Leibniz-Institut für Molekulare Pharmakologie (FMP), Robert Rössle Str. 10, 13125 Berlin, Germany.
Eur J Cell Biol. 2012 Apr;91(4):340-8. doi: 10.1016/j.ejcb.2011.09.002. Epub 2011 Oct 22.
Structural biology is developing into a universal tool for visualizing biological processes in space and time at atomic resolution. The field has been built by established methodology like X-ray crystallography, electron microscopy and solution NMR and is now incorporating new techniques, such as small-angle X-ray scattering, electron tomography, magic-angle-spinning solid-state NMR and femtosecond X-ray protein nanocrystallography. These new techniques all seek to investigate non-crystalline, native-like biological material. Solid-state NMR is a relatively young technique that has just proven its capabilities for de novo structure determination of model proteins. Further developments promise great potential for investigations on functional biological systems such as membrane-integrated receptors and channels, and macromolecular complexes attached to cytoskeletal proteins. Here, we review the development and applications of solid-state NMR from the first proof-of-principle investigations to mature structure determination projects, including membrane proteins. We describe the development of the methodology by looking at examples in detail and provide an outlook towards future 'big' projects.
结构生物学正在发展成为一种通用的工具，可以在原子分辨率下可视化空间和时间上的生物过程。该领域是通过 X 射线晶体学、电子显微镜和溶液 NMR 等成熟的方法建立起来的，现在正在结合新的技术，如小角 X 射线散射、电子断层扫描、魔角旋转固态 NMR 和飞秒 X 射线蛋白结晶学。这些新技术都试图研究非晶态、类似天然的生物材料。固态 NMR 是一种相对较年轻的技术，刚刚证明了其用于从头确定模型蛋白结构的能力。进一步的发展有望对功能生物系统进行深入研究，如膜整合受体和通道，以及与细胞骨架蛋白结合的大分子复合物。在这里，我们回顾了从最初的原理研究到成熟的结构测定项目（包括膜蛋白）中固态 NMR 的发展和应用。我们通过详细的例子来描述方法的发展，并对未来的“大”项目进行展望。
