This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.The Proteomics Facility at the Department of Biomedical Sciences continued to serve faculty and students. The instruments are regularly maintained either on service contract or by the technician in the Facility. During the time 215 mass spectral analysis were performed. The ECD instrument was used to analyze conformational changes of amyloid beta peptide by Michael C. Owen Ph. D. student. Attila Borics Ph.D. student used the VCD to characterize beta-turn peptides. Jeffrey Copps Ph. D. student analyzed conformational properties of TC5b, a 20 residue peptide which is the shortest sequence showing cooperatively folded tertiary structure, by VCD spectroscopy and revealed a complex structure in agreement with NMR results. These results will be presented at the 19th American Peptide Symposium. The ECD instrument was also used to support the research of Guangshun Wang at UNMC, Richard Hallworth and Parick Swanson at Creighton University.
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