NANOBATTERY

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。发芽蛋白作为受体酪氨酸激酶信号传导的细胞内抑制剂。在这里，我们发现哺乳动物Sprouty2蛋白含有铁硫复合物，可以以氧化、还原或亚硝基化状态存在。纯化的Sprouty2组装成大的单分散球体，每个颗粒含有大约24个多肽。生化实验表明，Sprouty2颗粒内铁的电荷状态可能不受细胞内氧化还原的影响。这些特性使得Sprouty2粒子能够以一种形式上等同于电池的方式接收、维持和耗散电荷。我们建议使用单粒子冷冻电镜来确定发芽蛋白的结构

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Sprouty proteins act as intracellular inhibitors of receptor tyrosine kinase signaling. Here we show that the mammalian Sprouty2 protein contains an iron-sulfur complex that can exist in an oxidized, reduced, or nitrosylated state. Purified Sprouty2 assembles into large monodisperse spheres containing approximately 24 polypeptides per particle. Biochemical experiments indicate that the charge state of the iron within Sprouty2 particles may be insulated from ambient intracellular redox. These features offer the possibility that Sprouty2 particles are capable of receiving, maintaining, and dissipating electrical charge in a manner formally equivalent to a battery. We propose to use single particle cryoEM to determine the structure of the sprouty proteins