500 MHZ NMR SPECTROMETER

500 MHz 核磁共振波谱仪

• 批准号: 3521017
• 负责人: RICHARD VANCE WOLFENDEN
• 金额: $ 29.9万
• 依托单位: UNIV OF NORTH CAROLINA CHAPEL HILL
• 依托单位国家: 美国
• 财政年份: 1991
• 资助国家: 美国
• 起止时间: 1991-02-05 至 1992-02-04
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3521017
• 关键词: biomedical equipment purchase; nuclear magnetic resonance spectroscopy

This proposal requests partial support for the purchase of a 500 MHz nuclear magnetic resonance spectrometer and a data analysis/graphics workstation for research on protein structure and function by investigators at the University of North Carolina. The work station would allow us to process and plot data obtained remotely. This would facilitate our use of the other NMR facilities in the Triangle area. Dr. Gary Pielak will use 2-D NMR to investigate the effects of mutation on the 3-dimensional structure and function of cytochrome c. Dr. Thomas N. Sorrell will examine the influence of altered iron ligands on the same protein. Dr. Richard Wolfenden will use high-field NMR to characterize complexes of enzymes with transition-state and multisubstrate analog inhibitors, as a guide to improvements in drug design. Dr. Mary Ellen Jones will investigate the effects of active site modification on the catalytic function of fragments of mouse orotate decarboxylase, expressed in E. coli. Dr. Bruce Erickson will perform 2-D NMR studies on synthetic polypeptides designed to adopt specific structures in solution and provide a scaffolding for the introduction of functional groups, to obtain new binding agents and catalysts. Dr. Susan Lord will use mutagenesis to explore the role of fibrinogen's primary structure in determining its secondary and tertiary structure, and its interactions with thrombin, as an aid to understanding blood coagulation. Dr. Richard G. Hiskey will use the instrument to elucidate the structure of gamma-carboxyglutamic acid domain peptides in prothrombin. Dr. Howard Reisner will examine the effects of mutations on the three-dimensional structure of the EGF-like domain of Factor IX and other blood coagulation proteins. Dr. Richard Tidwell will investigate the configurations of novel synthetic protease inhibitors. Dr. Avram Gold will use the instrument to examine mechanisms by which porphyrins activate polycyclic enviromnental hydrocarbons, as models for the physiological reactions that generate the ultimate carcinogens.

该建议要求部分支持购买500 MHz 核磁共振光谱仪和数据分析/图形 研究蛋白质结构和功能研究的工作站 北卡罗来纳大学的调查人员。 工作站 将使我们能够处理和绘制远程获得的数据。 这会 促进我们在三角区域使用其他NMR设施。 Gary Pielak博士将使用2-D NMR研究突变的影响 在细胞色素c的3维结构和功能上。托马斯博士 N. Sorrell将检查改变铁配体对 相同的蛋白质。 理查德·沃尔芬登（Richard Wolfenden）博士将使用高场NMR 表征了酶的复合物，并具有过渡状态和 多底物类似抑制剂，作为改善药物的指南 设计。 玛丽·埃伦·琼斯（Mary Ellen Jones）博士将研究活动的影响 对小鼠片段催化功能的位点修改 Orotate脱羧酶，在大肠杆菌中表达。布鲁斯·埃里克森（Bruce Erickson）博士 对旨在采用的合成多肽进行二维NMR研究 解决方案中的特定结构，并为 引入功能组，以获取新的结合剂和 催化剂。 苏珊·洛德（Susan Lord）博士将使用诱变来探索 纤维蛋白原的主要结构在确定其次级和第三纪 结构及其与凝血酶的相互作用，以帮助 了解血液凝血。 理查德·G·Hiskey博士将使用 阐明γ-羧基谷氨酸的结构的仪器 凝血酶原中的域肽。 霍华德·雷斯纳博士将检查 突变对EGF样结构的影响 因子IX和其他血液凝血蛋白的结构域。理查德博士 Tidwell将研究新型合成蛋白酶的配置 抑制剂。 Avram Gold博士将使用该乐器检查 卟啉激活多环境的机制 碳氢化合物，作为生成生理反应的模型 最终的致癌物。