3 , pp. 634-643
    • Ewoldt, R.H.1    Clasen, C.2    Hosoi, A.E.3    McKinley, G.H.4
  • 14
    • 3242778673 scopus 로고    scopus 로고
    • Relaxation of asphaltenes at the toluene/water interface: Diffusion exchange and surface rearrangement
    • 10.1080/00218460490477143
    • Freer, E. M., and C. J. Radke, Relaxation of asphaltenes at the toluene/water interface: Diffusion exchange and surface rearrangement., J. Adhes. 80, 481-496 (2004). 10.1080/00218460490477143
    • (2004) J. Adhes. , vol.80 , pp. 481-496
    • Freer, E.M.1    Radke, C.J.2
  • 15
    • 9644262320 scopus 로고    scopus 로고
    • Oscillating drop/bubble tensiometry: Effect of viscous forces on the measurement of interfacial tension
    • 10.1016/j.jcis.2004.08.058
    • Freer, E. M., H. Wong, and C. J. Radke, Oscillating drop/bubble tensiometry: Effect of viscous forces on the measurement of interfacial tension., J. Colloid Interface Sci. 282, 128-132 (2005). 10.1016/j.jcis.2004.08. 058
    • (2005) J. Colloid Interface Sci. , vol.282 , pp. 128-132
    • Freer, E.M.1    Wong, H.2    Radke, C.J.3
  • 16
    • 9144241823 scopus 로고    scopus 로고
    • Shear and dilatational relaxation mechanisms of globular and flexible proteins at the hexadecane/water interface
    • 10.1021/la0485226
    • Freer, E. M., K. S. Yim, G. G. Fuller, and C. J. Radke, Shear and dilatational relaxation mechanisms of globular and flexible proteins at the hexadecane/water interface., Langmuir 20, 10159-10167 (2004). 10.1021/la0485226
    • (2004) Langmuir , vol.20 , pp. 10159-10167
    • Freer, E.M.1    Yim, K.S.2    Fuller, G.G.3    Radke, C.J.4
  • 17
    • 80055082610 scopus 로고    scopus 로고
    • A review of nonlinear oscillatory shear tests: Analysis and application of large amplitude oscillatory shear (laos)
    • 10.1016/j.progpolymsci.2011.02.002
    • Hyun, K., M. Wilhelm, C. O. Klein, K. S. Cho, J. G. Nam, K. H. Ahn, S. J. Lee, R. H. Ewoldt, and G. H. McKinley, A review of nonlinear oscillatory shear tests: Analysis and application of large amplitude oscillatory shear (laos)., Prog. Polym. Sci. 36, 1697-1753 (2011). 10.1016/j.progpolymsci.2011.02.002
    • (2011) Prog. Polym. Sci. , vol.36 , pp. 1697-1753
    • Hyun, K.1    Wilhelm, M.2    Klein, C.O.3    Cho, K.S.4    Nam, J.G.5    Ahn, K.H.6    Lee, S.J.7    Ewoldt, R.H.8    McKinley, G.H.9
  • 18
    • 0037032767 scopus 로고    scopus 로고
    • Large amplitude oscillatory shear as away to classify the complex fluid
    • 10.1016/S0377-0257(02)00141-6
    • Hyun, K., S. H. Kim, K. Ahn, and S. Lee, Large amplitude oscillatory shear as away to classify the complex fluid., J. Non-Newtonian Fluid Mech. 107, 51-65 (2002). 10.1016/S0377-0257(02)00141-6
    • (2002) J. Non-Newtonian Fluid Mech. , vol.107 , pp. 51-65
    • Hyun, K.1    Kim, S.H.2    Ahn, K.3    Lee, S.4
  • 19
    • 80052536942 scopus 로고    scopus 로고
    • Unravelling adsorption and alignment of amyloid fibrils at interfaces by probe particle tracking
    • 10.1039/c1sm05602f
    • Isa, L., J.-M. Jung, and R. Mezzenga, Unravelling adsorption and alignment of amyloid fibrils at interfaces by probe particle tracking., Soft Matter 7, 8127-8134 (2011). 10.1039/c1sm05602f
    • (2011) Soft Matter , vol.7 , pp. 8127-8134
    • Isa, L.1    Jung, J.-M.2    Mezzenga, R.3
