Fast Magic‐Angle Spinning 19F NMR Spectroscopy of HIV‐1 Capsid Protein Assemblies,Angewandte Chemie International Edition

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Fast Magic‐Angle Spinning 19F NMR Spectroscopy of HIV‐1 Capsid Protein Assemblies
Angewandte Chemie International Edition ( IF 16.1 ) Pub Date : 2018-10-19 , DOI: 10.1002/anie.201809060
Mingzhang Wang _{1,

2} , Manman Lu _{1,

2,

3} , Matthew P Fritz _{1,

2} , Caitlin M Quinn ₁ , In-Ja L Byeon _{2,

3} , Chang-Hyeock Byeon _{2,

3} , Jochem Struppe ₄ , Werner Maas ₄ , Angela M Gronenborn _{2,

3} , Tatyana Polenova _{1,

2}

Affiliation

¹⁹F NMR spectroscopy is an attractive and growing area of research with broad applications in biochemistry, chemical biology, medicinal chemistry, and materials science. We have explored fast magic angle spinning (MAS) ¹⁹F solid‐state NMR spectroscopy in assemblies of HIV‐1 capsid protein. Tryptophan residues with fluorine substitution at the 5‐position of the indole ring were used as the reporters. The ¹⁹F chemical shifts for the five tryptophan residues are distinct, reflecting differences in their local environment. Spin‐diffusion and radio‐frequency‐driven‐recoupling experiments were performed at MAS frequencies of 35 kHz and 40–60 kHz, respectively. Fast MAS frequencies of 40–60 kHz are essential for consistently establishing ¹⁹F–¹⁹F correlations, yielding interatomic distances of the order of 20 Å. Our results demonstrate the potential of fast MAS ¹⁹F NMR spectroscopy for structural analysis in large biological assemblies.

中文翻译：

HIV-1 衣壳蛋白组装体的快速魔角旋转 19F NMR 光谱

¹⁹ F NMR 光谱是一个有吸引力且不断发展的研究领域，在生物化学、化学生物学、药物化学和材料科学中具有广泛的应用。我们探索了 HIV-1 衣壳蛋白组装中的快速魔角旋转 (MAS) ¹⁹ F 固态核磁共振波谱。吲哚环 5 位被氟取代的色氨酸残基被用作报告分子。五个色氨酸残基的¹⁹ F 化学位移是不同的，反映了它们当地环境的差异。自旋扩散和射频驱动重耦合实验分别在 35 kHz 和 40-60 kHz 的 MAS 频率下进行。 40-60 kHz 的快速 MAS 频率对于一致建立¹⁹ F- ¹⁹ F 相关性至关重要，从而产生 20 Å 量级的原子间距离。我们的结果证明了快速 MAS ¹⁹ F NMR 光谱在大型生物组件结构分析中的潜力。

更新日期：2018-10-19

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