Acquisition of a 600 MHZ NMR Spectrometer

塔夫茨大学医学院生物化学系和新英格兰医学中心医学系的六个主要用户或主要用户组需要共享一台新的、最先进的600 MHz NMR光谱仪和现有500 MHz光谱仪的升级。 新仪器和升级将被纳入塔夫茨大学医学院现有的生物核磁共振设施，并将位于生物化学系。 主要用户组目前正在进行11个NIH或NSF赞助的项目，需要现代NMR仪器。 因此，需要新仪器和升级，以应用于广泛的基础生物学和生物医学研究。这些项目包括： (i)来自SV 40 T抗原的结合至 DNA复制起点，包括结构 确定蛋白质来源DNA复合物。 （二） 丝氨酸蛋白酶的结构与作用机制研究。 这 包括对甲型肝炎病毒3C蛋白酶和谷氨酸的研究， 酸性蛋白酶;灰色的 (iii)通过电子-核交叉极化改进NMR灵敏度的发展。 (iv)T细胞表面受体的合成交联剂的结构分析和表征。 （五） 乳头瘤病毒E2蛋白及其与DNA复合物的结构分析 (vi)人乳头瘤病毒抑制蛋白的结构分析。 (vii)SH 2结构域和其他信号转导元件的结构分析。 （viii）凝血蛋白的结构分析及其与磷脂的相互作用。 (ix)细胞粘附结构域的结构分析。 （十） 凝血酶受体胞外域的结构分析。 (xi)抗DNA抗体的结构分析。

A new, state-of-the-art 600 MHz NMR spectrometer and an upgrade for an existing 500 MHz spectrometer is requested for shared use by six major users or major user groups at the Department of Biochemistry at Tufts University School of Medicine and the Department of Medicine at The New England Medical Center. The new instrument and the upgrade will be incorporated into the existing biological NMR facility at Tufts University School of Medicine and will be located in the Department of Biochemistry. The major user groups are currently working on eleven NIH or NSF sponsored projects that require modern NMR instrumentation. The new instrument and the upgrade are therefore needed for application in a wide range of basic biological and biomedical research. The projects include: (i) Structural analysis of the domain from SV40 T antigen that bind to the origin DNA replication, including structure determination of the protein origin DNA complex. (ii) Structure and mechanism studies of serine proteinases. This includes work on the type A hepatitis virus 3C proteinase and the glutamic acid specific proteinase from S. griseus. (iii) Development of improved NMR sensitivity through electron-nuclear cross polarization. (iv) Structural analysis and characterization of synthetic crosslinkers of T cell surface receptors. (v) Structural analysis of papillomavirus E2 protein and its complex with DNA. (vi) Structural analysis of human papillomavirus inhibitor proteins. (vii) Structural analysis of SH2 domains and other signal transducing elements. (viii) Structural analysis of blood coagulation proteins and their interaction with phospholipids. (ix) Structural analysis of cellular adhesion domains. (x) Structural analysis of the extracellular domain of the thrombin receptor. (xi) Structural analysis of an anti-DNA antibody.