Mechanical Rigidity of DNA and its Relation to DNA-Protein Interactions

DNA 的机械刚性及其与 DNA-蛋白质相互作用的关系

• 批准号: 8816340
• 负责人: Robert Austin
• 金额: $ 29.83万
• 依托单位: Princeton University
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 1989
• 资助国家: 美国
• 起止时间: 1989-02-01 至 1992-07-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=8816340&HistoricalAwards=false
• 关键词: Mechanical; Rigidity; DNA; its; Relation

Dr. Austin is studying the sequence dependence of the elastic properties of DNA and its implications for specificity in protein-DNA interactions. The goals are ambitious and involve the complete integration of physical and biological methodology. Until recently crystallographic data were only available for isolated protein or DNA molecules, that is, not docked together in a biological complex. As a result, models for site specific protein binding have often had a "lock and key" quality. They attempt to understand recognition in terms of a simple interaction between rigid and non--allosteric partners. This project will attempt to show that the bending and torsional strain stored in DNA upon complexation is of equal importance in binding specificity.

奥斯汀博士正在研究DNA弹性特性的序列依赖性，以及它对蛋白质-DNA相互作用的特异性的影响。这些目标雄心勃勃，涉及物理和生物方法论的完全整合。直到最近，只有分离的蛋白质或DNA分子的结晶学数据才能获得，也就是说，不能在生物复合体中对接在一起。因此，针对特定部位蛋白质结合的模型往往具有“锁和钥匙”的性质。他们试图通过刚性和非变构伙伴之间的简单相互作用来理解识别。本项目将试图证明，DNA络合时储存的弯曲和扭转应变在结合特异性方面具有同等重要的作用。