RUI: Domain-Domain and Protein-Protein Interactions in Reactive Oxygen Species

有了这个奖项，化学部的生命过程化学项目资助了南伊利诺伊大学爱德华兹维尔分校的魏金川博士，他正在研究一类重要的蛋白质，这些蛋白质与动脉粥样硬化和肿瘤生长等疾病过程有关。该计划涉及研究这些蛋白质的功能最终如何与其独特的结构相关，这些结构由各种蛋白质和其他分子之间的弱相互作用所控制。Wei教授正在描述这些弱相互作用，以了解这些蛋白质功能的相似性和差异，并为酶学提供新的见解。该项目的参与者，包括本科生和硕士。研究生，获得蛋白质制备和表征技术的专门培训，加强了基础研究计划在一个主要的本科院校。该项目还招募代表性不足的学生和高中生进行生物化学研究。本研究计划利用生物物理技术来阐明两种相关酶NADPH氧化酶5和双氧化酶的酶促机制。它们的酶活性受多种因素的调节，包括结构域-结构域和蛋白质-蛋白质相互作用。这些相互作用进行了研究，通过超灵敏量热法和紫外/荧光光谱，以获得热力学和动力学参数，以及有关结构变化的信息。此外，它们的序列，磷酸化，和辅助蛋白识别位点之间的差异进行了研究，其不同的活动概况。这项研究的信息提供了这两种酶在催化和调节方面的分子理解，为探索非吞噬细胞NADPH氧化酶定义了一个新的模型系统。

With this award, the Chemistry of Life Processes Program in the Chemistry Division is funding Dr. Chin-Chuan Wei from Southern Illinois University Edwardsville who is investigating an important class of proteins that have been implicated in disease processes such as atherosclerosis and tumor growth. The program involves studying how the functions of these proteins are ultimately related to their unique structures as governed by weak interactions between various proteins and other molecules. The Professor Wei is characterizing these weak interactions in an effort to understand the similarities and differences of these protein functions and to provide new insights in enzymology. The project participants, including undergraduate and M.S. graduate students, acquire specialized training in protein preparation and characterization techniques, that enhance fundamental research programs at a primary undergraduate institution. The project also recruits underrepresented students and high school students to biochemical research. This research project uses biophysical techniques to elucidate the enzymatic mechanism of two related enzymes, NADPH oxidase 5 and dual oxidase. Their enzymatic activities are modulated by several factors including domain-domain and protein-protein interactions. These interactions are investigated by ultra-sensitive calorimetry and UV/fluorescence spectroscopy to obtain thermodynamic and kinetic parameters, as well as information about structural changes. In addition, the dissimilarities between their sequences, phosphorylation, and auxiliary protein recognition sites are investigated for their distinct activity profiles. Information from this study provides a molecular understanding of these two enzymes in regards to their catalysis and regulation, defining a new model system for exploring non-phagocyte NADPH Oxidases.