Super-Resolution solid-state NMR Spectroscopy

IF 1.9 3区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Olivia Gampp, Riccardo Cadalbert, Roland Riek, Sarah A. Overall
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引用次数: 0

Abstract

Solid-state NMR spectroscopy is often limited by low spectral resolution, a problem typically addressed using fast magic-angle spinning (MAS) and ¹H detection, which require costly specialized hardware. Here, we demonstrate that the super-resolution method—previously applied in solution-state NMR—can be successfully implemented in solid-state NMR to enhance resolution. Applying dynamic number of scans (DNS) sampling to 2D ¹³C-¹³C DARR experiments on the AP205 capsid protein yielded an effective doubling of resolution, halving peak widths from ~ 180 Hz to ~ 87 Hz. Furthermore, DNS acquisition provides a significant advantage over post-acquisition apodization of conventional data with a 20% gain in sensitivity, yielding 309 more detectable peaks with 20% more sequential contacts and 25% more long-range contacts. This method is simple to implement and provides a powerful, accessible strategy to greatly improve the quality of solid-state NMR spectra applicable at all MAS frequencies.

超分辨率固态核磁共振光谱学。
固态核磁共振光谱通常受到低光谱分辨率的限制,通常使用快速魔角旋转(MAS)和¹H检测来解决这个问题,这需要昂贵的专用硬件。在这里,我们证明了以前应用于溶液态核磁共振的超分辨率方法可以成功地应用于固态核磁共振以提高分辨率。将动态扫描次数(DNS)采样应用于AP205衣壳蛋白的2D¹³C-¹³C DARR实验,可以有效地将分辨率提高一倍,将峰宽从~ 180 Hz降低到~ 87 Hz。此外,与传统数据的采集后apoapozation相比,DNS采集提供了显著的优势,灵敏度提高了20%,产生了309个可检测的峰值,顺序接触增加了20%,远程接触增加了25%。该方法易于实现,并提供了一个强大的,可访问的策略,以大大提高适用于所有MAS频率的固态核磁共振谱的质量。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Journal of Biomolecular NMR
Journal of Biomolecular NMR 生物-光谱学
CiteScore
6.00
自引率
3.70%
发文量
19
审稿时长
6-12 weeks
期刊介绍: The Journal of Biomolecular NMR provides a forum for publishing research on technical developments and innovative applications of nuclear magnetic resonance spectroscopy for the study of structure and dynamic properties of biopolymers in solution, liquid crystals, solids and mixed environments, e.g., attached to membranes. This may include: Three-dimensional structure determination of biological macromolecules (polypeptides/proteins, DNA, RNA, oligosaccharides) by NMR. New NMR techniques for studies of biological macromolecules. Novel approaches to computer-aided automated analysis of multidimensional NMR spectra. Computational methods for the structural interpretation of NMR data, including structure refinement. Comparisons of structures determined by NMR with those obtained by other methods, e.g. by diffraction techniques with protein single crystals. New techniques of sample preparation for NMR experiments (biosynthetic and chemical methods for isotope labeling, preparation of nutrients for biosynthetic isotope labeling, etc.). An NMR characterization of the products must be included.
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