MRI-R2: Acquisition of Biophysical Instruments for Interdisciplinary Faculty and Student Research

该奖项由2009年《美国复苏与再投资法案》(Public Law 111-5)资助。在重大研究与仪器(MRI)项目的资助下，卡尔文学院的Kumar Sinniah教授及其同事David E Benson和Amy Wilstermann，以及格兰谷州立大学的Brad Wallar将获得原子力显微镜(AFM)、等温滴定量热仪(ITC)和差示扫描量热仪(DSC)。这些仪器将用于一系列化学和生物学研究，包括：G-四链DNA与胰岛素和拓扑异构酶I之间的结合作用，控制蛋白质在纳米颗粒表面附着和稳定性的热力学参数，以及参与调节透明相关形成蛋白的蛋白质相互作用。用原子力显微镜、等温滴定量热法和差示扫描量热法研究了蛋白质-蛋白质和蛋白质-配位体络合物从单分子到本体的结合。单分子相互作用将使用原子力显微镜(AFM)进行研究，而整体系综表征将使用等温滴定热仪(ITC)和差示扫描量热仪(DSC)的互补技术进行。ITC和DSC提供了有关蛋白质-蛋白质和蛋白质-配体相互作用的稳定性和结合的关键信息，并将有助于解释从AFM研究中估计的单分子动力学和热力学性质。这些仪器将共同扩大研究和培训的范围，为卡尔文学院和大谷州立大学(GVSU)的教职员工和学生提供必要的生物分析能力。

This award is funded under the American Recovery and Reinvestment Act of 2009 (Public Law 111-5).With this award from the Major Research and Instrumentation (MRI) program, Professor Kumar Sinniah and his colleagues David E Benson and Amy Wilstermann from Calvin College, and Brad Wallar from Grand Valley State University will acquire an atomic force microscope (AFM), isothermal titration calorimeter (ITC), and differential scanning calorimeter (DSC). The instruments will be used in an array of chemical and biological investigations including: the binding interaction between G-quadruplex DNA with insulin and with topoisomerase I, the thermodynamic parameters that control protein attachment and stability on nanoparticle surfaces, and the protein interactions involved in the regulation of diaphanous related formins. Atomic force microscopy, isothermal titration calorimetry, and differential scanning calorimetry are used to study the binding of protein-protein and protein-ligand complexes from single molecule to bulk ensemble methods. The single molecule interactions will be studied using the atomic force microscope (AFM), while the bulk ensemble characterizations will be carried out using the complementary techniques of isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC). The ITC and DSC provide critical information regarding the stability and binding of protein-protein and protein-ligand interactions and will aid in the interpretation of single molecule kinetic and thermodynamic properties estimated from the AFM studies. Together these instruments will expand the scope of research and training possible, providing essential bioanalytical capabilities to faculty and students at Calvin College and Grand Valley State University (GVSU).