Acquisition of a Spectrofluorometer

已提供资金用于购买高性能 一组人共用静态荧光分光光度计 investigators. 该仪器将用于四个不同的 涉及蛋白质的项目，每个项目都利用荧光 作为一种技术。 将使用荧光强度测量 作为监测蛋白质-蛋白质和 蛋白质-核酸相互作用，配体诱导的构象 变化和荧光团对猝灭剂的可及性。 荧光各向异性的测量也将用于 研究蛋白质结合和构象变化。 荧光能量转移将被用作“光谱分析”。 “标尺”来测量蛋白质上位点的分离。 研究 需要高灵敏度的仪器 和稳定性，低背景，并提供 校正光谱。 个别项目涉及 Ca 2+结合调节因子的性质和相互作用 蛋白质钙调蛋白和肌钙蛋白C，催化的性质， 木瓜蛋白酶位点，核酸解旋特性 蛋白质，以及拓扑异构酶的性质， 介导DNA几何结构的改变。 分子生物学的一个中心目标是阐明 并确定它们的化学物质 特征影响其活动。 一种方法是 荧光光谱，它提供了有关分子的数据， 亚群和分子与分子相互作用。 这种 信息解释了最基本的生物过程 水平

Funds have been provided for the purchase of a high performance static spectrofluorometer for shared use by a group of investigators. The instrument will be used for four different projects involving proteins, each of which utilizes fluorescence as a technique. Fluorescence intensity measurements will be used as a means of monitoring such processes as protein-protein and protein-nucleic acid interactions, ligand-induced conformational changes, and accessibility of fluorophors to quencher. Measurements of fluorescence anisotropy will also be used to study protein associations and conformational changes. Fluorescence energy transfer will be employed as a "spectroscopic ruler" to measure the separation of sites on a protein. Studies of the above kinds require an instrument with high sensitivity and stability, low background, and capability of providing corrected spectra. The individual projects are concerned with the properties and interactions of the Ca2+-binding regulatory proteins calmodulin and troponin C, the nature of the catalytic site of papain, the characteristics of nucleic acid-unwinding proteins, and the properties of the topoismerase enzymes which mediate alterations in the geometry of DNA. A central goal of molecular biology is to elucidate the structure of specific molecules and determine how their chemical characteristics influence their activity. One approach is fluorescence spectroscopy, which provides data about molecular subgroups and molecule-molecule interactions. This kind of information explains biological processes at their most basic level.