RUI: Acquistion of a Circular Dichroism Spectropolarimeter

摘要我们正在申请资金购买圆二色（CD）分光偏振计。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，并已广泛用作帮助定义蛋白质折叠方式的工具。该仪器也用于研究其他生物分子的光谱特性，如本提案中描述的光收集组件。Fairman博士和Akerfeldt博士的实验室的研究重点是使用合成肽作为模型系统来研究重要的蛋白质结构。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的线圈结构基序，这是一种简单的蛋白质结构基序，涉及α螺旋之间的相互作用，在20世纪50年代初由弗朗西斯·克里克和莱纳斯·鲍林在分子水平上首次描述。从这些研究中获得的信息将用于设计自组装聚合物，以创造新的纳米工程工具。阿克菲尔德博士的研究试图了解蛋白质结构域是如何合作来定义蛋白质的功能的。Calbindin d28k被用作模型系统来研究旨在结合和储存钙的基序的合作相互作用。还原论的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肽组合在一起重建蛋白质的全部活性。德保拉博士的研究包括了解光捕获分子、卟啉和叶绿素聚集的机制。这些系统是很有希望用于光收集的纳米材料。White博士的研究涉及蛋白质-RNA相互作用的研究，重点研究酵母核糖体蛋白L30与其RNA转录物L30 RNA之间的相互作用。L30蛋白的肽片段中是否存在保留rna结合能力的二级结构将被检验。CD将用于研究rna -蛋白复合物，以探索复合物形成时的构象变化。除了在特定的研究项目中使用该仪器外，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，该仪器被用于所有专业必修的初级实验课程，主要研究纤维蛋白原的二级结构和稳定性。此外，正在计划在二年级的生物化学课程和三年级的化学实验课程中使用该仪器。因此，在我们的研究之外，使用这个工具的一个主要目标是培养学生跨学科的科学方法。这个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.