BIOLOGICAL INTERACTION ANALYSIS INSTRUMENT

生物相互作用分析仪

• 批准号: 2472761
• 负责人: ROBERT T SIMPSON
• 金额: $ 15.31万
• 依托单位: PENNSYLVANIA STATE UNIVERSITY, THE
• 依托单位国家: 美国
• 财政年份: 1998
• 资助国家: 美国
• 起止时间: 1998-03-01 至 1999-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2472761
• 关键词: biomedical equipment; biomedical equipment purchase; biosensor device; intermolecular interaction; surface plasmon resonance

Less than a decade old, biological interaction analysis (BIA), offers unique approaches to the study of kinetics, stability and specificity of interactions among biological macromolecules and their ligands. Based on the phenomenon of surface plasmon resonance (SPR), BIA does not require radioactive or chromophore labels and is suitable for analysis of proteins, peptides, nucleic acids, carbohydrates, lipids and various low molecular weight molecules. BIA is done in real time, allowing evaluation of the kinetics of the interactions ion many cases. We propose acquisition of a BIA instrument for use by a community of biochemists, molecular biologists, and biophysical chemists at Penn State. The instrument will be a component of the Macromolecular Interactions Facility (MIF), which has just acquired a Beckman XL-analytical ultracentrifuge. Faculty in several Colleges and Departments will utilize the MIF instrumentation. Intellectual interactions among these scientists cross traditional departmental lines, as exemplified by two groups, (I) the Center for Biomolecular Structure/Function and (ii) the Chemical Biology option in the integrative Biosciences degree program, in which most of the involved faculty participate. Eight coinvestigators will study systems that vary from prokaryotes to man in their origin and involve protein- protein, Protein-DNA, protein-RNA, and protein-small moleule interactions. Specific areas of investigation include: protein-protein interactions in assembly of the bacteriophage T4 replication complex; effect of post- translational modification on interactions of proteins that are critical in insulin control of translation; biophysical properties of proteins that bind heme; folding and multimerization of proteins; development of novel methods for study of small molecule-protein interactions by SPR; interactions of the proteins and DNA that form the eukaryotic basal transcription complex; association of histones, a repressor and structural proteins in formation of repressive chromatin domains; and interactions of three regulatory proteins with each other and with DNA in the HIV-1 long terminal repeat promoter. From protein folding to AIDS, the proposed instrumentation will facilitate interactions among a diverse group of scientists at Penn State.

不到十年的生物互动分析（BIA）提供 研究动力学，稳定性和特异性的独特方法 生物大分子及其配体之间的相互作用。 基于 表面等离子体共振（SPR）的现象不需要 放射性或发色团标签，适合分析 蛋白质，肽，核酸，碳水化合物，脂质和各种低 分子量分子。 BIA是实时完成的，允许评估 相互作用的动力学许多情况。 我们建议 收购BIA工具，以供生物化学家社区使用， 宾夕法尼亚州的分子生物学家和生物物理化学家。 这 仪器将是大分子相互作用设施的组成部分 （MIF），刚刚获得了Beckman XL分析超离心机。 几所大学和系的教师将利用MIF 仪器。 这些科学家之间的智力互动 传统的部门线，有两个组的例证，（i） 生物分子结构/功能和（ii）化学生物学中心 综合生物科学学位课程中的选项，其中大多数 涉及教师参加。 八个共同评估者将研究系统 从原核生物到人的起源不等，涉及蛋白质 蛋白质，蛋白-DNA，蛋白-RNA和蛋白质 - 小毛的相互作用。 调查的特定领域包括：蛋白质 - 蛋白质相互作用 噬菌体T4复制复合物的组装；后的影响 关于关键的蛋白质相互作用的翻译修改 在翻译的胰岛素控制中；蛋白质的生物物理特性 结合血红素；蛋白质的折叠和多聚化；小说的发展 SPR研究小分子蛋白相互作用的方法； 形成真核基础的蛋白质和DNA的相互作用 转录复合物；组蛋白的关联，阻遏物和结构 形成抑制性染色质结构域的蛋白质；和互动 彼此之间的三种调节蛋白和HIV-1中的DNA 长时间重复启动子。 从蛋白质折叠到艾滋病，提出了 仪器将促进各种各样的互动 宾夕法尼亚州立大学的科学家。