Five N-substituted acrylamides were prepared by reaction of substituted aromatic primary amines with acryloyl chloride in the presence of triethyl amine. The synthesized acrylamides were allowed to introduce copolymerization reaction with three vinylic monomers including acrylonitrile, methyl acrylate and methyl methacrylate respectively to obtain eleven new copolymers having different physical properties which may used in different applications.

   The removal of Ibuprofen antibiotics (IBU) by photo-degradation UV/H₂O₂/Fe⁺² system was investigated in a batch reactor under different initial concentrations of H₂O₂ (100-500) mg/L, Fe⁺² (10-40) mg/L, pH (3-9) and initial concentrations of IBU (10-80) mg/L, and their relationship with the degradation efficiency were studied. The result demonstrated that the maximum elimination of IBU was 85.54% achieved at 300 mg/L of H₂O₂, 30 mg/L of Fe⁺², pH=3, and irradiation time of 150 min, for 10 mg/L of IBU. The results have shown that the oxidation reagent H₂O₂ plays a very important role in IBU degradation.

Cholinesterases are among the most efficient enzymes known. They are divided into two groups: acetylcholinesterase (AChE) involved in the hydrolysis of the neurotransimitter acetylcholine, and butyrylcholinesterase (BChE) of unknown function. Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge. Human BChE has attracted attention because it can hydrolyze toxic esters and nerve agents. Here we analyze the complexes of cholinesterase with soman by describing the 3D geometry of the complex, the active site, the changes happened through the inhibition and provide a description for the mechanism of inhibition. Soman undergoes degradation in the active site of the AChE and B

Cholinesterases are among the most efficient enzymes known. They are divided into two groups: acetylcholinesterase (AChE) involved in the hydrolysis of the neurotransimitter acetylcholine, and butyrylcholinesterase (BChE) of unknown function. Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge. Human BChE has attracted attention because it can hydrolyze toxic esters and nerve agents. Here we analyze the complexes of cholinesterase with soman by describing the 3D geometry of the complex, the active site, the changes happened through the inhibition and provide a description for the mechanism of inhibition. Soman undergoes degradation in the active site of the AChE and BC

N-type Tin dioxide thin films with thickness (350 nm) prepared by thermal evaporation method. The thin film SnO2 was doped with Ag by the rate (0.01, 0.02 and 0.03). Atomic Force Microscopic (AFM) was adopted to determine the grain size and roughness of the film surface. The electrical properties were determined by mean of Hall Measurement system and mobility was calculated. SnO2: Ag/P–Si photodetectors demonstration the highest described visible responsivity of (0.287 A/W) with the Ag ratio of (0.03). I–V characteristics with different power density were measured. The best sensitive value of the spectral response, specific detectivity and quantum efficiency at wavelength (422 nm).