Macromolecular Biochemistry, Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, Leiden, The Netherlands.
Macromolecular Biochemistry, Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, Leiden, The Netherlands.
Curr Opin Struct Biol. 2016 Jun;38:75-82. doi: 10.1016/j.sbi.2016.05.008. Epub 2016 Jun 10.
Proteins come together in macromolecular assemblies, recognizing and binding to each other through their structures, and operating on their substrates through their motions. Detailed characterization of these processes is particularly suited to NMR, a high-resolution technique sensitive to structure, dynamics, and interactions. Advances in isotope-labeling have enabled such studies to an ever-increasing range of systems. Here we highlight recent applications and bring to the fore the range of options to produce labeled proteins and to control the specific placement of isotopes. The increased labeling control and affordability, together with the possibility to combine strategies will further deepen and extend the range of protein assembly investigations.
蛋白质通过其结构相互识别和结合,通过其运动作用于其底物,形成大分子组装体。这些过程的详细特征特别适合于 NMR,NMR 是一种对结构、动力学和相互作用敏感的高分辨率技术。同位素标记的进步使这些研究能够应用于越来越多的系统。在这里,我们重点介绍了最近的应用,并提出了一系列产生标记蛋白和控制同位素特异性位置的方法。增加的标记控制和可负担性,以及结合策略的可能性,将进一步深化和扩展蛋白质组装研究的范围。