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Université de Fribourg

Gelation, phase behavior, and dynamics of β-Lactoglobulin amyloid fibrils at varying concentrations and ionic strengths

Bolisetty, Sreenath ; Harnau, Ludger ; Jung, Jin-mi ; Mezzenga, Raffaele

In: Biomacromolecules, 2012, vol. 13, no. 10, p. 3241–3252

We have investigated the thermodynamic and dynamic behavior of multistranded β-lactoglobulin protein fibrils in water, by combining static, dynamic, and depolarized dynamic light scattering (SLS, DLS, DDLS), small angle neutron scattering (SANS), rheology, and cryogenic transmission electron microscopy (cryo-TEM). We focus on the region of the phase diagram at which ionic strength and...

Université de Fribourg

Unravelling adsorption and alignment of amyloid fibrils at interfaces by probe particle tracking

Isa, Lucio ; Jung, Jin-Mi ; Mezzenga, Raffaele

In: Soft Matter, 2011, vol. 7, p. 8127-8134

We report the first direct, non-invasive experimental evidence of a 2D isotropic–nematic transition for highly anisotropic nanoparticles at liquid–liquid interfaces by using passive fluorescent particle tracking. In order to illustrate the potential of this approach on systems of high real practical and biological relevance, we select as a model anisotropic nanoparticles β-lactoglobulin...

Université de Fribourg

Interfacial activity and interfacial shear rheology of native ß-lactoglobulin monomers and their heat-induced fibers

Jung, Jin-Mi ; Zeynel Gunes, Deniz ; Mezzenga, Raffaele

In: Langmuir, 2010, vol. 26, no. 19, p. 15366–15375

Interfacial properties of native β-lactoglobulin monomers and their heat-induced fibers, of two different lengths, were investigated at pH 2, through surface tension measurements at water−air and water−oil interfaces and interfacial shear rheology at the water−oil interface. The applied heat treatment generates a mixed system of fibers with unconverted monomers and hydrolyzed peptides. The...

Université de Fribourg

Understanding amyloid aggregation by statistical analysis of atomic force microscopy images

Adamcik, Jozef ; Jung, Jin-Mi ; Flakowski, Jérôme ; Rios, Paolo De Los ; Dietler, Giovanni ; Mezzenga, Raffaele

In: Nature Nanotechnology, 2010, vol. 5, p. 423 - 428

The aggregation of proteins is central to many aspects of daily life, including food processing, blood coagulation, eye cataract formation disease and prion-related neurodegenerative infections. However, the physical mechanisms responsible for amyloidosis—the irreversible fibril formation of various proteins that is linked to disorders such as Alzheimer's, Creutzfeldt–Jakob and Huntington's...

Université de Fribourg

Effects of charge double layer and colloidal aggregation on the isotropic-nematic transition of protein fibers in water

Mezzenga, Raffaele ; Jung, Jin-Mi ; Adamcik, Jozef

In: Langmuir, 2010, vol. 26, no. 13, p. 10401–10405

We investigate the effects of variable linear charge density and Debye length on the mesoscopic properties of β-lactoglobulin fibers in water, by changing the pH and ionic strength, respectively. We determine the isotropic−nematic (I−N) transition by cross-polarized microscopy and quantify by atomic force microscopy the increasing tendency of the fibers to aggregate upon raising ionic...

Université de Fribourg

Liquid crystalline phase behavior of protein fibers in water: experiments versus theory

Jung, Jin-Mi ; Mezzenga, Raffaele

In: Langmuir, 2010, vol. 26, no. 1, p. 504–514

We have developed a new method allowing the study of the thermodynamic phase behavior of mesoscopic colloidal systems consisting of amyloid protein fibers in water, obtained by heat denaturation and aggregation of β-lactoglobulin, a dairy protein. The fibers have a cross section of about 5.2 nm and two groups of polydisperse contour lengths: (i) long fibers of 1−20 μm, showing semiflexible...

Université de Fribourg

Structure of heat-induced β-lactoglobulin aggregates and their complexes with sodium-sodecyl sulfate

Jung, Jin-Mi ; Savin, Gabriela ; Pouzot, Matthieu ; Schmitt, Christophe ; Mezzenga, Raffaele

In: Biomacromolecules, 2008, vol. 9, no. 9, p. 2477–2486

We report on the conformation of heat-induced bovine β-lactoglobulin (βlg) aggregates prepared at different pH conditions, and their complexes with model anionic surfactants such as sodium dodecyl sulfate (SDS). The investigation was carried out by combining a wide range of techniques such as ultra small angle light scattering, static and dynamic light scattering, small angle neutron...