Kay L E
Department of Medical Genetics, University of Toronto, ON, Canada.
Biochem Cell Biol. 1997;75(1):1-15. doi: 10.1139/o97-023.
An understanding of the role played by a protein in cellular function requires a detailed picture of its three-dimensional structure as well as an appreciation of how the structure varies as a function of time as a result of molecular dynamics. Over the past several years, multidimensional, multinuclear solution NMR spectroscopy has become a powerful technology for obtaining both structural and dynamical information on proteins and protein-ligand systems. In the present review, a number of new methodological advances are highlighted that have significantly improved the quality of NMR spectra of biomolecules and have increased the molecular weight limitations previously imposed on NMR-based structural studies of macromolecules. Applications of this technology to a number of protein systems currently studied in my laboratory are presented.
要了解一种蛋白质在细胞功能中所起的作用,需要详细了解其三维结构,以及理解由于分子动力学导致结构如何随时间变化。在过去几年中,多维、多核溶液核磁共振光谱已成为获取蛋白质和蛋白质-配体系统结构与动力学信息的强大技术。在本综述中,重点介绍了一些新的方法学进展,这些进展显著提高了生物分子核磁共振谱的质量,并增加了先前对基于核磁共振的大分子结构研究施加的分子量限制。本文还介绍了该技术在我实验室目前研究的一些蛋白质系统中的应用。