Department of Biochemistry, Molecular Biology & Biophysics, University of Minnesota, Minneapolis, MN 55455, United States; Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, United States.
Department of Biochemistry, Molecular Biology & Biophysics, University of Minnesota, Minneapolis, MN 55455, United States; Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, United States.
J Mol Biol. 2017 Aug 18;429(17):2667-2676. doi: 10.1016/j.jmb.2017.07.007. Epub 2017 Jul 17.
Recent breakthroughs in isotope-labeling and pulse sequence techniques have enabled the NMR characterization of large protein systems with molecular masses of hundreds of kilodaltons. NMR studies of a great variety of large proteins have provided unique insights into the binding, dynamic, and allosteric mechanisms. Here we present a brief summary of these developments by highlighting few cases that exemplify the uniqueness of NMR in providing atomic resolution information into key dynamic processes and structures of protein complexes with high degree of flexibility.
近年来,同位素质谱标记和脉冲序列技术的突破,使得对数百千道尔顿分子量的大型蛋白质系统进行 NMR 特性分析成为可能。各种大型蛋白质的 NMR 研究为其结合、动态和变构机制提供了独特的见解。本文通过突出少数几个例子,简要总结了这些进展,这些例子说明了 NMR 在提供关键动态过程和高柔韧性蛋白质复合物的原子分辨率信息方面的独特性。