Acquisition of a Continuous Wave X-band EPR Spectrometer

描述（由申请人提供）：科罗拉多大学博尔德分校化学与生物化学系急需用现代仪器替换老化，不可靠，过时的电子顺磁共振（EPR）光谱仪。目前在博尔德还没有这样的仪器。目前的提案要求拨款购买新的连续波x波段EPR光谱仪（Bruker EleXsys E500），该光谱仪将由8名或更多的高影响力研究人员组成的不同小组使用，并将在部门共享仪器设施内安置和维护。研究应用：EPR光谱仪对于美国国立卫生研究院资助的四个主要用户和多个次要用户的研究至关重要。大多数应用将利用强大的位点导向自旋标签EPR方法来解决大分子结构，动力学，稳定性或功能的基本问题。其他应用将集中在顺磁性金属蛋白中心、纳米材料和聚合物的表征上。所要求的仪器对于正在进行的和新的研究至关重要，重点是：主要用户-蛋白质激酶的开关和骨干运动动力学(Natalie Ahn) -膜结合受体，信号蛋白和多蛋白信号复合物的结构和机制(Joseph Falke) -高浓度蛋白质药物中的蛋白质-蛋白质相互作用(Theodore Randolph) -细菌外膜生物发生中的蛋白质折叠机制（Marcelo Sousa）。次要用户代表-用于检测细胞内金属的新型生物传感器中的金属结合和配位(Amy Palmer) -最近发现的RNA开关的结构和动力学(Arthur Pardi) -用于磁共振成像的新型纳米颗粒磁性造影剂的自旋系统参数(Stephen Russeck) -新型聚合物中稳定有机自由基的结构（Josef Michl）。申请的EPR光谱仪将通过以下两方面对公共卫生产生积极影响：1)进一步推进涉及癌症、细菌感染和免疫反应的基本细胞信号传导过程的基础研究；2)使专注于蛋白质药物开发和改进MRI成像方法的应用研究成为可能。

DESCRIPTION (provided by applicant): The Department of Chemistry and Biochemistry at the University of Colorado, Boulder has a critical need to replace an aging, unreliable, obsolete Electron Paramagnetic Resonance (EPR) spectrometer with a modern instrument. No such instrument currently exists in Boulder. The present proposal requests funding to acquire a new continuous wave X-band EPR spectrometer (Bruker EleXsys E500) that will be utilized by a diverse group of eight or more high impact researchers, and will be housed and maintained within the departmental shared instrumentation facilities. Research applications: An EPR spectrometer is essential for the NIH-funded research of four major users, and multiple minor users. Most applications will utilize powerful site-directed spin-label EPR methods to address fundamental issues of macromolecular structure, dynamics, stability, or function. Other applications will focus on the characterization of paramagnetic metalloprotein centers, nanomaterials, and polymers. The requested instrument is essential for ongoing and new research focusing on: MAJOR USERS - Dynamics of on/off switching and backbone motions in protein kinases (Natalie Ahn) - Structures and mechanisms of membrane-bound receptors, signaling proteins, and multi-protein signaling complexes (Joseph Falke) - Protein-protein interactions at high concentrations of protein pharmaceuticals (Theodore Randolph) - Mechanisms of protein folding in bacterial outer-membrane biogenesis (Marcelo Sousa). REPRESENTATIVE MINOR USERS - Metal binding and coordination in new biosensors designed to detect intracellular metals (Amy Palmer) - Structures and dynamics of recently discovered RNA switches (Arthur Pardi) - Spin system parameters of novel nanoparticle magnetic contrast agents for magnetic resonance imaging (Stephen Russeck) - Structures of stable organic radicals in new polymers (Josef Michl). The requested EPR spectrometer will positively impact public health both by 1) furthering basic research on fundamental cellular signaling processes involved in cancer, bacterial infection and the immune response, and by 2) enabling applied research focusing on protein pharmaceutical development and improvements to MRI imaging methods.