为满足卫星平台快速研制和部组件即插即用的需求,针对小卫星研制产品化、数字化及规模化发展,提出了一种低成本功率与通信总线集成技术,可实现部组件接口标准化,满足部组件功率传输加断电控制和信号传输电气标准一致性的要求.为了兼容...为满足卫星平台快速研制和部组件即插即用的需求,针对小卫星研制产品化、数字化及规模化发展,提出了一种低成本功率与通信总线集成技术,可实现部组件接口标准化,满足部组件功率传输加断电控制和信号传输电气标准一致性的要求.为了兼容现有部组件控制器局域网络(controller area network,CAN)总线接口(采用信号电源线传输串行编码数据解决功率传输加断电控制的问题),提出了一种低成本电路方案,确保加断电指令的三模冗余,从而实现了基于CAN总线的功率信号传输电路容错技术方案,满足星载可靠性应用.试验结果证明了新技术方法实用有效.展开更多
The enzyme Ots A（trehalose-P synthase） plays a critical role in the biosynthesis of trehalose, which is a nonreducing disaccharide that plays important functions in many organisms. By using light scattering techniqu...The enzyme Ots A（trehalose-P synthase） plays a critical role in the biosynthesis of trehalose, which is a nonreducing disaccharide that plays important functions in many organisms. By using light scattering technique, we discovered that Ots A in Arthrobacter strain A3 polymerized in the presence of divalent metal ions（Mg2＋ or Ca2＋）, and the kinetics of the assembly was dependent on their concentrations. We identified potential compounds that can affect the kinetics of the polymerization, particularly, heparin, which acts as a very promising inhibitor of the polymerization. The Ots A assembly turns out to be a very delicate process that is finely regulated by p H. Ots A may be in the polymerized form at physiological pH in vivo, suggesting a more complicated mechanism of the enzyme. These unique properties of Ots A provide novel insights into the molecular mechanism of the biosynthesis of trehalose.展开更多
文摘为满足卫星平台快速研制和部组件即插即用的需求,针对小卫星研制产品化、数字化及规模化发展,提出了一种低成本功率与通信总线集成技术,可实现部组件接口标准化,满足部组件功率传输加断电控制和信号传输电气标准一致性的要求.为了兼容现有部组件控制器局域网络(controller area network,CAN)总线接口(采用信号电源线传输串行编码数据解决功率传输加断电控制的问题),提出了一种低成本电路方案,确保加断电指令的三模冗余,从而实现了基于CAN总线的功率信号传输电路容错技术方案,满足星载可靠性应用.试验结果证明了新技术方法实用有效.
基金Supported by the National Natural Science Foundation of China(21305056)the Open Fund of State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics(T151402)
文摘The enzyme Ots A（trehalose-P synthase） plays a critical role in the biosynthesis of trehalose, which is a nonreducing disaccharide that plays important functions in many organisms. By using light scattering technique, we discovered that Ots A in Arthrobacter strain A3 polymerized in the presence of divalent metal ions（Mg2＋ or Ca2＋）, and the kinetics of the assembly was dependent on their concentrations. We identified potential compounds that can affect the kinetics of the polymerization, particularly, heparin, which acts as a very promising inhibitor of the polymerization. The Ots A assembly turns out to be a very delicate process that is finely regulated by p H. Ots A may be in the polymerized form at physiological pH in vivo, suggesting a more complicated mechanism of the enzyme. These unique properties of Ots A provide novel insights into the molecular mechanism of the biosynthesis of trehalose.
