State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Innovation Academy for Precision Measurement Science and Technology, National Center for Magnetic Resonance in Wuhan, Key Laboratory of Magnetic Resonance in Biological Systems, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071, P. R. China.
University of Chinese Academy of Sciences, Beijing, 100049, P. R. China.
J Biomol NMR. 2021 May;75(4-5):193-202. doi: 10.1007/s10858-021-00367-9. Epub 2021 Apr 22.
Spectral editing is crucial to simplify the crowded solid-state NMR spectra of proteins. New techniques are introduced to edit C-C 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 Cα-Cβ double-quantum filtering (DQF). The Cα-Cβ 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 C, N labeled Aquaporin Z (AqpZ) membrane protein, demonstrating their potential to simplify spectral analyses in biological solid-state NMR.
谱编辑对于简化蛋白质的固态 NMR 谱图至关重要。本文介绍了在中等魔角旋转（MAS）条件下，基于我们最近的频率选择同核再耦序列[Zhang 等人，J. Phys. Chem. Lett. 2020, 11, 8077-8083]，编辑均标记蛋白质的 C-C 相关的新技术。通过选择性的 Cα-Cβ 双量子滤波（DQF）可以选择出丙氨酸、丝氨酸或苏氨酸残基的信号。丙氨酸残基的 Cα-Cβ 相关性可以有效地建立起来，效率高达~1.8 倍于偶极辅助转动共振（DARR）。这些技术在 2D/3D NCCX 实验中得到了展示，并应用于均 C、N 标记的 Aquaporin Z（AqpZ）膜蛋白，展示了它们在生物固态 NMR 中简化谱分析的潜力。
