BIOLOGICAL INTERACTION ANALYSIS INSTRUMENT

不到十年的历史，生物相互作用分析（BIA），提供 独特的方法来研究的动力学，稳定性和特异性， 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）现象，BIA不需要 放射性或发色团标记，并适用于分析 蛋白质、肽、核酸、碳水化合物、脂质和各种低 分子量分子。 BIA是在真实的时间内完成的，允许评估 的动力学的相互作用离子许多情况下。 我们提出 获得BIA仪器供生物化学家社区使用， 分子生物学家和生物物理化学家。 的 该仪器将成为高分子相互作用设施的一个组成部分 (MIF)该公司刚刚收购了一台贝克曼XL分析型超级离心机。 一些学院和系的教师将利用MIF 仪器仪表 这些科学家之间的智力交流 传统的部门线，如两组的例子，（一） 生物分子结构/功能与（ii）化学生物学中心 选择在综合生物科学学位课程，其中大部分的 教师参与。 八名共同研究者将研究系统 从原核生物到人类，它们的起源各不相同， 蛋白质、蛋白质-DNA、蛋白质-RNA和蛋白质-小分子相互作用。 研究的具体领域包括： 噬菌体T4复制复合物的组装; 蛋白质相互作用的翻译修饰， 在胰岛素的翻译控制中;蛋白质的生物物理特性， 结合血红素;蛋白质折叠和多聚化;新型 SPR研究小分子-蛋白质相互作用的方法; 蛋白质和DNA的相互作用，形成真核生物的基础 转录复合物;组蛋白、阻遏物和结构蛋白的结合 形成抑制性染色质结构域的蛋白质;和相互作用 三种调节蛋白的相互作用以及与HIV-1中DNA的相互作用 长末端重复序列启动子。 从蛋白质折叠到艾滋病， 仪器将促进不同群体之间的互动， 宾州州立大学的科学家们

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.