RUI: Acquistion of a Circular Dichroism Spectropolarimeter

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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.