Reduced Chemical Kinetic Mechanism for the Oxidation of Methyl Methacrylate in Flames at Atmospheric Pressure

Combustion, Explosion, and Shock Waves - Methyl methacrylate (MMA) is the main pyrolysis product of the widely used polymer polymethyl methacrylate; therefore, a compact mechanism of MMA...     

Dismantling of Active Drains in the Technological Enclosures of the MR Reactor

Atomic Energy - The results of the dismantling of the active drain system and the decontamination of technological enclosures of the loop installations of the MR reactor, which is being...     

Optimal Control of Queuing Systems with Channel Switching

Automation and Remote Control - We consider the problem of optimizing the operation of a queuing system in which the number of working service channels can be changed in a controlled manner at...     

Synthesis and Estimation of Some Surface-Active Compounds Derived from Fused Pyridine as Corrosion Inhibitors for Aluminum in Hydrochloric Acid Solutions

Protection of Metals and Physical Chemistry of Surfaces - Three nonionic surfactants molecules (NS) derived from a fused pyridine characterized by IR and 1HNMR spectra were synthesized and examined...     

Structural insights into peptide self-assembly using photo-induced crosslinking experiments and discontinuous molecular dynamics

Determining the structure of the (oligomeric) intermediates that form during the self-assembly of amyloidogenic peptides is challenging because of their heterogeneous and dynamic nature. Thus, there is need for methodology to analyze the underlying molecular structure of these transient species. In this work, a combination of fluorescence quenching, photo-induced crosslinking (PIC) and molecular dynamics simulation was used to study the assembly of a synthetic amyloid-forming peptide, Aβ_16-22. A PIC amino acid containing a trifluormethyldiazirine (TFMD) group—Fmoc(TFMD)Phe—was incorporated into the sequence (Aβ*_16–22). Electrospray ionization ion-mobility spectrometry mass-spectrometry (ESI-IMS-MS) analysis of the PIC products confirmed that Aβ*_16–22 forms assemblies with the monomers arranged as anti-parallel, in-register β-strands at all time points during the aggregation assay. The assembly process was also monitored separately using fluorescence quenching to profile the fibril assembly reaction. The molecular picture resulting from discontinuous molecule dynamics simulations showed that Aβ_16-22 assembles through a single-step nucleation into a β-sheet fibril in agreement with these experimental observations. This study provides detailed structural insights into the Aβ_16-22 self-assembly processes, paving the way to explore the self-assembly mechanism of larger, more complex peptides, including those whose aggregation is responsible for human disease.     

Combining Solutions of the Axial Assignment Problem

Automation and Remote Control - We consider the NP-hard integer three-index axial assignment problem. The task of optimal combination of the pairs of feasible solutions of the problem is posed, and...     

Theoretical and Experimental Study of the Electrodynamic Properties of Microwave Planar Slot Antennas

Journal of Communications Technology and Electronics - Mathematical models are developed for planar symmetric slot antennas (SAs) with constant slot width using a tensor Green function that takes...     

Using the Extraction–Pyrolysis Method in Synthesis of Bioactive Glass

Theoretical Foundations of Chemical Engineering - The paper focuses on synthesis of bioactive glass with tailored properties achieved by doping it with oxides of different elements. The bioglass...     

Influence of pH on the DSSC Performance of Template Assisted SnO2 Nanostructures

Journal of Inorganic and Organometallic Polymers and Materials - This paper reports the performance of alizarin based SnO2 dye-sensitized solar cells. A novel template assisted method has been...