Determination of protein structure and dynamics is key to understand the mechanism of protein action. Perdeuterated proteins have been used to obtain high resolution/sensitivty NMR experiments via proton-detection. These methods utilizes ¹H, ¹³C and ¹⁵N nuclei for chemical shift dispersion or relaxation probes, despite the existing abundant deuterons. However, a high-sensitivity NMR method to utilize deuterons and e.g. determine site-specific deuterium quadrupolar pattern information has been lacking due to technical difficulties associated with deuterium’s large quadrupolar couplings. Here, we present a novel deuterium-excited and proton-detected three-dimensional ²H–¹³C–¹H MAS NMR experiment to utilize deuterons and to obtain site-specific methyl ²H quadrupolar patterns on detuterated proteins for the first time. A high-resolution fingerprint ¹H–¹⁵N HSQC-spectrum is correlated with the anisotropic deuterium quadrupolar tensor in the third dimension. Results from a model perdeuterated protein has been shown.

蛋白质结构和动力学的测定是了解蛋白质作用机制的关键。过氘化蛋白质已被用于通过质子检测获得高分辨率/高灵敏度 NMR 实验。尽管存在丰富的氘核，这些方法仍利用¹ H、¹³ C 和^{15 N 原子核进行化学位移分散或弛豫探针。}然而，由于与氘的大型四极耦合相关的技术困难，一直缺乏一种利用氘并例如确定位点特异性氘四极模式信息的高灵敏度 NMR 方法。在这里，我们提出了一种新的氘激发和质子检测的三维² H- ¹³ C- ¹H MAS NMR 实验首次利用氘核并在氘代蛋白质上获得位点特异性甲基^{2 H 四极模式。}高分辨率指纹¹ H – ¹⁵ N HSQC 光谱与三维中的各向异性氘四极张量相关。已经显示了来自模型过氘化蛋白质的结果。