Wetting behavior in the inertial phase of droplet impacts onto sub-millimeter microstructured surfaces.

Hypothesis: The shape of the wetted region after a droplet impact can vary significantly even in the early phase of the process. How much of the early spreading process occurs within the structures versus above the structures, flow regimes and local wetting at groove intersections can have effects on the sizes and shapes of the final wetted regions. Experiments and simulations: We experimentally study droplet impacts onto cubic pillars with , and side length, height and separation.

Structural Basis for Aryl Hydrocarbon Receptor-Mediated Gene Activation.

The aryl hydrocarbon receptor (AHR) and the AHR nuclear translocator (ARNT) constitute a heterodimeric basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain containing transcription factor with central functions in development and cellular homeostasis. AHR is activated by xenobiotics, notably dioxin, as well as by exogenous and endogenous metabolites. Modulation of AHR activity holds promise for the treatment of diseases featuring altered cellular homeostasis, such as cancer or autoimmune disorders.

Visual Analysis of Inclusion Dynamics in Two-Phase Flow.

In single-phase flow visualization, research focuses on the analysis of vector field properties. In two-phase flow, in contrast, analysis of the phase components is typically of major interest. So far, visualization research of two-phase flow concentrated on proper interface reconstruction and the analysis thereof.

The immunity-related GTPase Irga6 dimerizes in a parallel head-to-head fashion.

Background: The immunity-related GTPases (IRGs) constitute a powerful cell-autonomous resistance system against several intracellular pathogens. Irga6 is a dynamin-like protein that oligomerizes at the parasitophorous vacuolar membrane (PVM) of Toxoplasma gondii leading to its vesiculation. Based on a previous biochemical analysis, it has been proposed that the GTPase domains of Irga6 dimerize in an antiparallel fashion during oligomerization.