  • 20
    • 78650386372 scopus 로고    scopus 로고
    • Fibrillation of β-lactoglobulin at low ph in the presence of a complexing anionic polysaccharide
    • 10.1021/la1026619
    • Jones, O. G., J. Adamcik, S. Handschin, S. Bolisetty, and R. Mezzenga, Fibrillation of β-lactoglobulin at low ph in the presence of a complexing anionic polysaccharide., Langmuir 26, 17449-17458 (2010). 10.1021/la1026619
    • (2010) Langmuir , vol.26 , pp. 17449-17458
    • Jones, O.G.1    Adamcik, J.2    Handschin, S.3    Bolisetty, S.4    Mezzenga, R.5
  • 21
    • 84855445083 scopus 로고    scopus 로고
    • Inhibiting, promoting, and preserving stability of functional protein fibrils
    • 10.1039/c1sm06643a
    • Jones, O. G., and R. Mezzenga, Inhibiting, promoting, and preserving stability of functional protein fibrils., Soft Matter 8, 876-895 (2012). 10.1039/c1sm06643a
    • (2012) Soft Matter , vol.8 , pp. 876-895
    • Jones, O.G.1    Mezzenga, R.2
  • 22
    • 80051507370 scopus 로고    scopus 로고
    • Complexation of β-lactoglobulin fibrils and sulfated polysaccharides
    • 10.1021/bm200686r
    • Jones, O. G., S. Handschin, J. Adamcik, L. Harnau, S. Bolisetty, and R. Mezzenga, Complexation of β-lactoglobulin fibrils and sulfated polysaccharides., Biomacromolecules 12, 3056-3065 (2011). 10.1021/bm200686r
    • (2011) Biomacromolecules , vol.12 , pp. 3056-3065
    • Jones, O.G.1    Handschin, S.2    Adamcik, J.3    Harnau, L.4    Bolisetty, S.5    Mezzenga, R.6
  • 23
    • 78651345777 scopus 로고    scopus 로고
    • Disassembly and reassembly of amyloid fibrils in water ethanol mixtures
    • 10.1021/bm101119t
    • Jordens, S., J. Adamcik, I. Amar-Yuli, and R. Mezzenga, Disassembly and reassembly of amyloid fibrils in water ethanol mixtures., Biomacromolecules 12, 187-193 (2011). 10.1021/bm101119t
    • (2011) Biomacromolecules , vol.12 , pp. 187-193
    • Jordens, S.1    Adamcik, J.2    Amar-Yuli, I.3    Mezzenga, R.4
  • 24
    • 79952112477 scopus 로고    scopus 로고
    • Interfacial activity and interfacial shear rheology of native β-lactoglobulin monomers and their heat-induced fibers
    • 10.1021/la102721m
    • Jung, J.-M., D. Z. Gunes, and R. Mezzenga, Interfacial activity and interfacial shear rheology of native β-lactoglobulin monomers and their heat-induced fibers., Langmuir 26, 15366-15375 (2010). 10.1021/la102721m
    • (2010) Langmuir , vol.26 , pp. 15366-15375
    • Jung, J.-M.1    Gunes, D.Z.2    Mezzenga, R.3
  • 25
    • 52649129277 scopus 로고    scopus 로고
    • Structure of heat induced β-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate
    • 10.1021/bm800502j
    • Jung, J.-M., G. Savin, M. Pouzot, C. Schmitt, and R. Mezzenga, Structure of heat induced β-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate., Biomacromolecules 9, 2477-2486 (2008). 10.1021/bm800502j
    • (2008) Biomacromolecules , vol.9 , pp. 2477-2486
    • Jung, J.-M.1    Savin, G.2    Pouzot, M.3    Schmitt, C.4    Mezzenga, R.5
  • 26
    • 73649116661 scopus 로고    scopus 로고
    • Liquid crystalline phase behavior of protein fibres in water: Experiments versus theory
    • Jung, J.-M., and R. Mezzenga, Liquid crystalline phase behavior of protein fibres in water: Experiments versus theory., Langmuir 26 (1), 504-514 (2009).
