溶液核磁共振得出的一种82千道尔顿单体酶的整体折叠结构。
Solution NMR-derived global fold of a monomeric 82-kDa enzyme.
作者信息
Tugarinov Vitali, Choy Wing-Yiu, Orekhov Vladislav Yu, Kay Lewis E
机构信息
Protein Engineering Network Centres of Excellence and Department of Medical Genetics, University of Toronto, Toronto, ON, Canada M5S 1A8.
出版信息
Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):622-7. doi: 10.1073/pnas.0407792102. Epub 2005 Jan 6.
Abstract
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 high-molecular-weight, single-polypeptide 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.
摘要
由于方法学上的最新进展，可通过溶液核磁共振光谱法研究的蛋白质大小已显著增加。重要的实验包括那些利用增加核磁共振信号寿命的方法或定义核间键向量相对于共同分子框架方向的方法的实验。核磁共振技术的进步与同位素标记方法紧密相关，同位素标记方法可提高灵敏度并降低核磁共振谱的复杂性。我们表明，这些进展可用于高分子量单多肽蛋白质的结构研究，并且我们展示了来自大肠杆菌的723个残基（82 kDa）单体苹果酸合酶G的溶液整体折叠结构，该结构在过去几年中已通过核磁共振进行了广泛表征。
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