ACQUISITION OF A 600 MHZ NMR SPECTROMETER

请拨资金购买14.1T液态核磁共振 一组来自化学领域的科学家将使用光谱仪 中国科学院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能力 化学系。首席调查员目前都在 参与需要收集高分辨率数据的项目 溶液中的蛋白质。简要介绍他们的研究兴趣 下面是。 斯蒂芬·J·本科维奇--催化基础因素的研究 和底物结合在几类酶中：催化抗体， DNA聚合酶I、T4聚合酶复合体、二氢叶酸还原酶和 嘌呤生物合成新途径中的三功能酶。 唐纳德·A·布莱恩特-光合作用中的分子生物学和生物化学 蓝藻和绿色细菌的仪器.电子机制 蓝藻的运输；结构与功能的关系 光系统I；叶绿体的起源。 克里斯托弗·J·福尔宗--利用多核技术研究蛋白质的溶液结构 和多维核磁共振方法；主链动力学；底物动力学 以及定点突变对底物特异性和 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.小分子水溶性结构的决定因素 蛋白质.结构和热力学性质的调节 特定的和非特定的盐效应。 C.罗伯特·马修斯-蛋白质一级结构的机制 将快速有效的折叠引导到天然构象； 定向突变靶向阿尔法亚基中的单个氨基酸 色氨酸合成酶、二氢叶酸还原酶和ras p21。 有了新的仪器，这些调查人员和一组几个 二级调查人员将能够参与和执行 与生物学结构和功能相关的竞争性研究 系统。14.1T光谱仪的可用性也将使其他 研究人员可以使用目前超额预定的11.7T仪器。

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.