U.S.-Germany Cooperative Research: Dynamics of ATP-Na(+),K(+)-ATPase Interactions

0072563 Pratap这项为期一年的美德生物化学合作研究奖由格林斯博罗北卡罗来纳大学的Promod Pratap和德国乌尔姆大学的Uli Nienhaus获得。普拉塔普博士将在乌尔姆大学呆上七个月，进行底物与钠/钾ATPase(Na+/K+-ATPase)结合的实验，这是一种相当于钠泵的酶。该泵将ATPase水解释放的能量与钠和钾的运输结合到细胞内。它在体内受胰岛素和甲状腺激素的调节，并作为数字糖苷药物的受体。该项目的目标是了解这种钠泵对运输的能源需求。研究人员将研究酶与ATP之间的相互作用，并探测与ATP底物结合相关的蛋白质结构的变化。将使用两种技术：傅里叶变换红外光谱(FTIR)和单分子荧光能量转移(FRET)。美国研究人员将拟议的酶系统(钠/钾ATPase)方面的专业知识带到了这次合作中。这一点得到了类似的德国专业知识的补充。该项目还利用了乌尔姆大学提供的专门设备(时间分辨可见红外光谱仪)。对钠/钾ATPase的详细分子理解将为调节细胞新陈代谢和能量平衡提供信息。

0072563PratapThis one-year award for U.S.-Germany cooperative research in biochemistry involves Promod Pratap of the University of North Carolina in Greensboro and Uli Nienhaus of the University of Ulm in Germany. Dr. Pratap will spend seven months at the University of Ulm, conducting experiments on substrate binding to sodium/potassium ATPase (Na+/K+-ATPase), an enzymatic equivalent of a sodium pump. The pump couples energy released from ATPase hydrolysis with transport of sodium and potassium into the cell. It is regulated in vivo by insulin and thyroid hormone and serves as a receptor for digital glycoside drugs. The objective of the project is to understand the energy requirements for transport mediated by this sodium pump. The investigators will examine the interaction between the enzyme and ATP and probe changes in protein structure associated with ATP substrate binding. Two techniques will be employed; fourier-transform infrared (FTIR) spectroscopy and single-molecule fluorescence energy transfer (FRET). The U.S. investigator brings to this collaboration expertise in the proposed enzymatic system (sodium/potassium ATPase). This is complemented by similar German expertise. The project also takes advantage of specialized equipment (time-resolved visible infrared spectroscopy) available at the University of Ulm. Detailed molecular understanding of sodium/potassium ATPase will provide information about regulating cellular metabolism and energy balance.