Faculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, Żwirki i Wigury 101, 02-089 Warsaw, Poland.
Faculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, Żwirki i Wigury 101, 02-089 Warsaw, Poland.
Methods. 2018 Sep 15;148:81-87. doi: 10.1016/j.ymeth.2018.04.031. Epub 2018 Apr 27.
Intrinsically disordered proteins (IDPs) are getting more and more interest of the scientific community. Nuclear magnetic resonance (NMR) is often a technique of choice for these studies, as it provides atomic-resolution information on structure, dynamics and interactions of IDPs. Nonetheless, NMR spectra of IDPs are typically extraordinary crowded, comparing to those of structured proteins. To overcome this problem, high-dimensional NMR experiments can be used, which allow for a better peak separation. In the present review different aspects of such experiments are discussed, from data acquisition and processing to analysis, focusing on experiments for resonance assignment.
无规卷曲蛋白质（IDPs）越来越受到科学界的关注。核磁共振（NMR）通常是此类研究的首选技术，因为它可以提供 IDPs 的结构、动态和相互作用的原子分辨率信息。尽管如此，与结构蛋白相比，IDPs 的 NMR 谱通常异常拥挤。为了克服这个问题，可以使用高维 NMR 实验，这可以实现更好的峰分离。在本综述中，从数据采集和处理到分析，讨论了此类实验的不同方面，重点是共振分配实验。
