2 research outputs found
Recent Developments in Modeling Heteroepitaxy/Heterogeneous Nucleation by Dynamical Density Functional Theory
Crystallization of supersaturated liquids usually starts by epitaxial growth or by heterogeneous
nucleation on foreign surfaces. Herein, we review recent advances made in modeling
heteroepitaxy and heterogeneous nucleation on flat/modulated surfaces and nanoparticles
within the framework of a simple dynamical density functional theory, known as the phase-field
crystal model. It will be shown that the contact angle and the nucleation barrier are nonmonotonous
functions of the lattice mismatch between the substrate and the crystalline phase.
In continuous cooling studies for substrates with lattice mismatch, we recover qualitatively the
Matthews–Blakeslee mechanism of stress release via the misfit dislocations. The simulations
performed for particle-induced freezing will be confronted with recent analytical results,
exploring thus the validity range of the latter. It will be demonstrated that time-dependent
studies are essential, as investigations based on equilibrium properties often cannot identify the
preferred nucleation pathways. Modeling of these phenomena is essential for designing materials
on the basis of controlled nucleation and/or nano-patterning
Chimera proteins with affinity for membranes and microtubule tips polarize in the membrane of fission yeast cells
Cell polarity refers to a functional spatial organization of proteins that is crucial for the control of essential cellular processes such as growth and division. To establish polarity, cells rely on elaborate regulation networks that control the distribution of proteins at the cell membrane. In fission yeast cells, a microtubule-dependent network has been identified that polarizes the distribution of signaling proteins that restricts growth to cell ends and targets the cytokinetic machinery to the middle of the cell. Although many molecular components have been shown to play a role in this network, it remains unknown which molecular functionalities are minimally required to establish a polarized protein distribution in this system. Here we show that a membrane-binding protein fragment, which distributes homogeneously in wild-type fission yeast cells, can be made to concentrate at cell ends by attaching it to a cytoplasmic microtubule end-binding protein. This concentration results in a polarized pattern of chimera proteins with a spatial extension that is very reminiscent of natural polarity patterns in fission yeast. However, chimera levels fluctuate in response to microtubule dynamics, and disruption of microtubules leads to disappearance of the pattern. Numerical simulations confirm that the combined functionality of membrane anchoring and microtubule tip affinity is in principle sufficient to create polarized patterns. Our chimera protein may thus represent a simple molecular functionality that is able to polarize the membrane, onto which additional layers of molecular complexity may be built to provide the temporal robustness that is typical of natural polarity patterns.BN/BionanoscienceBN/Marileen Dogterom La