Quantifying the dynamics of protein function at the atomic level using NMR and calorimetry

使用核磁共振和量热法在原子水平上量化蛋白质功能的动态

• 批准号: 327028-2009
• 负责人: Mittermaier, Anthony
• 金额: $ 3.64万
• 依托单位: McGill University
• 依托单位国家: 加拿大
• 项目类别: Discovery Grants Program - Individual
• 财政年份: 2013
• 资助国家: 加拿大
• 起止时间: 2013-01-01 至 2014-12-31
• 项目状态: 已结题
• 来源: https://www.nserc-crsng.gc.ca/ase-oro/Details-Detailles_eng.asp?id=526790
• 关键词: Quantifying; dynamics; protein; function; atomic

Proteins are central players in an enormous variety of cellular processes, thus understanding how they function is critical to understanding the molecular basis of life. Proteins are highly flexible molecules, and there is growing evidence that their internal dynamics play an essential, but still poorly understood, role in their biological activities. We will use three complementary biophysical techniques to relate the internal motions of protein molecules to their function: Nuclear magnetic resonance (NMR), isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC).

蛋白质是各种细胞过程的核心参与者，因此了解它们的功能对于理解生命的分子基础至关重要。蛋白质是高度灵活的分子，越来越多的证据表明，它们的内部动力学在其生物活动中发挥着重要作用，但人们对其了解甚少。我们将使用三种互补的生物物理技术将蛋白质分子的内部运动与其功能联系起来：核磁共振（NMR），等温滴定量热法（ITC）和差示扫描量热法（DSC）。