Upgrade of Bruker E500 EPR spectrometer

布鲁克E500 EPR光谱仪升级

• 批准号: 7794600
• 负责人: DAVID S CAFISO
• 金额: $ 50万
• 依托单位: UNIVERSITY OF VIRGINIA
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-02-04 至 2012-02-03
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7794600
• 关键词: Biological; Chemistry; Crystallography; Electrons; Funding Applicant; Housing; Mediating; Membrane; Membrane Fusion; Membrane Proteins; Methods; Molecular; Pharmacologic Substance; Physiologic pulse; Physiology; Proteins; Recovery; Research; Resolution; Running; Signal Transduction; Site; Spin Labels; Structure; System; Techniques; Time; Universities; Virginia; instrument; macromolecule; protein complex; research study; tool

DESCRIPTION (provided by applicant): Funds are requested to upgrade an existing commercial Bruker Elexsys 500 continuous wave EPR spectrometer to add pulse capability. The upgraded instrument will be a highly versatile EPR instrument that will be capable of a broad range of pulse experiments with ns time resolution, but will retain the ability to run in CW mode. This instrument is also capable of saturation recovery as well as ELDOR experiments. This will be a multiuser instrument that will be housed and maintained by the Department of Chemistry. The primary user group will consist of five research groups at the University of Virginia: Profs. Bryant, Cafiso and Columbus in the Department of Chemistry, and Profs. Tamm and Nakamoto in the Department of Molecular Physiology. The facility will also be available to other research groups at the University. The primary use of the instrument will be for the determination of intermolecular distances within macromolecules using techniques such as double electron-electron resonance (DEER). A focus of the user group is to obtain information on the structure and dynamics of membrane proteins, and large protein complexes. This information will be used to determine the structures and structural changes in proteins that facilitate transport across biological membranes, the structures and mechanisms of proteins that facilitate membrane attachment in cell-signaling systems, and the mechanisms of protein- mediated membrane fusion. Membrane proteins are an extremely important class of proteins that are targets of the majority of the pharmaceuticals currently in use. Unfortunately, it is quite challenging to understand their molecular function, because they are not easily approached using standard structural methods such as crystallography and high-resolution NMR. As a result approaches using EPR, such as site-directed spin labeling, have become important tools to examine this class of proteins.

描述（由申请人提供）：要求资金升级现有的商业Bruker Elexsys 500连续波EPR光谱仪以添加脉冲能力。升级的仪器将是一种通用的EPR仪器，它将能够进行NS时间分辨率的广泛脉冲实验，但将保留在CW模式下运行的能力。该仪器还能够进行饱和恢复以及Eldor实验。这将是一种多源工具，该工具将由化学系载和维护。主要用户组将由弗吉尼亚大学的五个研究小组组成：教授。化学系的科比，Cafiso和哥伦布和教授。分子生理系的TAMM和NAKAMOTO。该设施也将提供给大学的其他研究小组。该仪器的主要用途是使用诸如双电子电子共振（DEER）等技术确定大分子内分子间距离。用户组的重点是获取有关膜蛋白结构和动力学的信息，以及大型蛋白质复合物。该信息将用于确定蛋白质的结构和结构变化，这些结构和结构变化促进了跨生物膜转运，蛋白质的结构和机制，这些蛋白质的结构和机制促进了细胞信号系统中膜附着的结构以及蛋白质介导的膜融合的机制。膜蛋白是一类极为重要的蛋白质类别，是当前使用的大多数药物的靶标。不幸的是，了解它们的分子功能是非常具有挑战性的，因为使用标准的结构方法（例如晶体学和高分辨率NMR）不容易接近它们。结果，使用EPR（例如位于定位的自旋标记）的方法已成为检查此类蛋白质的重要​​工具。