干式变压器有限元仿真模型的电磁和振动分析

随着电力需求的逐年增长,干式变压器的数量也在不断增加。干式变压器在运行时存在着振动和噪声的问题,为了对干式变压器振动的规律与特点进行研究,本文建立了干式变压器本体振动的有限元仿真模型,通过电磁分析获得相应的磁场分布,然后利用结构动力学分析得到其本体振动的相关规律。通过对处于运行状态的变压器振动数据进行实测分析,得到变压器振动的特征频率,然后对仿真结果进行对比分析,可以发现振动幅度与频率之间存在的关系。本文的研究结果可对干式变压器的减振降噪研究提供参考。     

Ionic Conductivity of β‐Cyclodextrin–Polyethylene‐Oxide/Alkali‐Metal‐Salt Complex

Highly conductive, crystalline, polymer electrolytes, β‐cyclodextrin (β‐CD)–polyethylene oxide (PEO)/LiAsF₆ and β‐CD–PEO/NaAsF₆, were prepared through supramolecular self‐assembly of PEO, β‐CD, and LiAsF₆/NaAsF₆. The assembled β‐CDs form nanochannels in which the PEO/X⁺ (X=Li, Na) complexes are confined. The nanochannels provide a pathway for directional motion of the alkali metal ions and, at the same time, separate the cations and the anions by size exclusion.     

From single‐chain folding to polymer nanoparticles via intramolecular quadruple hydrogen‐bonding interaction

Single‐chain folding via intramolecular noncovalent interaction is regarded as a facile mimicry of biomacromolecules. Single‐chain folding and intramolecular crosslinking is also an effective method to prepare polymer nanoparticles. In this study, poly(methyl methacrylate‐co?2‐ureido‐5‐deazapterines functionalized ethylene methacrylate) (P(MMA‐co‐EMA‐DeAP)) is synthesized via free radical polymerization. The single‐chain folding of P(MMA‐co‐EMA‐DeAP) and the formation of the nanoparticles in diluted solution (concentration <0.005 mg/mL) are achieved via supramolecular interaction and intramolecular collapsing during the disruption‐reformation process of the hydrogen bonding triggered by water. The size and the morphology of the nanoparticles are characterized by dynamic light scattering, transmission electron microscope, and atomic force microscope. The results show that the size of the nanoparticles depends on the molecular weight of the polymer and the loading of 2‐ureido‐5‐deazapterines functionalized ethylene methacrylate (EMA‐DeAP) on the polymer backbone. © 2015 Wiley Periodicals, Inc. J. Polym. Sci., Part A: Polym. Chem. 2015 , 53, 1832–1840     

Visible-Light-Mediated Click Chemistry for Highly Regioselective Azide–Alkyne Cycloaddition by a Photoredox Electron-Transfer Strategy

Click chemistry focuses on the development of highly selective reactions using simple precursors for the exquisite synthesis of molecules. Undisputedly, the Cu^I-catalyzed azide–alkyne cycloaddition (CuAAC) is one of the most valuable examples of click chemistry, but it suffers from some limitations as it requires additional reducing agents and ligands as well as cytotoxic copper. Here, we demonstrate a novel strategy for the azide–alkyne cycloaddition reaction that involves a photoredox electron-transfer radical mechanism instead of the traditional metal-catalyzed coordination process. This newly developed photocatalyzed azide–alkyne cycloaddition reaction can be performed under mild conditions at room temperature in the presence of air and visible light and shows good functional group tolerance, excellent atom economy, high yields of up to 99 %, and absolute regioselectivity, affording a variety of 1,4-disubstituted 1,2,3-triazole derivatives, including bioactive molecules and pharmaceuticals. The use of a recyclable photocatalyst, solar energy, and water as solvent makes this photocatalytic system sustainable and environmentally friendly. Moreover, the azide–alkyne cycloaddition reaction could be photocatalyzed in the presence of a metal-free catalyst with excellent regioselectivity, which represents an important development for click chemistry and should find versatile applications in organic synthesis, chemical biology, and materials science.     

Polyhydrido Copper Nanoclusters with a Hollow Icosahedral Core: [Cu30H18{E2P(OR)2}12] (E=S or Se; R=nPr,iPr or iBu)

Although atomically precise polyhydrido copper nanoclusters are of prime interest for a variety of applications, they have so far remained scarce. Herein, this work describes the synthesis of a dithiophosphate-protected copper(I) hydride-rich nanocluster (NC), [Cu₃₀H₁₈{S₂P(OnPr)₂}₁₂] ( 1_H ), fully characterized by various spectroscopic methods and single-crystal X-ray diffraction. The X-ray structure of 1_H reveals an unprecedented central Cu₁₂ hollow icosahedron. Six faces of this icosahedron are capped by Cu₃ triangles, the whole Cu₃₀ core being wrapped by twelve dithiophosphate ligands and the whole cluster has ideal S₆ symmetry. The locations of the 18 hydrides in 1_H were ascertained by a single-crystal neutron diffraction study. They are composed of three types: capping μ₃-H, interstitial μ₄-H (seesaw) and μ₅-H ligands (square pyramidal), in good agreement with the DFT simulations. The numbers of hydrides and ligand resonances in the ¹H NMR spectrum of 1_H are in line with their coordination environment in the solid state, retaining the S₆ symmetry in solution. Furthermore, two new Se-protected polyhydrido copper nanoclusters, [Cu₃₀H₁₈{Se₂P(OR)₂}₁₂] ( 2_H : R=iPr 3_H : R=iBu) were synthesized from their sulfur relative 1_H via ligand displacement reaction and their X-ray structures feature the exceptional case where both the NC shape and size are fully conserved during the course of ligand exchange. DFT and TD-DFT calculations allow understanding the bonding and optical properties of clusters 1_H – 3_H . In addition, the reaction of 1_H with [Pd(PPh₃)₂Cl₂] in the presence of terminal alkynes led to the formation of new bimetallic Cu−Pd alloy clusters [PdCu₁₄H₂{S₂P(OnPr)₂}₆(C≡CR)₆] ( 4 : R=Ph; 5 : R = C₆H₄F).     

Purification of low-abundance lysozyme in egg white via free-flow electrophoresis with gel-filtration chromatography

As an effective separation tool, free-flow electrophoresis has not been used for purification of low-abundance protein in complex sample matrix. Herein, lysozyme in complex egg white matrix was chosen as the model protein for demonstrating the purification of low-content peptide via an FFE coupled with gel fitration chromatography (GFC). The crude lysozyme in egg while was first separated via free-flow zone electrophoresis (FFZE). After that, the fractions with lysozyme activity were condensed via lyophilization. Thereafter, the condensed fractions were further purified via a GFC of Sephadex G50. In all of the experiments, a special poly(acrylamide- co-acrylic acid) (P(AM-co-AA)) gel electrophoresis and a mass spectrometry were used for identification of lysozyme. The conditions of FFZE were optimized as follows: 130 μL/min sample flow rate, 4.9 mL/min background buffer of 20 mM pH 5.5 Tris-Acetic acid, 350 V, and 14 °C as well as 2 mg/mL protein content of crude sample. It was found that the purified lysozyme had the purity of 80% and high activity as compared with its crude sample with only 1.4% content and undetectable activity. The recoveries in the first and second separative steps were 65% and 82%, respectively, and the total recovery was about 53.3%. The reasons of low recovery might be induced by diffusion of lysozyme out off P(AM-co-AA) gel and co-removing of high-abundance egg ovalbumin. All these results indicated FFE could be used as alternative tool for purification of target solute with low abundance.