Flexible Rasch Mixture Models with Package psychomix

Measurement invariance is an important assumption in the Rasch model and mixture models constitute a flexible way of checking for a violation of this assumption by detecting unobserved heterogeneity in item response data. Here, a general class of Rasch mixture models is established and implemented in R, using conditional maximum likelihood estimation of the item parameters (given the raw scores) along with flexible specification of two model building blocks: (1) Mixture weights for the unobserved classes can be treated as model parameters or based on covariates in a concomitant variable model. (2) The distribution of raw score probabilities can be parametrized in two possible ways, either using a saturated model or a specification through mean and variance. The function raschmix() in the R package "psychomix" provides these models, leveraging the general infrastructure for fitting mixture models in the "flexmix" package. Usage of the function and its associated methods is illustrated on artificial data as well as empirical data from a study of verbally aggressive behavior.mixed Rasch model, Rost model, mixture model, flexmix, R

Multi-materials Composites Provide Lightweight Engineering

Sustainability demands materials and energy saving. As a consequence light weight engineered products are a must. This paper approaches the possibility to substitute heavy weight metal design by multi-material light weight design considering polymeric materials and employing manufacturing techniques which are optimal adapted to the materials, e.g. assembly injection moulding. The needed necessary steps for such a development are described and the conceivable result is discussed exemplarily with regard to a novel and weight saving pump housing construction

Investigation on synthesis and properties of isosorbide based bis-GMA analogue

The aim of this work was to synthesize and investigate properties of a novel dimethacrylic monomer based on bioderived alicyclic diol—isosorbide. Its potential as a possible substitute of 2,2-bis[4-(2-hydroxy-3-methacryloyloxypropoxy)phenyl]propane (BISGMA), widely used in dental restorative materials and suspected for toxicity was assessed. The novel monomer was obtained in a three-step synthesis. First, isosorbide was etherified by a Williamson nucleophilic substitution and subsequently oxidized to isosorbide diglycidyl ether (ISDGE). A triphenyl phosphine catalyzed addition of methacrylic acid to ISDGE resulted in 2,5-bis(2-hydroxy-3-methacryloyloxypropoxy)- 1,4:3,6-dianhydro-sorbitol (ISDGMA). The monomer obtained was photopolymerized using camphorquinone/2-(dimethylamino)ethyl methacrylate initiating system. Next, compositions with triethylene glycol dimethacrylate (TEGDMA) were prepared and polymerized. Double bond conversion, polymerization shrinkage and water sorption of resulting polymers were determined. Selected mechanical (flexular strength and modulus, Brinell hardness) and thermomechanical (DMA analysis) properties were also investigated. BISGMA based materials were prepared as reference for comparison of particular properties

The Glycosylphosphatidylinositol-PLC in Trypanosoma brucei Forms a Linear Array on the Exterior of the Flagellar Membrane Before and After Activation

Bloodstream forms of Trypanosoma brucei contain a glycosylphosphatidylinositol-specific phospholipase C (GPI-PLC) that cleaves the GPI-anchor of the variable surface glycoprotein (VSG). Its location in trypanosomes has been controversial. Here, using confocal microscopy and surface labelling techniques, we show that the GPI-PLC is located exclusively in a linear array on the outside of the flagellar membrane, close to the flagellar attachment zone, but does not co-localize with the flagellar attachment zone protein, FAZ1. Consequently, the GPI-PLC and the VSG occupy the same plasma membrane leaflet, which resolves the topological problem associated with the cleavage reaction if the VSG and the GPI-PLC were on opposite sides of the membrane. The exterior location requires the enzyme to be tightly regulated to prevent VSG release under basal conditions. During stimulated VSG release in intact cells, the GPI-PLC did not change location, suggesting that the release mechanism involves lateral diffusion of the VSG in the plane of the membrane to the fixed position of the GPI-PLC