Magic angle spinning (MAS) solid-state NMR (ssNMR) spectroscopy is a major technique for the characterization of the structural dynamics of biopolymers at atomic resolution. However, the intrinsic low sensitivity of this technique poses significant limitations to its routine application in structural biology. Here we achieve substantial savings in experimental time using a new subclass of Polarization Optimized Experiments (POEs) that concatenate TEDOR and SPECIFIC-CP transfers into a single pulse sequence. Specifically, we designed new 2D and 3D experiments (2D TEDOR-NCX, 3D TEDOR-NCOCX, and 3D TEDOR-NCACX) to obtain distance measurements and heteronuclear chemical shift correlations for resonance assignments using only one experiment. We successfully tested these experiments on N-Acetyl-Val-Leu dipeptide, microcrystalline U-13C,15N ubiquitin, and single- and multi-span membrane proteins reconstituted in lipid membranes. These pulse sequences can be implemented on any ssNMR spectrometer equipped with standard solid-state hardware using only one receiver. Since these new POEs speed up data acquisition considerably, we anticipate their broad application to fibrillar, microcrystalline, and membrane-bound proteins.

中文翻译：

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TEDOR 和 NCX MAS 固态 NMR 实验的杂交，用于同时采集异核相关光谱和距离测量。

魔角旋转 (MAS) 固态核磁共振 (ssNMR) 光谱是在原子分辨率下表征生物聚合物结构动力学的主要技术。然而，该技术固有的低灵敏度对其在结构生物学中的常规应用造成了重大限制。在这里，我们使用偏振优化实验 (POE) 的新子类将 TEDOR 和 SPECIFIC-CP 传输连接成单个脉冲序列，从而大大节省了实验时间。具体来说，我们设计了新的 2D 和 3D 实验（2D TEDOR-NCX、3D TEDOR-NCCOX 和 3D TEDOR-NCACX），仅使用一项实验即可获得共振分配的距离测量和异核化学位移相关性。我们成功地对 N-乙酰基-缬氨酸-亮氨酸二肽、微晶 U-13C、15N 泛素以及在脂质膜中重建的单跨度和多跨度膜蛋白进行了这些实验。这些脉冲序列可以在任何配备标准固态硬件的 ssNMR 波谱仪上实现，仅使用一个接收器。由于这些新的 POE 大大加快了数据采集速度，我们预计它们将广泛应用于纤维状、微晶和膜结合蛋白。