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）：申请资金用于升级现有的商用布鲁克Elexsys 500连续波EPR光谱仪，以增加脉冲能力。升级后的仪器将是一个高度通用的EPR仪器，将能够以ns时间分辨率进行大范围的脉冲实验，但将保留在连续波模式下运行的能力。该仪器还可以进行饱和度恢复和ELDOR实验。这将是一个多用户仪器，将由化学系安置和维护。主要用户组将由弗吉尼亚大学的五个研究小组组成：教授；化学系的布莱恩特，卡菲索和哥伦布教授。Tamm和Nakamoto在分子生理学系。该设施也将供该大学的其他研究小组使用。该仪器的主要用途是利用双电子-电子共振（DEER）等技术测定大分子内的分子间距离。用户组的一个重点是获得膜蛋白和大蛋白复合物的结构和动力学信息。这些信息将用于确定促进跨生物膜运输的蛋白质的结构和结构变化，促进细胞信号系统中膜附着的蛋白质的结构和机制，以及蛋白质介导的膜融合机制。膜蛋白是一类极其重要的蛋白质，是目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相当具有挑战性的，因为它们不容易使用标准的结构方法，如晶体学和高分辨率核磁共振。因此，使用EPR的方法，如定点自旋标记，已成为检查这类蛋白质的重要工具。