4D solid-state NMR for protein structure determination
4D solid-state NMR for protein structure determination
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DOI：
10.1039/c2cp23872a
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发表时间：
2012-01-01
影响因子：
3.3
通讯作者：
Meier, Beat H.
中科院分区：
文献类型：
--
作者：
Huber, Matthias;Boeckmann, Anja;Meier, Beat H.
固态核磁共振提供了将结构研究扩展到难以在原子分辨率下研究的蛋白质的机会，例如蛋白质原纤维、膜蛋白或衍射性能较差的晶体。由于蛋白质的二维空间相关核磁共振谱存在严重的共振重叠，我们在这篇透视文章中分析了高维（3D 和 4D）质子检测实验的潜力，这些实验为固态结构研究提供了更多可识别和可分配的距离限制。我们讨论了 NMR 测量和合适蛋白质样品制备的实际考虑因素，并展示了 4D 固态 NMR 谱的结构计算结果。
Solid-state NMR offers the chance to extend structural studies to proteins that are otherwise difficult to study at atomic resolution, such as protein fibrils, membrane proteins or poorly diffracting crystals. As two-dimensional spatial correlation NMR spectra of proteins suffer from severe resonance overlap, we analyze in this perspective article the potential of higher-dimensional (3D and 4D) proton-detected experiments, which have an increased number of identifiable and assignable distance restraints for solid-state structural studies. We discuss practical considerations for the NMR measurements and the preparation of suitable protein samples and show results of structure calculations from 4D solid-state NMR spectra.