ANALYTICAL ULTRACENTRIFUGE PURCHASE: POLIO VIRUS, FOOT & MOUTH DISEASE

该子项目是利用由NIH/NCRR资助的共享仪器补助金提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是资助机构，不一定是研究者的机构。描述（由申请人提供）：科罗拉多大学医学院将在NCRR共享仪器资助计划的支持下购买一台分析超离心仪器。该仪器需要满足对大分子和配合物的大小、形状、关联和相互作用的准确和快速测定的日益增长的需求。增加的需求是由于学院几个部门的师资队伍扩大，以及建立了跨部门的生物分子结构项目。所要求的仪器将极大地改善现有资源，并将加速广泛系统的研究，包括：分析人类黄体酮受体的自结合和异源蛋白相互作用（D.L. Bain）获得病毒DNA包装的机制理解（C.E. Catalano）。从头设计螺旋状线圈，以了解蛋白质折叠和稳定性，并研究螺旋状线圈在天然蛋白质中的作用，如运动蛋白、ProP转运蛋白和sars冠状病毒（R.S. Hodges）。测定黄体酮同种异构体的功能差异（K. Horwitz）。检查生物学上重要的RNA分子的折叠，包括脊髓灰质炎病毒和相关病毒的功能RNA，并研究口蹄疫病毒的蛋白质-RNA相互作用（J.S. Kieft）。细胞复制酶中蛋白质组装机制和蛋白质相互作用强度的定量分析（C. McHenry）。当前研究的其他领域还包括测定一系列受体（如B细胞补体受体、冠状病毒糖蛋白、雌激素受体配体结合蛋白）中的寡聚化和/或蛋白-蛋白相互作用；ETS转录因子在上皮细胞发育和肿瘤发生中的作用；信号转导通路的亚细胞组织；早期B细胞因子对淋巴细胞特异性转录的影响；脂质储存和细胞内运输；组织纤溶酶原激活物蛋白的鉴定酵母端粒酶和末端保护复合物的基因鉴定前mrna剪接的分子机制。

This subproject is one of many research subprojects utilizing the resources provided by a Shared Instrumentation Grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the grant, which is not necessarily the institution for the investigator. DESCRIPTION (provided by applicant): The University of Colorado School of Medicine will purchase an analytical ultracentrifugation instrument with support from the NCRR Shared Instrumentation Grant Program. This instrument is required to meet the growing demand for the accurate and rapid determination of size, shape, association and interactions of macromolecules and complexes. The increased demand results from expansion of the faculty in several departments in the School as well as the establishment of the interdepartmental Program in Biomolecular Structure. The requested instrument will greatly improve the existing resources and will accelerate research in a broad range of systems, including: Analysis of self-association and heteroprotein interactions in the human progesterone receptor (D.L. Bain) Obtaining a mechanistic understanding of viral DNA packaging (C.E. Catalano). De novo design of coiled-coils to understand protein folding and stability and investigations of coiled- coils in native proteins, e.g., motor proteins, transporter of ProP and SARS-coronavirus (R.S. Hodges). Determining functional differences of isoforms of progesterone (K. Horwitz). Examining folding of biologically important RNA molecules including functional RNAs from poliovirus and related viruses, and studying protein-RNA interactions from foot and mouth disease virus (J.S. Kieft). Analysis of protein assembly mechanisms and quantification of strength of protein-protein interactions in cellular replicases (C. McHenry). Other areas of current research also include determination of oligomerization and/or protein-protein interactions in a range of receptors (e.g., B cell complement receptor, glycoproteins of coronavirus, ligand binding proteins of estrogen receptor); the role of ETS transcription factors in epithelial cell development and tumorigenesis; subcellular organization of signal transduction pathways; lymphocyte-specific transcription by early B cell factor; storage and intracellular trafficking of lipids; characterization of tissue plasminogen activator protein; characterization of genetically identified telomerase and end-protection complexes in yeast; and molecular mechanisms of pre-mRNA splicing.