Shock waves in gas flows with nanoparticles

Journal of Thermal Analysis and Calorimetry - The paper focuses on the analytical analysis of the propagation of a normal shock wave in an adiabatic gas flow with nanoparticles. A modified...     

Effects of external global harmonic influence on chimera states

Nonlinear Dynamics - The effects of the global harmonic force on an ensemble of nonlocally coupled chaotic Rössler oscillators is studied. The autonomous ensemble without external force...     

Asymptotic analysis of the nonsteady micropolar fluid flow through a curved pipe

ABSTRACT

We consider the nonsteady flow of a micropolar fluid in a thin (or long) curved pipe via rigorous asymptotic analysis. Germano's reference system is employed to describe the pipe's geometry. After writing the governing equations in curvilinear coordinates, we construct the asymptotic expansion up to a second order. Obtained in the explicit form, the asymptotic approximation clearly demonstrates the effects of pipe's distortion, micropolarity and the time derivative. A detailed study of the boundary layers in space is provided as well as the construction of the divergence correction. Finally, a rigorous justification of the proposed effective model is given by proving the error estimates.     

Point Mutations of Nicotinic Receptor α1 Subunit Reveal New Molecular Features of G153S Slow-Channel Myasthenia

Slow-channel congenital myasthenic syndromes (SCCMSs) are rare genetic diseases caused by mutations in muscle nicotinic acetylcholine receptor (nAChR) subunits. Most of the known SCCMS-associated mutations localize at the transmembrane region near the ion pore. Only two SCCMS point mutations are at the extracellular domains near the acetylcholine binding site, α1(G153S) being one of them. In this work, a combination of molecular dynamics, targeted mutagenesis, fluorescent Ca²⁺ imaging and patch-clamp electrophysiology has been applied to G153S mutant muscle nAChR to investigate the role of hydrogen bonds formed by Ser 153 with C-loop residues near the acetylcholine-binding site. Introduction of L199T mutation to the C-loop in the vicinity of Ser 153 changed hydrogen bonds distribution, decreased acetylcholine potency (EC₅₀ 2607 vs. 146 nM) of the double mutant and decay kinetics of acetylcholine-evoked cytoplasmic Ca²⁺ rise (τ 14.2 ± 0.3 vs. 34.0 ± 0.4 s). These results shed light on molecular mechanisms of nAChR activation-desensitization and on the involvement of such mechanisms in channelopathy genesis.