Gronenborn A M, Clore G M
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
Crit Rev Biochem Mol Biol. 1995;30(5):351-85. doi: 10.3109/10409239509083489.
With the advent of multidimensional heteronuclear-edited and -filtered NMR experiments, the field of three-dimensional structure determination by NMR has again increased in scope, making it possible to move the technology beyond the approximately 10 kDa limit inherent to conventional two-dimensional NMR to systems up to potentially 35 to 40 kDa. This article outlines the basic strategies for solving three-dimensional structures of larger systems, in particular, protein complexes and multimeric proteins using three- and four-dimensional NMR spectroscopy, summarizes the key experiments, and illustrates the power of these methods using several examples of protein-DNA, protein-peptide complexes, and oligomeric proteins from the authors' laboratories.
随着多维异核编辑和过滤核磁共振实验的出现，核磁共振三维结构测定领域的范围再次扩大，使得该技术能够突破传统二维核磁共振固有的约10 kDa的限制，应用于潜在分子量高达35至40 kDa的系统。本文概述了使用三维和四维核磁共振光谱解析更大系统（特别是蛋白质复合物和多聚体蛋白质）三维结构的基本策略，总结了关键实验，并通过作者实验室的几个蛋白质 - DNA、蛋白质 - 肽复合物和寡聚体蛋白质的例子说明了这些方法的强大之处。