    • (2009) Langmuir , vol.26 , Issue.1 , pp. 504-514
    • Jung, J.-M.1    Mezzenga, R.2
  • 27
    • 4243120936 scopus 로고    scopus 로고
    • Invited review: Beta-lactoglobulin: Binding properties, structure, and function
    • 10.3168/jds.S0022-0302(04)73222-1
    • Kontopidis, G., C. Holt, and L. Sawyer, Invited review: Beta-lactoglobulin: Binding properties, structure, and function., J. Dairy Sci. 87, 785-796 (2004). 10.3168/jds.S0022-0302(04)73222-1
    • (2004) J. Dairy Sci. , vol.87 , pp. 785-796
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 28
    • 79955863547 scopus 로고    scopus 로고
    • General self-assembly mechanism converting hydrolyzed globular proteins into giant multistranded amyloid ribbons
    • 10.1021/bm200216u
    • Lara, C., J. Adamcik, S. Jordens, and R. Mezzenga, General self-assembly mechanism converting hydrolyzed globular proteins into giant multistranded amyloid ribbons., Biomacromolecules 12, 1868-1875 (2011). 10.1021/bm200216u
    • (2011) Biomacromolecules , vol.12 , pp. 1868-1875
    • Lara, C.1    Adamcik, J.2    Jordens, S.3    Mezzenga, R.4
  • 30
    • 77957928572 scopus 로고    scopus 로고
    • Effect of gastric conditions on β-lactoglobulin interfacial networks: Influence of the oil phase on protein structure
    • 10.1021/la102294u
    • Maldonado-Valderrama, J., R. Miller, V. B. Fainerman, P. J. Wilde, and V. J. Morris, Effect of gastric conditions on β-lactoglobulin interfacial networks: Influence of the oil phase on protein structure., Langmuir 26, 15901-15908 (2010). 10.1021/la102294u
    • (2010) Langmuir , vol.26 , pp. 15901-15908
    • Maldonado-Valderrama, J.1    Miller, R.2    Fainerman, V.B.3    Wilde, P.J.4    Morris, V.J.5
  • 31
    • 77954279639 scopus 로고    scopus 로고
    • Effects of charge double layer and colloidal aggregation on the isotropic-nematic transition of protein fibers in water
    • 10.1021/la101636r
    • Mezzenga, R., J.-M. Jung, and J. Adamcik, Effects of charge double layer and colloidal aggregation on the isotropic-nematic transition of protein fibers in water., Langmuir 26, 10401-10405 (2010). 10.1021/la101636r
    • (2010) Langmuir , vol.26 , pp. 10401-10405
    • Mezzenga, R.1    Jung, J.-M.2    Adamcik, J.3
  • 32
    • 84875939276 scopus 로고    scopus 로고
    • The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions
    • 10.1088/0034-4885/76/4/046601
    • Mezzenga, R., and P. Fischer, The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions., Rep. Prog. Phys. 76, 046601 (2013). 10.1088/0034-4885/76/4/046601
    • (2013) Rep. Prog. Phys. , vol.76 , pp. 046601
    • Mezzenga, R.1    Fischer, P.2
  • 33
    • 25444522601 scopus 로고    scopus 로고
    • Thermodynamics of a(140) amyloid fibril elongation
    • 10.1021/bi050927h
    • ONuallain, B., S. Shivaprasad, I. Kheterpal, and R. Wetzel, Thermodynamics of a(140) amyloid fibril elongation., Biochemistry 44, 12709-12718 (2005). 10.1021/bi050927h
    • (2005) Biochemistry , vol.44 , pp. 12709-12718
    • Onuallain, B.1    Shivaprasad, S.2    Kheterpal, I.3    Wetzel, R.4
  • 34
    • 77954027906 scopus 로고    scopus 로고
    • Interfacial dilational rheology by oscillating bubble/drop methods
    • 10.1016/j.cocis.2010.04.001
    • Ravera, F., G. Loglio, and V. I. Kovalchuk, Interfacial dilational rheology by oscillating bubble/drop methods., Curr. Opin. Colloid Interface Sci. 15, 217-228 (2010). 10.1016/j.cocis.2010.04.001
    • (2010) Curr. Opin. Colloid Interface Sci. , vol.15 , pp. 217-228
    • Ravera, F.1    Loglio, G.2    Kovalchuk, V.I.3
  • 35
    • 27944432163 scopus 로고    scopus 로고
    • Influence of surface processes on the dilational visco-elasticity of surfactant solutions
    • 10.1016/j.cis.2005.06.002
    • Ravera, F., M. Ferrari, E. Santini, and L. Liggieri, Influence of surface processes on the dilational visco-elasticity of surfactant solutions., Adv. Colloid Interface Sci. 117, 75-100 (2005). 10.1016/j.cis.2005.06.002
