Meier Beat H, Böckmann Anja
Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, CH-8093 Zurich, Switzerland.
Institut de Biologie et Chimie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon, 7 passage du Vercors, 69367 Lyon, France.
Curr Opin Struct Biol. 2015 Feb;30:43-49. doi: 10.1016/j.sbi.2014.12.001. Epub 2014 Dec 24.
Recent developments in solid-state NMR have opened the way to the structural analysis of protein fibrils, with the power of studying them at atomic resolution. Solid-state NMR is a relatively new player in the field of structural biology, and reliable approaches to successfully tackle 3D structures have been developed and applied recently. Here we discuss a number of applications to selected fibrils, including prions, α-synuclein and Amyloid-β (Aβ). The latter is, as for its small monomer size, accessible to full 3D structure determination by solid-state NMR. In addition, chemical-shift assignments, from which secondary structure can be directly be determined, is possible for much larger proteins, and has provided important insight in the structural organization of prions and other amyloids playing a central role in disease.
固态核磁共振技术的最新进展为蛋白质纤维的结构分析开辟了道路，使其能够在原子分辨率下对其进行研究。固态核磁共振在结构生物学领域是一个相对较新的方法，近年来已开发并应用了可靠的方法来成功解析三维结构。在这里，我们讨论了一些在选定纤维上的应用，包括朊病毒、α-突触核蛋白和β-淀粉样蛋白（Aβ）。就其小单体尺寸而言，后者可以通过固态核磁共振确定完整的三维结构。此外，对于更大的蛋白质，也可以进行化学位移归属，从而直接确定二级结构，这为朊病毒和其他在疾病中起核心作用的淀粉样蛋白的结构组织提供了重要见解。
