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

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

Abstract

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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高效溶剂抑制与绝热反演的1h检测固态核磁共振
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)。
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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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Solid state NMR spectral editing of histidine, arginine and lysine using Hadamard encoding. 15N-detected TROSY for 1H-15N heteronuclear correlation to study intrinsically disordered proteins: strategies to increase spectral quality. Evaluation of TOCSY mixing for sensitivity-enhancement in solid-state NMR and application of 4D experiments for side-chain assignments of the full-length 30 kDa membrane protein GlpG. Alpha-helices as alignment reporters in residual dipolar coupling analysis of proteins. Using temperature coefficients to support resonance assignment of intrinsically disordered proteins.
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