UPGRADE OF A GE-OMEGA 500MHZ NMR SPECTROMETER

要求提供资金来升级已有10年历史的GE Omega 500核磁共振光谱仪。升级后的仪器将提供现代的三重共振脉冲场梯度探头和射频电子学能力，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。该提案包括来自俄勒冈大学NIH资助的总共8名研究人员的15个基于蛋白质的项目。这些项目包括详细的溶液结构测定，折叠蛋白质的动力学性质的研究，折叠机制和热力学的研究，蛋白质相互作用的研究，以及催化机制的研究。这些包括细菌信号转导途径中蛋白质-蛋白质相互作用的结构和动力学，F1F0 ATP合成酶野生型和突变型亚基的结构，线虫转录因子SKN-1中发现的一个不寻常的DNA结合基序识别DNA的机制，T4溶菌酶的折叠途径，T4溶菌酶和绿色荧光蛋白疏水核心和空腔的溶剂进入，细菌磷脂酶C的结构和功能，以及与酵母羧肽酶前体序列突变相关的结构变化。

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.