RUI: Acquistion of a Circular Dichroism Spectropolarimeter

我们请求资金购买圆二向色性(CD)光谱偏振仪。该仪器是生物化学中研究蛋白质和核酸规则结构的重要工具，已被广泛用作帮助确定蛋白质如何折叠的工具。该仪器还可用于研究其他生物分子的光谱性质，如本提案中所述的捕光组件。费尔曼博士和阿克费尔特博士的实验室的研究重点是使用合成多肽作为研究重要蛋白质结构的模型系统。费尔曼博士的研究项目包括研究氨基酸序列如何决定蛋白质结构的稳定性和特异性。他的工作使用了卷曲结构基序，这是一种涉及α-螺旋之间相互作用的简单蛋白质结构基序，由弗朗西斯·克里克和莱纳斯·鲍林在20世纪50年代初首次在分子水平上描述。从这些研究中获得的信息将被用于设计自组装聚合物，以创造新的纳米工程工具。阿克费尔特博士的研究试图理解蛋白质结构域如何相互协作来定义蛋白质中的功能。以Calbindin d28k为模型系统，研究了钙结合和储存基序之间的协同作用。还原方法是通过合成每个单独的结构基序，表征其结构和对钙的亲和力，然后通过将这些合成的多肽重新组合在一起来重建蛋白质的全部活性。德·保拉博士的研究涉及了解捕光分子、卟啉和叶绿素的聚集机制。这些体系是很有前途的纳米材料，可用于集光应用。怀特博士的研究涉及蛋白质-RNA相互作用的研究，重点是研究酵母核糖体蛋白L30及其RNA转录物L30 RNA之间的相互作用。将检查保留RNA结合能力的L30蛋白的多肽片段中是否存在二级结构。CD将用于研究RNA-蛋白质复合体，以探索复合体形成时的构象变化。除了将该仪器用于特定的研究项目外，该仪器还将在哈弗福德学院生物系和化学系的学生培训中发挥重要作用。在生物系，该仪器用于所有专业必修的初级实验室课程，重点研究纤维蛋白原的二级结构和稳定性。此外，正在制定计划，在二年级的生物化学课程和三年级的化学实验室课程中使用该仪器。因此，除了我们的研究之外，使用这种仪器的一个主要目标是培训学生以跨学科的方法接触科学。这一工具将有助于强调哈弗福德学院最近对促进跨学科教育的承诺。

9970203Abstract We are requesting funds to purchase a circular dichroism (CD) spectropolarimeter. This instrument is an important tool in biochemistry for studying regular structure in proteins and nucleic acids and has been used extensively as a tool to help define how proteins fold. Thisinstrument is also used to study spectroscopic properties of other biomolecules, such as light-harvesting assemblies as described in this proposal. Research in Dr. Fairman's and Dr. Akerfeldt's laboratories focuses on the use of synthetic peptides as model systems to study important protein structures. Dr. Fairman's research program involves a study of how amino acid sequences dictate the stability and specificity of protein structures. His work uses the coiled coil structural motif, a simple protein structural motif involving interactions between alpha-helices, first described at the molecular level by Frances Crick and Linus Pauling in the early 1950's. Information gained from these studies will be used to design self-assembling polymers towards the creation of new nanoengineering tools. Dr. Akerfeldt's research tries to understand how protein domains cooperate to define functions in proteins. Calbindin d28k is used as a model system to study the cooperative interactions of motifs designed to bind and store calcium. A reductionist approach is applied by synthesizing each individual structural motif, characterizing its structure and affinity for calcium, and then reconstructing the full activity of the protein by combining these synthetic peptides back together. Dr. de Paula's research involves understanding the mechanism of aggregation of the light-harvesting molecules, porphyrin and chlorophyll. These systems are promising nano-sized materials for light-harvesting applications. Dr. White's research involves the study of protein-RNA interactions focusing on investigating the interaction between yeast ribosomal protein L30 and its RNA transcript, L30 RNA. The existence of secondary structure in peptide fragments of the L30 proteins that retain RNA-binding ability will be examined. CD will be used to study the RNA-protein complex for exploring conformational changes upon complex formation. In addition to the use of this instrument for specific research programs, the instrument will also play an important role in the training of students in both the Biology and Chemistry Departments at Haverford College. In the Biology Department, the instrument is used in a junior level laboratory course, required of all majors, focusing on the study of secondary structure and stability in fibrinogen. In addition, plans are being developed to use the instrument both in a sophomore level biochemistry course and a junior level Chemistry laboratory course. Thus, a major goal for the use of this instrument beyond our research is to train students in interdisciplinary approaches to science. This instrument will help emphasize a recent commitment by Haverford College to promote interdisciplinary education.