Solution NMR-derived global fold of a monomeric 82-kDa enzyme
Solution NMR-derived global fold of a monomeric 82-kDa enzyme
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DOI：
10.1073/pnas.0407792102
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发表时间：
2005-01-18
影响因子：
11.1
通讯作者：
Kay, LE
中科院分区：
文献类型：
--
作者：
Tugarinov, V;Choy, WY;Kay, LE
由于方法学的最新发展，可以通过溶液NMR光谱研究的蛋白质的大小显着增加。重要的实验包括那些利用增加NMR信号的寿命或定义核间键矢量相对于共同分子框架的取向的方法的实验。核磁共振技术的进步与同位素标记方法密切相关，同位素标记方法提高了灵敏度，降低了核磁共振谱的复杂性。我们表明，这些发展可以利用高分子量，单多肽蛋白质的结构研究，我们提出了解决方案的整体折叠的单体723-残基（82-kDa）酶苹果酸合酶G大肠杆菌，这已被广泛的特点是在过去几年中的NMR。
The size of proteins that can be studied by solution NMR spectroscopy has increased significantly because of recent developments in methodology. Important experiments include those that make use of approaches that increase the lifetimes of NMR signals or that define the orientation of internuclear bond vectors with respect to a common molecular frame. The advances in NMR techniques are strongly coupled to isotope labeling methods that increase sensitivity and reduce the complexity of NMR spectra. We show that these developments can be exploited in structural studies of highmolecular-weight, single-polypepticle proteins, and we present the solution global fold of the monomeric 723-residue (82-kDa) enzyme malate synthase G from Escherichia coli, which has been extensively characterized by NMR in the past several years.