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Dry electrodes of a smart shirt for measuring biological signals were prepared by the additive printing method using a stretchable conductive paste with Ag fillers loading. Interfacial impedance between the electrode and skin depended on the contact pressure of electrode and the moisture of stratum corneum. When moisture of stratum corneum was more than 30%, ECG could be measured using the stretchable electrodes printed on a compression shirt. However, noise signal in the ECG signal increased when the moisture of stratum corneum was less than 30%. To solve this problem, we propose to use additional electrodes made of an electrically conductive kneaded rubber.  相似文献   
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The cell dimensions of pure triclinic 3CaO·SiO2 and monoclinic 3CaO·SiO2 solid solution (54CaO·16SiO2·Al2O3·MgO) were determined and the powder diffraction patterns were indexed by the method of precise measurement of the spacings. The lattice constants are expressed in terms of triclinic or monoclinic cells corresponding to pseudo-orthorhombic cells derived from Jeffery's trigonal cell. The apparent lattice constants for pure 3CaO·SiO2 are a = 12.195 a.u., b = 7.104 au., c = 25.096 a.u., α= 90°, β= 89°44'γ= 89°44'; for 54CaO·16SiO2.-Al2O3MgO, a = 12.246 a.u., b = 7.045 a.u., c = 24.985 a.u., β= 90°04'. Precise lattice constants of Jeffery's monoclinic lattice for 54CaO.-16SiO2-Al2O3·MgO are derived as a = 33.091 a.u., b = 7.045 a.u., c = 18.546 a.u., β= 94°08'. High-temperature X-ray patterns showed that pure triclinic 3CaO·SiO2 transformed to a monoclinic form at about 920°C. and then to a trigonal form at about 970°C. Monoclinic 54CaO.16SiO2·Al2O3–MgO transformed to trigonal at about 830°C. These transitions were reversible and reproducible and were accompanied by only slight deformation of the structure forms.  相似文献   
3.
Although tin monoxide (SnO) is an interesting compound due to its p-type conductivity,a widespread application of SnO has been limited by its narrow band gap of...  相似文献   
4.
This paper describes the mechanical characteristics of microscale single crystal silicon (SCS) and UV‐LIGA nickel (Ni) films used for microelectromechanical systems (MEMS). A compact tensile tester, operated in an atomic force microscope (AFM), was developed for accurate evaluation of Young's modulus, tensile strain and tensile strength of microscale SCS and UV‐LIGA Ni specimens. SCS specimens with nominal dimensions of 20 μm in thickness, 50 μm in width and 600 μm in length were prepared by a conventional photolithography and etching process. UV‐LIGA Ni specimens, with a thickness of 15 μm, a width of 50 μm and a length of 600 μm in nominal dimensions, were also fabricated by electroplating using a UV thick photoresist mould. All specimens have line patterns on their specimen gauge section to measure axial elongation under tensile loading. The SCS specimens showed a linear stress–strain response and fractured in a brittle manner, whereas the UV‐LIGA Ni specimens showed elastic–inelastic deformation behaviour. Young's modulus of SCS and UV‐LIGA Ni specimens obtained from tensile tests averaged 169.2 GPa and 183.6 GPa, respectively, close to those of bulk materials. However, the tensile strength of both materials showed a larger value than the bulk materials: 1.47 GPa for the SCS and 0.98 GPa for the Ni specimens. Yield stress and breaking elongation of UV‐LIGA Ni specimens were also quite different from those of the bulk Ni because of the specimen size effect on inelastic properties.  相似文献   
5.
Carp Natural Actomyosin: Thermal Denaturation Mechanism   总被引:8,自引:0,他引:8  
Structural changes of actomyosin, the major protein of muscle, on heating have been estimated on ATPase activity. We investigated carp actomyosin molecule changes on heating based on biophysical and biochemical techniques. Actomyosin molecules began to unfold at ~30°C. Hydrophobic amino acid residues and SH groups, which had been inside the molecule, emerged to the surface. Because of hydrophobic interactions and disulfide bonds, actomyosin molecules formed aggregates. At > 40°C, a part of myosin molecules was dissociated from actin filaments. Thus, dissociated myosin and the myosin-lacking molecules co-existed. In addition, fragmentation of actin filaments was observed, which was associated with the dissociation of myosin molecules. At ≥ 60 °C actomyosin molecules formed larger aggregates, in which no filamentous shape was observed. This aggregation occurred mainly by formation of SS bonds.  相似文献   
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