Scaling in Late Stage Spinodal Decomposition with Quenched Disorder

We study the late stages of spinodal decomposition in a Ginzburg-Landau mean field model with quenched disorder. Random spatial dependence in the coupling constants is introduced to model the quenched disorder. The effect of the disorder on the scaling of the structure factor and on the domain growth is investigated in both the zero temperature limit and at finite temperature. In particular, we find that at zero temperature the domain size, $R(t)$, scales with the amplitude, $A$, of the quenched disorder as $R(t) = A^{-\beta} f(t/A^{-\gamma})$ with $\beta \simeq 1.0$ and $\gamma \simeq 3.0$ in two dimensions. We show that $\beta/\gamma = \alpha$, where $\alpha$ is the Lifshitz-Slyosov exponent. At finite temperature, this simple scaling is not observed and we suggest that the scaling also depends on temperature and $A$. We discuss these results in the context of Monte Carlo and cell dynamical models for phase separation in systems with quenched disorder, and propose that in a Monte Carlo simulation the concentration of impurities, $c$, is related to $A$ by $A \sim c^{1/d}$.Comment: RevTex manuscript 5 pages and 5 figures (obtained upon request via email [email protected]

Effect of Ordering on Spinodal Decomposition of Liquid-Crystal/Polymer Mixtures

Partially phase-separated liquid-crystal/polymer dispersions display highly fibrillar domain morphologies that are dramatically different from the typical structures found in isotropic mixtures. To explain this, we numerically explore the coupling between phase ordering and phase separation kinetics in model two-dimensional fluid mixtures phase separating into a nematic phase, rich in liquid crystal, coexisting with an isotropic phase, rich in polymer. We find that phase ordering can lead to fibrillar networks of the minority polymer-rich phase

Novel Myosin Heavy Chain Kinase Involved in Disassembly of Myosin II Filaments and Efficient Cleavage in Mitotic Dictyostelium Cells

We have cloned a full-length cDNA encoding a novel myosin II heavy chain kinase (mhckC) from Dictyostelium. Like other members of the myosin heavy chain kinase family, the mhckC gene product, MHCK C, has a kinase domain in its N-terminal half and six WD repeats in the C-terminal half. GFP-MHCK C fusion protein localized to the cortex of interphase cells, to the cleavage furrow of mitotic cells, and to the posterior of migrating cells. These distributions of GFP-MHCK C always corresponded with that of myosin II filaments and were not observed in myosin II-null cells, where GFP-MHCK C was diffusely distributed in the cytoplasm. Thus, localization of MHCK C seems to be myosin II-dependent. Cells lacking the mhckC gene exhibited excessive aggregation of myosin II filaments in the cleavage furrows and in the posteriors of the daughter cells once cleavage was complete. The cleavage process of these cells took longer than that of wild-type cells. Taken together, these findings suggest MHCK C drives the disassembly of myosin II filaments for efficient cytokinesis and recycling of myosin II that occurs during cytokinesis