CORE--PROTEIN INTERACTION

生物大分子（如蛋白质、寡核苷酸和寡糖）之间的特定相互作用为所有细胞过程提供了化学基础。表征这些相互作用对于在分子水平上定义大分子的生物学功能至关重要。蛋白质相互作用共享资源的作用是为癌症中心的研究人员提供方便地访问用于表征结合相互作用的先进技术。目前，BIACORE 2000光学生物传感器被用于定义组装状态、亲和力和相互作用的动力学。在一个典型的生物传感器实验中，一个相互作用的分子被固定在一个表面上，另一个分子在溶液中通过这个表面。当分子相互作用形成复合物时，利用表面等离子体共振的光学现象记录响应。由于结合反应是实时监测的，因此有可能解释相互作用的动力学信息。考虑到生物传感器分析的复杂性，研究人员与实验室主任David Myszka博士密切合作，以确保实验设计得当，数据得到正确解释。

Specific interactions between biological macromolecules such as proteins, oligonucleotides, and oligosaccharides provide the chemical foundation for all cellular processes. Characterizing these interactions is essential to defining the biological function of a macromolecule at the molecular level. The role of the Protein Interaction Shared Resource is to provide Cancer Center researchers with easy access to the advanced technologies used in characterizing binding interactions. Currently, a BIACORE 2000 optical biosensor is used to define the assembly state, affinity, a kinetics of an interaction. In a typical biosensor experiment one of the interacting molecules is immobilized onto a surface and the second is passed over this surface in solution. When the molecules interact to form a complex, a response is registered using the optical phenomena of surface plasmon resonance. Since binding reactions are monitored in real time, it is possible to interpret kinetic information about the interaction. Given the complexities involved in biosensor analysis, investigators work closely with the facility's director, Dr. David Myszka, to ensure that experiments are designed properly and that the data are interpreted correctly.