MRI: Acquisition of a Circular Dichroism Spectropolarimeter

埃默里大学获得了一项奖励，以资助购买圆二色性分光偏振仪。该仪器将支持化学、生物和物理科学领域基础广泛的跨学科研究人员小组的研究，并将加强学生在应用先进生物物理技术表征生物分子（蛋白质和核酸）方面的培训。这种新的仪器将允许埃默里社区，包括研究生和本科生，博士后助理和研究人员，进行先进的研究到相关的基础生物学，人类健康和潜在的工业意义的生物催化剂的生物分子的基本结构和动态特性。该仪器还将推进埃默里大学的教学使命，通过提供最先进的生物分析方法的应用访问和实践经验，这将在研究生和本科生的核心学术课程的教学环境中进行，将通过化学系管理。圆二色谱分光偏振仪将对埃默里大学的研究活动产生重大而持久的影响，包括以下领域：a.使用圆二色性和线性二色性（LD）分析方法对自组装蛋白质、肽和核酸纳米结构进行结构研究，B.）通过圆二色性和荧光测量以及停流方法和可变温度研究促进的工程化蛋白质的结构表征，c.）混合生物/非生物材料内的生物分子的构象性质的分析，d.） 利用仪器的圆二色性和磁性圆二色性能力，询问金属酶内的金属离子结合位点，以及e.）确定核糖核蛋白复合物（如核糖体）中RNA和蛋白质之间相互作用的方式。

An award is made to Emory University to fund the acquisition of a circular dichroism spectropolarimeter. This instrument will support the research of a broad-based and cross-disciplinary group of investigators in the chemical, biological and physical sciences and will enhance student training in the application of advanced biophysical techniques for the characterization of biomolecules (proteins and nucleic acids). This new instrument will allow the Emory community, including graduate and undergraduate students, postdoctoral associates and research faculty, to conduct advanced research into the fundamental structural and dynamic properties of biomolecules of relevance to basic biology, human health and of biocatalysts of potential industrial significance. This instrument will also advance the teaching mission of Emory University by providing access and hands-on experience in application of state-of-the-art bio-analytical methods, which will be conducted in an instructional setting in core academic courses for graduate and undergraduate students that will be administered through the Chemistry Department. The circular dichroism spectropolarimeter will have a significant and lasting impact on research activities at Emory University including the following areas: a.) structural investigation self-assembled protein, peptide, and nucleic acid nanostructures using circular dichroism and linear dichroism (LD) methods of analysis, b.) structural characterization of engineered proteins, facilitated by circular dichroism and fluorescence measurements, as well as stopped-flow methods and variable temperature studies, c.) analysis of the conformational properties of biomolecules within hybrid biotic/abiotic materials, d.) interrogation of metal ion binding sites within metallo-enzymes, utilizing the circular dichroism and magnetic circular dichroism capabilities of the instrument, and e.) determination of the mode of interaction between RNA and proteins in ribonucleo-protein complexes, such as the ribosome.