Probing amide bond nitrogens in solids using ¹⁴N NMR spectroscopy

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• 作者：Sasa Antonijevic ; Nicholas Halpern-Manners
• 关键词：NMR spectroscopy ; Solid state ; Nitrogen-14 ; Peptides ; Proteins
• 刊名：Solid State Nuclear Magnetic Resonance
• 出版年：2008
• 期刊代码：83_09262040
• 类别：ce
• 出版时间：May 2008
• 卷：33
• 期：4
• 页码：82-87
• 文件大小：265 K

摘要

A novel two-dimensional nuclear magnetic resonance (NMR) experiment is proposed for indirect observation of ¹⁴N nuclei in various types of nitrogen-containing solids. In a method somewhat similar to the heteronuclear single-quantum correlation (HSQC) experiment widely used for protein structure determination in solutions, this technique correlates spin S=1/2 nuclei, e.g., ¹H, ¹³C, with the ¹⁴N spin I=1 nucleus in solids. The present experiment, however, transfers coherence from neighboring ¹H or ¹³C nuclei to ¹⁴N via a combination of J-couplings and residual dipolar splittings (RDS). Projections of the two-dimensional NMR spectra onto the ¹⁴N dimension yield powder patterns that reflect the ¹⁴N quadrupolar interaction, which can be used to study molecular structure and dynamics. Indirect detection of amide nitrogen-14 via ¹H and ¹³C is shown experimentally on a model compound of N-acetyl-glycine.