Upgrade of a Bruker AMX 500 MHz Nuclear Magnetic Resonance Spectrometer

9908399摘要该项目涉及500 MHz NMR光谱仪的升级，以提供最先进的能力，以支持阿默斯特马萨诸塞州大学化学系的一组用户的研究。 新仪器的提供将促进重大研究项目。 这项研究将包括确定分子伴侣DnaK和BiP的肽结合结构域的结构;确定信号序列与其受体相互作用时的结合构象;确定单独的和与多肽复合的SRP结合RNA片段的结构;研究主要的β折叠蛋白，细胞视黄酸结合蛋白的折叠机制;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;金属蛋白的活性位点几何形状的测定;膜蛋白的结构和动力学的测定，包括E.大肠杆菌趋化性受体和大肠杆菌素A;与适应有关的大肠杆菌趋化性受体;以及核糖体蛋白及其结合的RNA结构的确定。 其他项目将进一步利用这一工具的剩余时间。

9908399Abstract This project involves the upgrade of a 500 MHz NMR spectrometer to provide state-of-the-art capabilities in order to support the research of a group of users in the Department of Chemistry at University of Massachusetts, Amherst. The major research projects will be facilitated by the availability of the new instrumentation. This research will include determination of the structure of the peptide-binding domains of the molecular chaperones DnaK and BiP; determination of 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 biding protein; structural analysis of myoglobin mutants as models for guanylate cyclase; conformational studies of model helical peptides; determination of the active site geometry of metalloproteins; 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 of ribosomal proteins and the RNAs to which they bind. Additional projects will further utilize the remaining time on this instrument.