REAL-TIME ASSESSMENT OF MACROMOLECULAR INTERACTIONS BY SURFACE PLASMON RESONANCE

通过表面等离子共振实时评估大分子相互作用

• 批准号: 5201598
• 负责人: J LAUTENBERGER
• 金额: --
• 依托单位: DIVISION OF CANCER EPIDEMIOLOGY AND GENETICS
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/5201598
• 关键词: DNA binding protein; chemical bond resonance; chemical kinetics; intermolecular interaction; ligands; macromolecule; nucleic acid sequence; transcription factor

The exploration of macromolecular binding to immobilized ligands through the measurement of changes in surface plasmon resonance (SPR) measured in real-time has given new insight into how these processes occur. For example, the real-time binding of the full-length p51 ETS1 to its cognate DNA has been characterized as 'fast-on, fast off' binding while by contrast, the alternate splice product, p42 ETS1 is a 'slow-on, slow off' binder to the same cognate DNA sequence. Each of these proteins has complex, "change-of-state" binding kinetics. Such findings have justified studies of other DNA binding proteins in order to determine if SPR measurements could distinguish different kinetic mechanisms.

利用固定化配体与大分子结合的研究 测量表面等离子体共振（SPR）的变化 对这些过程如何发生有了新的认识。 为 例如，全长p51 ETS1与其同源物的实时结合 DNA的特征是“快速开启，快速关闭”结合，而 相反，交替剪接产物p42 ETS1是一种“慢开慢关”的蛋白， 与相同的同源DNA序列结合。 这些蛋白质中的每一种都有 复杂的“状态变化”结合动力学。 这些发现有 证明了其他DNA结合蛋白的研究，以确定是否 SPR测量可以区分不同的动力学机制。