Acquisition of a Multinuclear High-Field Fourier Transform Nuclear Magnetic Resonance Spectrometer

获得多核高场傅里叶变换核磁共振波谱仪

• 批准号: 8822707
• 负责人: Bruce Brown
• 金额: $ 15万
• 依托单位: Portland State University
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 1989
• 资助国家: 美国
• 起止时间: 1989-03-01 至 1990-08-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=8822707&HistoricalAwards=false
• 关键词: Acquisition; Multinuclear; Field; Fourier; Transform

Nuclear Magnetic Resonance (NMR) spectroscopy is the most powrful tool available to the chemist for the elucidation of the structure of molecules. It is used to identify unknown substances, characterize specific arrangements of atoms within molecules, and to study the dynamics of interactions between molecules in solution. Access to state-of-the-art NMR spectroscopy is essential to chemists and biologists who are carrying out frontier research. The Department of Chemistry at Portland State University (a Predominantly Undergraduate Institution) will use this award given by the Chemistry Shared Instrumentation Program and the Instrumentation and Instrument Development Program to help acquire a high-field NMR spectrometer. The acquisition will enhance research actvity in the following areas of chemistry and biology: 1) Compounds relevant to membranes for artificial photosynthesis 2) Fluorine-containing low molecular weight compounds and polymers 3) High valent chromium oxidants 4) Atmospheric reaction products 5) Electron deficient heterocyclic pi-systems 6) Fluorine-ligated iron-sulfur clusters in photosystem I 7) Structure of a small iron-sulfur protein 8) Protein thermodynamics probed by denaturation 9) Structure of calcium-binding proteins using NOE.

核磁共振（NMR）光谱是最 化学家可用来阐明 分子的结构 它用于识别未知 物质，表征内部原子的特定排列 分子，并研究相互作用的动力学之间 溶液中的分子。 获得最先进的NMR 光谱学对化学家和生物学家来说是必不可少的， 开展前沿研究。 波特兰州立大学化学系（a 主要本科院校）将使用此奖项 由化学共享仪器计划和 仪器和仪表开发计划，以帮助 获取一台高场核磁共振光谱仪 此次收购将 加强以下化学领域的研究活动 生物学： 1)与人工血管膜相关的化合物 光合作用 2)含氟低分子量化合物和 聚合物 3)高价铬氧化剂 4)大气反应产物 5)缺电子杂环π-体系 6)光系统I中氟连接的铁硫簇合物 7)一种小铁硫蛋白的结构 8)蛋白质变性热力学研究 9)使用NOE的钙结合蛋白的结构。