A confined bicontinuous CE-DO--octane microemulsion is studied using neutron spin echo spectroscopy (NSE). Controlled pore glasses serve as confining matrices with pore diameters ranging from 24 to 112 nm. Firstly, the microemulsion in bulk is investigated by NSE and dynamic light scattering, which allows the determination of the unperturbed collective dynamics as well as the observation of the undulation of the surfactant film.
View Article and Find Full Text PDFA mathematical model is developed to jointly analyze elastic and inelastic scattering data of fluctuating membranes within a single theoretical framework. The model builds on a nonhomogeneously clipped time-dependent Gaussian random field. This specific approach provides one with general analytical expressions for the intermediate scattering function for any number of sublayers in the membrane and arbitrary contrasts.
View Article and Find Full Text PDFWhile Ising criticality in classical liquids has been firmly established both theoretically and experimentally, much less is known about criticality in liquids in which the growth of the correlation length is frustrated by finite-size effects. A theoretical approach for dealing with this issue is the random-field Ising model (RFIM). While experimental critical-exponent values have been reported for magnetic samples (here, we consider γ, ν and η), little experimental information is available for critical fluctuations in corresponding liquid systems.
View Article and Find Full Text PDFCrowding effects significantly influence the phase behavior and the structural and dynamic properties of the concentrated protein mixtures present in the cytoplasm of cells or in the blood serum. This poses enormous difficulties for our theoretical understanding and our ability to predict the behavior of these systems. While the use of course grained colloid-inspired models allows us to reproduce the key physical solution properties of concentrated monodisperse solutions of individual proteins, we lack corresponding theories for complex polydisperse mixtures.
View Article and Find Full Text PDFHypothesis: To analyze protein stabilized emulsions, SAXS and SANS are emerging techniques capturing oil droplet radius, interfacial coverage and structure. Protein shape, thus protein structure change during interfacial adsorption with partial protein unfolding is detected via SAXS analysis at and below the monolayer concentration for proteins, known as critical interfacial concentration (CIC). SANS determines the same phenomena below and above the CIC, via contrast variation and coarse-grained modelling.
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