Motional Modelling by NMR

这项研究将详细研究蛋白质动力学，以了解这些大分子，特别是酶，是如何准确工作的。多年来，核磁共振光谱已被证明是一种可行的确定蛋白质动力学的方法。但是，它主要局限于确定蛋白质中NH载体的运动。在这个项目中，我们将利用剩余偶极耦合实验、构象交换展宽实验和互相关弛豫测量来研究蛋白质中多种不同载体的动力学过程。为了解释这些数据，还将进行化学位移张量的理论计算。所有这些数据将被组合在一起，形成各向异性局部运动的综合动力学模型，这些模型对于完整描述蛋白质的分子和能量性质是重要的。蛋白质并不像人们通常认为的那样是静态的。这些分子具有固有的可移动区域，这些区域是在活细胞中执行各种功能所必需的。核磁共振波谱是一种可以分别恢复生物大分子(如蛋白质)中几乎每个原子的动力学性质的技术。这些详细的见解可能有助于对生命分子的基本理解。

This research will investigate protein dynamics in detail in order to understand how these macromolecules, especially enzymes, precisely work. Nuclear Magnetic Resonance Spectroscopy has proven over the years to be a viable method to determine protein dynamics. But, it has mostly been limited to the determination of the motions of the NH vector in proteins. In this project, the dynamical processes of many different vectors in proteins using residual dipolar couplings experiments, conformational exchange broadening experiments and cross-correlated relaxation measurements will be investigated. To interpret these data, theoretical computations of the chemical shift tensors will also be carried out. All these data will be combined to formulate comprehensive dynamical models of anisotropic local motion that are important for the complete description of the protein's molecular and energetic properties. Proteins are not nearly as static as is often assumed. The molecules have intrinsically mobile areas which are necessary to perform diverse functions in a living cell. Nuclear magnetic resonance spectroscopy is a technique that can retrieve the dynamical properties of virtually each atom, individually, in a biological macromolecule, such as protein. The detailed insights will likely help in the fundamental understanding of the molecules of life.