UPGRADE OF A GE-OMEGA 500MHZ NMR SPECTROMETER

GE-OMEGA 500MHZ 核磁共振波谱仪的升级

• 批准号: 2803027
• 负责人: Frederick W. Dahlquist
• 金额: $ 36.9万
• 依托单位: UNIVERSITY OF OREGON
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-06-01 至 2000-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2803027
• 关键词: biomedical equipment; biomedical equipment purchase; nuclear magnetic resonance spectroscopy; structural biology

Funds are requested to upgrade a 10 year old GE Omega 500 NMR spectrometer. The upgraded instrument will provide modern triple resonance pulsed field gradient probes and RF electronics capability for the observation of macromolecules in solution. The proposed system will complement a modern 600 MHz instrument that is currently over saturated with users. The proposal includes 15 protein based projects from a total of eight NIH-funded investigators at the University of Oregon. The projects vary from detailed solution structure determination, investigations of the dynamic properties of folded proteins, folding mechanisms and thermodynamics, studies of protein-protein interaction, and investigations of catalytic mechanisms. These include the structure and dynamics of protein-protein interactions in bacterial signal transduction pathways, the structure of wild-type and mutant subunits of the F1F0 ATP synthase, the mechanism of DNA recognition by an unusual DNA binding motif found in the putative transcription factor, Skn-1, from C. elegans, the folding pathway of T4 lysozyme, solvent access into the hydrophobic cores and cavities of both T4 lysozyme and green fluorescent protein, the structure and function of a bacterial phospholipase C and the structural changes associated with mutations of the pro-sequence of yeast carboxypeptidase.

申请资金升级已有10年历史的通用欧米茄500核磁共振光谱仪。升级后的仪器将提供现代三重共振脉冲场梯度探针和射频电子功能，用于观察溶液中的大分子。拟议的系统将补充目前用户过度饱和的现代600 MHz仪器。该提案包括15个基于蛋白质的项目，这些项目来自俄勒冈大学的8名nih资助的研究人员。这些项目包括详细的溶液结构测定、折叠蛋白质动态特性的研究、折叠机制和热力学、蛋白质-蛋白质相互作用的研究以及催化机制的研究。这些研究包括细菌信号转导通路中蛋白-蛋白相互作用的结构和动力学、野生型和突变型F1F0 ATP合成酶亚基的结构、在线虫的假设转录因子Skn-1中发现的一个不寻常的DNA结合基序的DNA识别机制、T4溶菌酶的折叠途径、溶剂进入T4溶菌酶和绿色荧光蛋白的疏水核心和空腔的途径。细菌磷脂酶C的结构和功能以及与酵母羧肽酶前序列突变相关的结构变化。

项目成果

Solution structure of a complex of the histidine autokinase CheA with its substrate CheY.

• DOI: 10.1021/bi300147m
• 发表时间: 2012-05-08
• 期刊: Biochemistry
• 影响因子: 2.9
• 作者: Mo G;Zhou H;Kawamura T;Dahlquist FW
• 通讯作者: Dahlquist FW