4,562 research outputs found

    Coherent Single Spin Source based on topological insulator

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    We report on the injection of quantized pure spin current into quantum conductors. In particular, we propose an on demand single spin source generated by periodically varying the gate voltages of two quantum dots that are connected to a two dimensional topological insulator via tunneling barriers. Due to the nature of the helical states of the topological insulator, one or several {\it spin pair}s can be pumped out per cycle giving rise to a pure quantized alternating spin current. Depending on the phase difference between two gate voltages, this device can serve as an on demand single spin emitter or single charge emitter. Again due to the helicity of the topological insulator, the single spin emitter or charge emitter is dissipationless and immune to disorders. The proposed single spin emitter can be an important building block of future spintronic devices.Comment: 5 pages, 4 figures, append one co-author that has been misse

    Improvement of activity and stability of chloroperoxidase by chemical modification

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    <p>Abstract</p> <p>Background</p> <p>Enzymes show relative instability in solvents or at elevated temperature and lower activity in organic solvent than in water. These limit the industrial applications of enzymes.</p> <p>Results</p> <p>In order to improve the activity and stability of chloroperoxidase, chloroperoxidase was modified by citraconic anhydride, maleic anhydride or phthalic anhydride. The catalytic activities, thermostabilities and organic solvent tolerances of native and modified enzymes were compared. In aqueous buffer, modified chloroperoxidases showed similar <it>K</it><sub>m </sub>values and greater catalytic efficiencies <it>k</it><sub>cat</sub>/<it>K</it><sub>m </sub>for both sulfoxidation and oxidation of phenol compared to native chloroperoxidase. Of these modified chloroperoxidases, citraconic anhydride-modified chloroperoxidase showed the greatest catalytic efficiency in aqueous buffer. These modifications of chloroperoxidase increased their catalytic efficiencies for sulfoxidation by 12%~26% and catalytic efficiencies for phenol oxidation by 7%~53% in aqueous buffer. However, in organic solvent (DMF), modified chloroperoxidases had lower <it>K</it><sub>m </sub>values and higher catalytic efficiencies <it>k</it><sub>cat</sub>/<it>K</it><sub>m </sub>than native chloroperoxidase. These modifications also improved their thermostabilities by 1~2-fold and solvent tolerances of DMF. CD studies show that these modifications did not change the secondary structure of chloroperoxidase. Fluorescence spectra proved that these modifications changed the environment of tryptophan.</p> <p>Conclusion</p> <p>Chemical modification of epsilon-amino groups of lysine residues of chloroperoxidase using citraconic anhydride, maleic anhydride or phthalic anhydride is a simple and powerful method to enhance catalytic properties of enzyme. The improvements of the activity and stability of chloroperoxidase are related to side chain reorientations of aromatics upon both modifications.</p

    Exact periodic cross-kink wave solutions for the (2+1)-dimensional Boiti-Leon-Manna-Pempinelli equation

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    Based on the extended homoclinic test technique and the Hirota’s bilinear method, the (2+1)-dimensional Boiti-Leon-Manna-Pempinelli equation is investigated which describes the fluid propagating and can be considered as a model for an incompressible fluid. With the aid of symbolic computation, we introduce two new Ansätz functions to discuss the multiple periodic-soliton solutions of the (2+1)-dimensional Boiti-Leon-Manna-Pempinelli equation. Some entirely new periodic-soliton solutions are presented. The figures corresponding to these solutions are illustrated to show abundant physics structures
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