Fushman David
Department of Chemistry and Biochemistry and Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD, USA.
Methods Mol Biol. 2012;831:485-511. doi: 10.1007/978-1-61779-480-3_24.
Motions are essential for protein function, and knowledge of protein dynamics is a key to our understanding the mechanisms underlying protein folding and stability, ligand recognition, allostery, and catalysis. In the last two decades, NMR relaxation measurements have become a powerful tool for characterizing backbone and side chain dynamics in complex biological macromolecules such as proteins and nucleic acids. Accurate analysis of the experimental data in terms of motional parameters is an essential prerequisite for developing physical models of motions to paint an adequate picture of protein dynamics. Here, I describe in detail how to use the software package DYNAMICS that was developed for accurate characterization of the overall tumbling and local dynamics in a protein from nuclear spin-relaxation rates measured by NMR. Step-by-step instructions are provided and illustrated through an analysis of (15)N relaxation data for protein G.
运动对于蛋白质功能至关重要，了解蛋白质动力学是我们理解蛋白质折叠与稳定性、配体识别、变构作用及催化作用背后机制的关键。在过去二十年中，核磁共振弛豫测量已成为表征蛋白质和核酸等复杂生物大分子中主链和侧链动力学的强大工具。根据运动参数对实验数据进行准确分析，是开发运动物理模型以充分描绘蛋白质动力学的必要前提。在此，我将详细描述如何使用为根据核磁共振测量的核自旋弛豫率准确表征蛋白质的整体翻滚和局部动力学而开发的软件包DYNAMICS。文中提供了详细的分步说明，并通过对蛋白质G的(15)N弛豫数据的分析进行了说明。
