Lu Xingyu, Guo Changmiao, Hou Guangjin, Polenova Tatyana
Department of Chemistry and Biochemistry, University of Delaware, Newark, DE, 19716, USA,
J Biomol NMR. 2015 Jan;61(1):7-20. doi: 10.1007/s10858-014-9875-6. Epub 2014 Nov 25.
Fast magic angle spinning (MAS) NMR spectroscopy is emerging as an essential analytical and structural biology technique. Large resolution and sensitivity enhancements observed under fast MAS conditions enable structural and dynamics analysis of challenging systems, such as large macromolecular assemblies and isotopically dilute samples, using only a fraction of material required for conventional experiments. Homonuclear dipolar-based correlation spectroscopy constitutes a centerpiece in the MAS NMR methodological toolbox, and is used essentially in every biological and organic system for deriving resonance assignments and distance restraints information necessary for structural analysis. Under fast MAS conditions (rotation frequencies above 35-40 kHz), dipolar-based techniques that yield multi-bond correlations and non-trivial distance information are ineffective and suffer from low polarization transfer efficiency. To overcome this limitation, we have developed a family of experiments, CORD-RFDR. These experiments exploit the advantages of both zero-quantum RFDR and spin-diffusion based CORD methods, and exhibit highly efficient and broadband dipolar recoupling across the entire spectrum, for both short-range and long-range correlations. We have verified the performance of the CORD-RFDR sequences experimentally on a U-(13)C,(15)N-MLF tripeptide and by numerical simulations. We demonstrate applications of 2D CORD-RFDR correlation spectroscopy in dynein light chain LC8 and HIV-1 CA tubular assemblies. In the CORD-RFDR spectra of LC8 acquired at the MAS frequency of 40 kHz, many new intra- and inter-residue correlations are detected, which were not observed with conventional dipolar recoupling sequences. At a moderate MAS frequency of 14 kHz, the CORD-RFDR experiment exhibits excellent performance as well, as demonstrated in the HIV-1 CA tubular assemblies. Taken together, the results indicate that CORD-RFDR experiment is beneficial in a broad range of conditions, including both high and moderate MAS frequencies and magnetic fields.
快速魔角旋转(MAS)核磁共振光谱正成为一种重要的分析和结构生物学技术。在快速MAS条件下观察到的分辨率和灵敏度的大幅提高,使得仅使用传统实验所需材料的一小部分,就能对具有挑战性的系统进行结构和动力学分析,比如大型大分子聚集体和同位素稀释样品。基于同核偶极的相关光谱是MAS NMR方法工具箱的核心内容,并且基本上用于每个生物和有机系统,以获取结构分析所需的共振归属和距离限制信息。在快速MAS条件下(旋转频率高于35 - 40 kHz),产生多键相关性和重要距离信息的基于偶极的技术效率低下且极化转移效率低。为了克服这一限制,我们开发了一系列实验,即CORD - RFDR。这些实验利用了零量子RFDR和基于自旋扩散的CORD方法的优点,并且在整个光谱范围内展示了高效且宽带的偶极重新耦合,适用于短程和长程相关性。我们已经通过在U - (13)C,(15)N - MLF三肽上的实验以及数值模拟验证了CORD - RFDR序列的性能。我们展示了二维CORD - RFDR相关光谱在动力蛋白轻链LC8和HIV - 1 CA管状聚集体中的应用。在以40 kHz的MAS频率采集的LC8的CORD - RFDR光谱中,检测到了许多新的残基内和残基间相关性,这些相关性在传统偶极重新耦合序列中未被观察到。在14 kHz的中等MAS频率下,CORD - RFDR实验也表现出优异的性能,如在HIV - 1 CA管状聚集体中所示。综上所述,结果表明CORD - RFDR实验在广泛的条件下都有益处,包括高和中等MAS频率以及磁场条件。