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

该奖项将资助南伊利诺伊大学爱德华斯维尔分校生命过程化学项目资助魏金川博士，他正在研究一类与动脉粥样硬化和肿瘤生长等疾病过程有关的重要蛋白质。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，这些结构受各种蛋白质和其他分子之间的弱相互作用所支配。魏教授正在刻画这些弱相互作用的特征，以努力了解这些蛋白质功能的相似和不同之处，并在酶学方面提供新的见解。项目参与者，包括本科生和硕士研究生，接受蛋白质制备和表征技术的专门培训，以加强小学本科院校的基础研究项目。该项目还招募了未被充分代表的学生和高中生从事生物化学研究。本研究利用生物物理技术，对NADPH氧化酶5和双氧化酶两种相关酶的作用机理进行了研究。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。用超灵敏热法和紫外/荧光光谱研究了这些相互作用，以获得热力学和动力学参数，以及关于结构变化的信息。此外，由于它们不同的活性图谱，研究了它们的序列、磷酸化和辅助蛋白质识别位点之间的不同之处。这项研究的信息提供了关于这两种酶的催化和调节的分子理解，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.