600 MHZ NUCLEAR MAGNETIC RESONANCE SPECTROMETER

我们申请资金购买最先进的600 MHz核磁共振光谱仪，以支持一组NIH赞助的主要用户（Gierasch，Decatur，Maroney，Thompson，Weis，Zimmermann）的研究，他们的研究将需要85%的仪器时间。仪器的剩余时间将分配给小用户（Gross、Hong、Martin、Rotello、Krejsa），并由NMR设施经理和副经理维护和实施新实验。获得所要求的仪器将有助于开展的主要研究项目包括：确定分子伴侣DnaK和BiP的肽结合域的结构;确定信号序列与其受体相互作用后的结合构象;确定单独的和与多肽复合的结合SRP的RNA片段的结构;主要是β折叠蛋白，细胞视黄酸结合蛋白的折叠机制的研究;作为鸟苷酸环化酶模型的肌红蛋白突变体的结构分析;模型螺旋肽的构象研究;膜蛋白，包括E.大肠杆菌趋化性受体和大肠杆菌素A;大肠杆菌趋化性受体，参与适应;和确定结构或核糖体蛋白质和RNA，它们结合。小项目，将受益于这种仪器的可用性包括：EGF受体片段与肌动蛋白相互作用后的结合构象的研究;结构表征的肽合成困难的序列;结构域的T7 RNA聚合酶的结构研究;模型的结构研究黄素辅因子及其环境扰动;和交联剂结构与尼龙的物理和化学性质的相关性。

We request funds to purchase a state-of-the-art 600 MHz nuclear magnetic resonance spectrometer to support the research of a group of NIH- sponsored major users (Gierasch, Decatur, Maroney, Thompson, Weis, Zimmermann), whose research will require 85% of the instrument time. The remaining time of the instrument will be allotted to minor users (Gross, Hong, Martin, Rotello, Krejsa) and to maintenance and implementation of new experiments by the NMR Facility Manager and Associate Manager. The major research projects that will be facilitated by the availability of the requested instrumentation include: determination of the structure of the peptide-binding domains of the molecular chaperones DnaK and BiP; determination of the bound conformation of signal sequences upon interaction with their receptors; determination of the structure of an SRP-binding RNA fragment alone and in complex with a polypeptide; studies of the mechanism of folding of the predominantly beta-sheet protein, cellular retinoic acid binding protein; structural analysis of myoglobin mutants as models for guanylate cyclase; conformational studies of model helical peptides; determination of the structure and dynamics of membrane proteins, including E. coli chemotactic receptors and colicin A; studies of domains of the E. coli chemotactic receptor that are involved in adaptation; and determination of the structures or ribosomal proteins and the RNAs to which they bind. Minor projects that will benefit from the availability of this instrumentation include: studies of bound conformations of EGF receptor fragments upon interactions with actin; structural characterization of difficult sequences for peptide synthesis; structural studies of domain of T7 RNA polymerase; structural studies of models for flavin cofactors and their environmental perturbations; and correlation of crosslinker structure with physical and chemical properties of nylons.