Robust heteronuclear correlations for proteins in ultrafast magic-angle spinning solid-state NMR

doi:10.26434/chemrxiv-2025-pnhvq

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	Robust heteronuclear correlations for proteins in ultrafast magic-angle spinning solid-state NMR
	Xiao, Hang ; Wang, Jian ; Tan, Huan ; Gan, Yuefang ; Liu, Wenjing ; Zhang, Yan ; Yang, Jun ; Zhang, Zhengfeng
	2025-01-02
状态	已发表
摘要	Under ultrafast magic-angle spinning (MAS), proton-detected solid-state nuclear magnetic resonance (ssNMR) has emerged as a powerful technique for elucidating structures from sub-milligram protein, where establishing ¹³ C-¹⁵N correlations is essential. However, traditional ¹³C-¹⁵N cross-polarization (CP), which performs well at lower MAS frequencies, suffers diminished efficiency under ultrafast MAS conditions. To address this challenge, we have developed a robust method for selective polarization between insensitive nuclei (SPINE). This approach significantly enhances the efficiency of heteronuclear13C-15N correlation compared to CP, achieving gain factors of 1.75 for ¹³CA- ¹⁵N and 1.9 and¹³CO- ¹⁵N transfers. These enhancements can reduce the duration of current multi-dimensional experiments to approximately one-third of that required by ¹³C-¹⁵N CP and to approximately one-tenth when involving two ¹³C- ¹⁵N transfers. The effectiveness of SPINE has been validated through experiments on four distinct proteins: the microcrystalline Î² immunoglobulin binding domain of protein G (GB1), the large-conductance mechanosensitive ion channel from Methanosarcina acetivorans (MaMscL), fibrillar septum-forming protein (SepF), and the vertex protein of the Î²-carboxysome shell (CcmL). These findings highlight the practical utility and versatility of SPINE in ssNMR spectroscopy, making it a valuable approach for structural biology applications.
关键词	protein solid-state nuclear magnetic resonance (NMR) heteronuclear correlation ultrafast magic-angle spinning selective polarization transfer dipolar recoupling solid-state NMR heteronuclear ¹³C-¹⁵N correlation
语种	英语
DOI	10.26434/chemrxiv-2025-pnhvq
相关网址	查看原文
出处	chemRxiv
收录类别	PPRN.PPRN
WOS记录号	PPRN:120257352
WOS类目	Chemistry, Multidisciplinary
文献类型	预印本
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/483967
专题	上海科技大学
作者单位	1.Chinese Acad Sci, Innovat Acad Precis Measurement Sci & Technol, Wuhan, Peoples R China 2.ShanghaiTech Univ, ShanghaiTech Lab Topol Phys, Shanghai, Peoples R China 3.Chinese Acad Sci, Innovat Acad Precis Measurement Sci & Technol, Wuhan, Peoples R China 4.Chinese Acad Sci, Innovat Acad Precis Measurement Sci & Technol, Wuhan, Peoples R China 5.Chinese Acad Sci, Innovat Acad Precis Measurement Sci & Technol, Wuhan, Peoples R China 6.Chinese Acad Sci, Innovat Acad Precis Measurement Sci & Technol, Wuhan, Peoples R China 7.Chinese Acad Sci, Wuhan Inst Phys & Math, Innovat Acad Precis Measurement Sci & Technol, Innovat Acad Precis Measurement Sci & Technol, Wuhan 430071, Peoples R China 8.Wuhan Univ Sci & Technol, Wuhan, Peoples R China
推荐引用方式 GB/T 7714	Xiao, Hang,Wang, Jian,Tan, Huan,et al. Robust heteronuclear correlations for proteins in ultrafast magic-angle spinning solid-state NMR. 2025.