2,2′‐Dinitramino‐5,5′‐bi(1‐oxa‐3,4‐diazole) (2) is a new highly energetic material with superior calculated detonation performance in comparison to cyclo‐1,3,5‐trimethylene‐2,4,6‐trinitramine (RDX) and penta‐erythritoltetranitrate (PETN) and can be prepared by an economical and practical two‐step synthesis. The starting material 2,2′‐diamino‐5,5′‐bi(1‐oxa‐3,4‐diazole) (1) is synthesized by the reaction of oxalyl dihydrazide with cyanogen bromide. Nitration of 1 yields the title compound in perfect yield and purity. The combination of its high density of 1.986 g cm−3, the positive heat of formation (+190 kJ mol−1), and a slightly positive oxygen balance (+6.2 %) results in ideal calculated detonation parameters (e.g. detonation velocity 9296 m s−1). The sensitivities toward impact and friction can be adjusted by deprotonation and formation of corresponding nitrogen‐rich salts, for example, ammonium (3), hydroxylammonium (4), and guanidinium (5) salts.

The formation of protein patterns inside cells is generically described by reaction-diffusion models.The study of such systems goes back to Turing, who showed how patterns can emerge from a homogenous steady state when two reactive components have different diffusivities (e.g. membranebound and cytosolic states). However, in nature, systems typically develop in a heterogeneous environment, where upstream protein patterns affect the formation of protein patterns downstream. Examples for this are the polarization of Cdc42 adjacent to the previous bud-site in budding yeast, and the formation of an actin-recruiter ring that forms around a PIP3 domain in macropinocytosis. This suggests that previously established protein patterns can serve as a template for downstream proteins and that these downstream proteins can 'sense' the edge of the template. A mechanism for how this edge sensing may work remains elusive.Here we demonstrate and analyze a generic and robust edge-sensing mechanism, based on a twocomponent mass-conserving reaction-diffusion (McRD) model. Our analysis is rooted in a recently developed theoretical framework for McRD systems, termed local equilibria theory. We extend this framework to capture the spatially heterogeneous reaction kinetics due to the template. This enables us to graphically construct the stationary patterns in the phase space of the reaction kinetics. Furthermore, we show that the protein template can trigger a regional mass-redistribution instability near the template edge, leading to the accumulation of protein mass, which eventually results in a stationary peak at the template edge. We show that simple geometric criteria on the reactive nullcline's shape predict when this edge-sensing mechanism is operational. Thus, our results provide guidance for future studies of biological systems, and for the design of synthetic pattern forming systems. * These three authors contributed equally † frey@lmu.de 1 GTPases are hydrolase enzymes that can bind and hydrolyze guanosine triphosphate (GTP). Ras is a subfamily of small GTPases.

An oxygen- and nitrogen-rich energetic triazole as an excellent example with outstanding performance but high sensitivity, which can be adjusted by the formation of nitrogen-rich salts.

The reaction of a variety of amino-furazans with chlorosulfonyl isocyanate was carried out to synthesize ureido-furazans. The nitration to nitro-ureido-furazan was successful in the case of 3-nitro-4nitroureido-furazan and 3,4-dinitroureido-furazan. Furthermore, furazan derivatives linked to a second amino-oxadiazole were synthesized. All compounds were intensively characterized by X-ray diffraction measurements, NMR spectroscopy, vibrational spectroscopy (IR, Raman), BAM sensitivity tests and differential thermal analysis. The energetic properties were calculated using EXPLO5 6.03.