Institute of Complex Systems, Structural Biochemistry (ICS-6), Research Center Jülich, 52425, Jülich, Germany; Institute of Physical Biology, Heinrich-Heine-University Düsseldorf, Universitätsstraße 1, 40225, Düsseldorf, Germany.
Institute of Complex Systems, Structural Biochemistry (ICS-6), Research Center Jülich, 52425, Jülich, Germany; Institute of Physical Biology, Heinrich-Heine-University Düsseldorf, Universitätsstraße 1, 40225, Düsseldorf, Germany.
Solid State Nucl Magn Reson. 2019 Apr;98:1-11. doi: 10.1016/j.ssnmr.2018.12.003. Epub 2019 Jan 3.
In this article we give an overview over the use of DNP-enhanced solid-state NMR spectroscopy for the investigation of unfolded, disordered and misfolded proteins. We first provide an overview over studies in which DNP spectroscopy has successfully been applied for the structural investigation of well-folded amyloid fibrils formed by short peptides as well as full-length proteins. Sample cooling to cryogenic temperatures often leads to severe line broadening of resonance signals and thus a loss in resolution. However, inhomogeneous line broadening at low temperatures provides valuable information about residual dynamics and flexibility in proteins, and, in combination with appropriate selective isotope labeling techniques, inhomogeneous linewidths in disordered proteins or protein regions may be exploited for evaluation of conformational ensembles. In the last paragraph we highlight some recent studies where DNP-enhanced MAS-NMR-spectroscopy was applied to the study of disordered proteins/protein regions and inhomogeneous sample preparations.
在本文中，我们综述了利用 DN P 增强的固态 NMR 光谱学研究展开的、无规的和错误折叠的蛋白质。我们首先综述了成功应用 DNP 光谱学研究由短肽以及全长蛋白质形成的折叠良好的淀粉样原纤维结构的研究。将样品冷却到低温通常会导致共振信号的严重线宽展宽，从而导致分辨率降低。然而，低温下的不均匀线宽提供了有关蛋白质中残留动力学和柔韧性的有价值的信息，并且与适当的选择性同位素标记技术相结合，在无规蛋白质或蛋白质区域中的不均匀线宽可用于评估构象集合体。在最后一段中，我们强调了一些最近的研究，其中应用了 DN P 增强的 MAS-NMR 光谱学来研究无规蛋白质/蛋白质区域和不均匀的样品制备。
