Bruker BioSpin GmbH, 76287 Rheinstetten, Germany.
J Biomol NMR. 2013 Mar;55(3):231-7. doi: 10.1007/s10858-013-9704-3. Epub 2013 Jan 12.
Intrinsically disordered proteins (IDPs) have recently attracted the attention of the scientific community challenging the well accepted structure-function paradigm. In the characterization of the dynamic features of proteins nuclear magnetic resonance spectroscopy (NMR) is a strategic tool of investigation. However the peculiar properties of IDPs, with the lack of a unique 3D structure and their high flexibility, have a strong impact on NMR observables (low chemical shift dispersion, efficient solvent exchange broadening) and thus on the quality of NMR spectra. Key aspects to be considered in the design of new NMR experiments optimized for the study of IDPs are discussed. A new experiment, based on direct detection of (13)C(α), is proposed.
无规卷曲蛋白质（IDPs）最近引起了科学界的关注，挑战了人们广泛接受的结构-功能范式。在蛋白质动态特性的研究中，核磁共振波谱学（NMR）是一种重要的研究工具。然而，IDPs 的特殊性质，如缺乏独特的三维结构和高度的灵活性，对 NMR 可观测性（低化学位移分散度、高效溶剂交换展宽）产生了强烈影响，从而影响 NMR 谱的质量。讨论了为研究 IDPs 而设计新的 NMR 实验时需要考虑的关键方面。提出了一种基于直接检测（13）C（α）的新实验。
