Spectral editing is crucial to simplify the crowded solid-state NMR spectra of proteins. New techniques are introduced to edit ¹³C-¹³C correlations of uniformly labeled proteins under moderate magic-angle spinning (MAS), based on our recent frequency-selective homonuclear recoupling sequences [Zhang et al., J. Phys. Chem. Lett. 2020, 11, 8077–8083]. The signals of alanine, serine, or threonine residues are selected out by selective ¹³Cα-¹³Cβ double-quantum filtering (DQF). The ¹³Cα-¹³Cβ correlations of alanine residues are selectively established with efficiency up to ~ 1.8 times that by dipolar-assisted rotational resonance (DARR). The techniques are shown in 2D/3D NCCX experiments and applied to the uniformly ¹³C, ¹⁵N labeled Aquaporin Z (AqpZ) membrane protein, demonstrating their potential to simplify spectral analyses in biological solid-state NMR.

光谱编辑对于简化蛋白质的拥挤的固态 NMR 光谱至关重要。基于我们最近的频率选择性同核重偶联序列，引入了新技术以在中等魔角旋转 (MAS) 下编辑均匀标记蛋白质的¹³ C- ¹³ C 相关性 [Zhang et al., J. Phys. 化学 莱特。2020, 11, 8077–8083]。丙氨酸、丝氨酸或苏氨酸残基的信号通过选择性¹³ Cα- ¹³ Cβ 双量子过滤 (DQF) 筛选出来。在¹³ Cα- ¹³丙氨酸残基的 Cβ 相关性被选择性地建立，效率高达偶极辅助旋转共振 (DARR) 的 1.8 倍。这些技术显示在 2D/3D NCCX 实验中，并应用于均匀¹³ C、¹⁵ N 标记的水通道蛋白 Z (AqpZ) 膜蛋白，证明它们有可能简化生物固态 NMR 中的光谱分析。