ACQUISITION OF A 600 MHZ NMR SPECTROMETER

购买 600 MHZ 核磁共振波谱仪

• 批准号: 2286084
• 负责人: JULIETTE T LECOMTE
• 金额: $ 40万
• 依托单位: PENNSYLVANIA STATE UNIVERSITY, THE
• 依托单位国家: 美国
• 财政年份: 1995
• 资助国家: 美国
• 起止时间: 1995-08-01 至 1998-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2286084
• 关键词: biomedical equipment purchase; nuclear magnetic resonance spectroscopy

Funds are requested for the acquisition of a liquid state 14.1 T NMR spectrometer to be used by a group of scientists from the Chemistry Department and the Biochemistry and Molecular Biology Department of The Pennsylvania State University. This instrument would update and expand the capabilities available within the Nuclear Magnetic Resonance Facility of the Chemistry Department. The primary investigators are all currently involved in projects that require the collection of high-resolution data on proteins in solution. A short description of their research interests follows. Stephen J. Benkovic - Investigation of the factors underlying catalysis and substrate binding in several classes of enzymes: catalytic antibodies, DNA polymerase I, T4 polymerase complex, dihydrofolate reductase, and trifunctional enzymes in the de novo pathway for purine biosynthesis. Donald A. Bryant - Molecular biology and biochemistry in photosynthetic apparatus from cyanobacteria and green bacteria; mechanism of electron transport of cyanobacteria; structure-function relationships in photosystem I; origins of chloroplasts. Christopher J. Falzone - Solution structure of proteins using multinuclear and multidimensional NMR methods; backbone dynamics; substrate dynamics and the effects of site-directed mutation on substrate specificity and protein structure. Juliette T. J. Lecomte - Structure and dynamics of partially folded proteins in solution; determinants of structure in small water-soluble proteins; modulation of structural and thermodynamic properties by specific and non-specific salt effects. C. Robert Matthews - Mechanism by which the primary structure of a protein directs the rapid and efficient folding to the native conformation; site- directed mutagenesis to target individual amino acids in the alpha subunit of tryptophan synthase, dihydrofolate reductase, and ras p2l. With the new instrument, these investigators and a group of several secondary investigators will be in a position to engage in and carry out competitive research related to structure and function in biological systems. The availability of a 14.1 T spectrometer will also allow other researchers to access the currently overbooked 11.7 T instrument.

要求获得液态14.1 T NMR的资金 一组化学科学家使用的光谱仪 部门以及生物化学和分子生物学系 宾夕法尼亚州立大学。该工具将更新和扩展 核磁共振设施中可用的功能 化学系。主要调查人员目前都是 参与需要收集高分辨率数据的项目 在溶液中的蛋白质上。对他们的研究兴趣的简短描述 跟随。 Stephen J. Benkovic-研究基础催化因素 和几类酶的底物结合：催化抗体， DNA聚合酶I，T4聚合酶复合物，二氢叶酸还原酶和 嘌呤生物合成的从头途径中的三功能酶。 Donald A. Bryant-光合作用的分子生物学和生物化学 蓝细菌和绿细菌的设备；电子机理 蓝细菌的运输；结构功能关系中的关系 光系统I；叶绿体的起源。 Christopher J. Falzone-使用多核的蛋白质溶液结构 和多维NMR方法；骨干动力学；底物动力学 以及位于位置突变对底物特异性的影响和 蛋白质结构。 Juliette T. J. Lecomte-部分折叠的结构和动力学 溶液中的蛋白质；小水溶性结构的决定因素 蛋白质；调节结构和热力学特性 特异性和非特异性盐效应。 C. Robert Matthews-蛋白质的主要结构的机制 将快速有效的折叠引导到天然构象。地点- 定向诱变，以靶向α亚基中的单个氨基酸 色氨酸合酶，二氢叶酸还原酶和RAS P2L的。 使用新工具，这些调查人员和一组由几个 次要调查人员将有能力参与并进行 与生物学的结构和功能有关的竞争性研究 系统。 14.1 t光谱仪的可用性也将允许其他 研究人员可以访问当前被超额预订的11.7 T仪器。