NANOBATTERY

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 Sprouty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，我们表明，哺乳动物Sprouty 2蛋白含有铁硫复合物，可以存在于氧化，还原或亚硝基化状态。纯化的Sprouty 2组装成每个颗粒含有约24个多肽的大的单分散球体。生物化学实验表明，Sprouty 2颗粒内的铁的电荷状态可以与周围的细胞内氧化还原绝缘。这些特征提供了一种可能性，即Sputy 2颗粒能够以形式上等同于电池的方式接收、维持和耗散电荷。我们建议使用单颗粒cryoEM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.