高效溶剂抑制与绝热反演的1h检测固态核磁共振

IF 1.3 3区生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY

Journal of Biomolecular NMR Pub Date : 2021-10-21 DOI:10.1007/s10858-021-00384-8

Tatsuya Matsunaga, Ryotaro Okabe, Yoshitaka Ishii

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引用次数: 4

摘要

本研究提出了一种概念上的新型溶剂抑制方案，即“溶剂抑制液体信号与绝热脉冲”(SLAP)，用于生物分子和其他体系的1h检测多维固态核磁共振(SSNMR)。采用超快魔角纺丝，在60 kHz的纺丝速率下，对均匀13C-和15n -标记的GB1样品进行了二维13C/1H SSNMR数据检测，结果表明，在平均射频功率为2/3的情况下，SLAP方案比传统的SSNMR溶剂抑制方案的溶剂抑制性能提高了3.5倍(Zhou和Rienstra, J Magn Reson 192:167-172, 2008)。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

Efficient solvent suppression with adiabatic inversion for 1H-detected solid-state NMR

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Efficient solvent suppression with adiabatic inversion for 1H-detected solid-state NMR

This study introduces a conceptually new solvent suppression scheme with adiabatic inversion pulses for ¹H-detected multidimensional solid-state NMR (SSNMR) of biomolecules and other systems, which is termed “Solvent suppression of Liquid signal with Adiabatic Pulse” (SLAP). ¹H-detected 2D ¹³C/¹H SSNMR data of uniformly ¹³C- and ¹⁵N-labeled GB1 sample using ultra-fast magic angle spinning at a spinning rate of 60 kHz demonstrated that the SLAP scheme showed up to 3.5-fold better solvent suppression performance over a traditional solvent-suppression scheme for SSNMR, MISSISSIPPI (Zhou and Rienstra, J Magn Reson 192:167–172, 2008) with 2/3 of the average RF power.

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来源期刊

Journal of Biomolecular NMR 生物-光谱学

CiteScore

6.00

自引率

3.70%

发文量

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.