Dr. Remco Tuinier Scientist at IFF-Institute: Soft Matter (Weiche Materie) Project-leader: Biomacromolecules
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Institut für Festkörperforschung
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Curriculum Vitae of Remco Tuinier | ||||||||||||
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Research Interests of R. Tuinier |
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My interests are the physical properties of colloids, and polymers, and their biological analogues: polysaccharides and proteins, their interactions and properties such as phase behavior. The experimental techniques that have my main interest are scattering techniques, both dynamic and static, using light, X-Rays or neutrons. Theoretically, I am attracted to depletion type of interactions (see refs 1,4,6,9,11,13). These types of interactions play an important role in mixed biopolymer systems. My Project is briefly described below:
Segregative interaction in dispersions with charged particles Mixing biomacromolecules may lead to instability due to segregative or associative interactions. If proteins are mixed with polysaccharides, often a segregative interaction occurs and the resulting properties can be explained in terms of depletion interaction. The depletion mechanism has been used successfully over the last decades to describe the phase behavior of polymer-colloid mixtures of which protein-polysaccharide mixtures are a specific example. So far, theories mainly consider uncharged mixed colloids and polymers. Proteins (and polysaccharides) however are (often) charged and the effect of these charges together with depletion is not well understood. Therefore, theories have to be developed in order to describe polyelectrolyte depletion. These theories can be tested with total internal reflection microscopy (TIRM) (in collaboration with Dr. P. Lang), which allows a direct measurement of the force between a sphere and a plate. A thorough understanding of polyelectrolyte depletion and the effects of charges on the biocolloids will make it possible to describe the phase behavior of charged polysaccharides mixed with biocolloids. Aggregation, gelation, and influence of attractions in lysozyme dispersions The aggregation of proteins is relevant in several practical systems. For instance food products, often containing proteins, undergo a heat treatment when sterilized or pasteurized. During those treatments proteins tend to denature and subsequently aggregate. This process affects the final properties of a product. The aggregation of proteins may, in the later stages, also result in gelation. The aggregation process can thus be used to build structures. The aggregation process of lysozyme will be studied as a function of pH and temperature and the aggregated particles will be analyzed with scattering techniques. The transition from a dispersion of aggregated particles toward gelation will be studied and compared with theory and computer simulation results. The effect of non-adsorbing polymer on dispersions with aggregated lysozyme, and on gelation is another point of interest. Adding non-adsorbing polymer leads to phase separation and the kinetics of phase separation will be investigated. The effect of non-adsorbing polymer on protein gelation still poorly understood. Scattering techniques will be important tools in order to understand lysozyme aggregation and gelation (in presence of polymers).
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Forschungszentrum Jülich, IFF, wwwiff@fz-juelich.de
Letzte Änderung: 15/10/2003, 12.54 URL: <http://www.fz-juelich.de /iff/personen/R.Tuinier/index.shtml> |