    • (2005) Adv. Colloid Interface Sci. , vol.117 , pp. 75-100
    • Ravera, F.1    Ferrari, M.2    Santini, E.3    Liggieri, L.4
  • 36
    • 0034029210 scopus 로고    scopus 로고
    • Interfacial shear rheology of aged and heat-treated β-lactoglobulin films: Displacement by nonionic surfactant
    • 10.1021/jf990976z
    • Roth, S., B. S. Murray, and E. Dickinson, Interfacial shear rheology of aged and heat-treated β-lactoglobulin films: Displacement by nonionic surfactant., J. Agric. Food Chem. 48, 1491-1497 (2000). 10.1021/jf990976z
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 1491-1497
    • Roth, S.1    Murray, B.S.2    Dickinson, E.3
  • 37
    • 84867525281 scopus 로고    scopus 로고
    • Simultaneous control of ph and ionic strength during interfacial rheology of β-lactoglobulin fibrils adsorbed at liquid/liquid interfaces
    • 10.1021/la3026705
    • Rühs, P. A., N. Scheuble, E. J. Windhab, R. Mezzenga, and P. Fischer, Simultaneous control of ph and ionic strength during interfacial rheology of β-lactoglobulin fibrils adsorbed at liquid/liquid interfaces., Langmuir 28, 12536-12543 (2012). 10.1021/la3026705
    • (2012) Langmuir , vol.28 , pp. 12536-12543
    • Rühs, P.A.1    Scheuble, N.2    Windhab, E.J.3    Mezzenga, R.4    Fischer, P.5
  • 38
    • 83055180326 scopus 로고    scopus 로고
    • Dynamic properties of interfaces in soft matter: Experiments and theory
    • 10.1103/RevModPhys.83.1367
    • Sagis, L. M. C., Dynamic properties of interfaces in soft matter: Experiments and theory., Rev. Mod. Phys. 83, 1367-1403 (2011). 10.1103/RevModPhys.83.1367
    • (2011) Rev. Mod. Phys. , vol.83 , pp. 1367-1403
    • Sagis, L.M.C.1
  • 39
    • 77949270264 scopus 로고    scopus 로고
    • A double wall-ring geometry for interfacial shear rheometry
    • 10.1007/s00397-009-0407-3
    • Vandebril, S., A. Franck, G. Fuller, P. Moldenaers, and J. Vermant, A double wall-ring geometry for interfacial shear rheometry., Rheol. Acta 49, 131-144 (2010). 10.1007/s00397-009-0407-3
    • (2010) Rheol. Acta , vol.49 , pp. 131-144
    • Vandebril, S.1    Franck, A.2    Fuller, G.3    Moldenaers, P.4    Vermant, J.5
  • 40
    • 18844398622 scopus 로고    scopus 로고
    • Interfacial dilatational elasticity and viscosity of β-lactoglobulin at air-water interface using pulsating bubble tensiometry
    • 10.1021/la047374g
    • Wang, Z., and G. Narsimhan, Interfacial dilatational elasticity and viscosity of β-lactoglobulin at air-water interface using pulsating bubble tensiometry., Langmuir 21, 4482-4489 (2005). 10.1021/la047374g
    • (2005) Langmuir , vol.21 , pp. 4482-4489
    • Wang, Z.1    Narsimhan, G.2
  • 41
    • 33749824175 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of amyloid fibril assembly
    • 10.1021/ar050069h
    • Wetzel, R., Kinetics and thermodynamics of amyloid fibril assembly., Acc. Chem. Res. 39, 671-679 (2006). 10.1021/ar050069h
    • (2006) Acc. Chem. Res. , vol.39 , pp. 671-679
    • Wetzel, R.1
  • 42
    • 31544451797 scopus 로고    scopus 로고
    • Shear effects in interfacial rheology and their implications on oscillating pendant drop experiments
    • 10.1021/la051795w
    • Yeung, A., and L. Zhang, Shear effects in interfacial rheology and their implications on oscillating pendant drop experiments., Langmuir 22, 693-701 (2006). 10.1021/la051795w
    • (2006) Langmuir , vol.22 , pp. 693-701
    • Yeung, A.1    Zhang, L.2
  • 43
    • 0031272461 scopus 로고    scopus 로고
    • Dissipative interfaces and departures from the Young Laplace equation
    • 10.1021/la9706835
    • Yeung, A., T. Dabros, and J. Masliyah, Dissipative interfaces and departures from the Young Laplace equation., Langmuir 13, 6597-6606 (1997). 10.1021/la9706835
    • (1997) Langmuir , vol.13 , pp. 6597-6606
    • Yeung, A.1    Dabros, T.2    Masliyah, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.