13 research outputs found

    Fabrication of a SnO2-Based Acetone Gas Sensor Enhanced by Molecular Imprinting

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    This work presents a new route to design a highly sensitive SnO2–based sensor for acetone gas enhanced by the molecular imprinting technique. Unassisted and acetone-assisted thermal synthesis methods are used to synthesis SnO2 nanomaterials. The prepared SnO2 nanomaterials have been characterized by X-ray powder diffraction, scanning electron microscopy and N2 adsorption−desorption. Four types of SnO2 films were obtained by mixing pure deionized water and liquid acetone with the two types of as-prepared powders, respectively. The acetone gas sensing properties of sensors coated by these films were evaluated. Testing results reveal that the sensor coated by the film fabricated by mixing liquid acetone with the SnO2 nanomaterial synthesized by the acetone-assisted thermal method exhibits the best acetone gas sensing performance. The sensor is optimized for the smooth adsorption and desorption of acetone gas thanks to the participation of acetone both in the procedure of synthesis of the SnO2 nanomaterial and the device fabrication, which results in a distinct response–recovery behavior

    Effects of initial texture on rolling texture and property of electrodeposited nickel plate

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    By cutting electro-deposited nickel plates at different angles between the rolling planes and the growth plane, we obtained bulk samples with different initial textures. We investigated the microstructures, macrotextures, and microhardness of such samples before and after cold rolling. The results showed that the samples cut at different angles have different initial textures before the cold rolling, and their microstructures changed from isotropic crystals to columnar ones as the cutting angle increased. After cold rolling, the deformed microstructures textures were the same. However, the microhardness of the material was closely related to the cutting angle. As the cutting angle increased, the microhardness decreased significantly. This phenomenon is associated with the dimensional differences between the axial and horizontal directions of the columnar crystal grains of the electro-deposited materials

    Optimization of the Energy Level Alignment between the Photoactive Layer and the Cathode Contact Utilizing Solution-Processed Hafnium Acetylacetonate as Buffer Layer for Efficient Polymer Solar Cells

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    The insertion of an appropriate interfacial buffer layer between the photoactive layer and the contact electrodes makes a great impact on the performance of polymer solar cells (PSCs). Ideal interfacial buffer layers could minimize the interfacial traps and the interfacial barriers caused by the incompatibility between the photoactive layer and the electrodes. In this work, we utilized solution-processed hafnium­(IV) acetylacetonate (Hf­(acac)<sub>4</sub>) as an effective cathode buffer layer (CBL) in PSCs to optimize the energy level alignment between the photoactive layer and the cathode contact, with the short-circuit current density (<i>J</i><sub>sc</sub>), open-circuit voltage (<i>V</i><sub>oc</sub>), and fill factor (FF) all simultaneously improved with Hf­(acac)<sub>4</sub> CBL, leading to enhanced power conversion efficiencies (PCEs). Ultraviolet photoemission spectroscopy (UPS) and scanning Kelvin probe microscopy (SKPM) were performed to confirm that the interfacial dipoles were formed with the same orientation direction as the built-in potential between the photoactive layer and Hf­(acac)<sub>4</sub> CBL, benefiting the exciton separation and electron transport/extraction. In addition, the optical characteristics and surface morphology of the Hf­(acac)<sub>4</sub> CBL were also investigated

    Receptor-specific recognition of NPY peptides revealed by structures of NPY receptors

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    In response to three highly conserved neuropeptides, neuropeptide Y (NPY), peptide YY, and pancreatic polypeptide (PP), four G protein-coupled receptors mediate multiple essential physiological processes, such as food intake, vasoconstriction, sedation, and memory retention. Here, we report the structures of the human Y-1, Y-2, and Y-4 receptors in complex with NPY or PP, and the G(i)(1) protein. These structures reveal distinct binding poses of the peptide upon coupling to different receptors, reflecting the importance of the conformational plasticity of the peptide in recognizing the NPY receptors. The N terminus of the peptide forms extensive interactions with the Y-1 receptor, but not with the Y-2 and Y-4 receptors. Supported by mutagenesis and functional studies, subtype-specific interactions between the receptors and peptides were further observed. These findings provide insight into key factors that govern NPY signal recognition and transduction, and would enable development of selective drugs

    Structures of human mGlu2 and mGlu7 homo- and heterodimers

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    International audienceThe metabotropic glutamate receptors (mGlus) are involved in the modulation of synaptic transmission and neuronal excitability in the central nervous system1. These receptors probably exist as both homo- and heterodimers that have unique pharmacological and functional properties2-4. Here we report four cryo-electron microscopy structures of the human mGlu subtypes mGlu2 and mGlu7, including inactive mGlu2 and mGlu7 homodimers; mGlu2 homodimer bound to an agonist and a positive allosteric modulator; and inactive mGlu2-mGlu7 heterodimer. We observed a subtype-dependent dimerization mode for these mGlus, as a unique dimer interface that is mediated by helix IV (and that is important for limiting receptor activity) exists only in the inactive mGlu2 structure. The structures provide molecular details of the inter- and intra-subunit conformational changes that are required for receptor activation, which distinguish class C G-protein-coupled receptors from those in classes A and B. Furthermore, our structure and functional studies of the mGlu2-mGlu7 heterodimer suggest that the mGlu7 subunit has a dominant role in controlling dimeric association and G-protein activation in the heterodimer. These insights into mGlu homo- and heterodimers highlight the complex landscape of mGlu dimerization and activation
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