CUMC: PROTEOMICS

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。生物医学科学系的蛋白质组学设施继续为教师和学生提供服务。这些仪器按服务合同或由设施中的技术员定期维护。在此期间进行了215次质谱分析。ECD仪器用于分析Michael C.Owen博士研究生的淀粉样β多肽的构象变化。Attila Borics的一名博士生使用VCD来表征贝塔转化肽。Jeffrey Copps博士学生用VCD光谱分析了TC5b的构象特性，发现了与核磁共振结果一致的复杂结构。TC5b是一种20个残基的多肽，是显示协同折叠三级结构的最短序列。这些结果将在第19届美国多肽研讨会上公布。ECD仪器也被用于支持UNMC的王广顺、克雷顿大学的理查德·霍尔沃斯和帕里克·斯旺森的研究。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for 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.