NANOBATTERY

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 芽胞蛋白是受体酪氨酸激酶信号转导的细胞内抑制因子。在这里，我们展示了哺乳动物的Sprouty2蛋白含有一种铁硫复合体，它可以以氧化、还原或亚硝化的状态存在。纯化的Sprouty2组装成大的单分散球体，每个粒子包含大约24个多肽。生化实验表明，Sprouty2颗粒中铁的带电状态可能与周围细胞内的氧化还原隔绝。这些特征提供了一种可能性，即Sprouty2颗粒能够以正式等同于电池的方式接收、保持和消耗电荷。我们建议使用单颗粒低温电子显微镜来确定芽状蛋白质的结构。

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.