Probing amide bond nitrogens in solids using 14N NMR spectroscopy

被引:25
作者
Antonijevic, Sasa [1 ,2 ]
Halpern-Manners, Nicholas [1 ]
机构
[1] Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720, 1 Cyclotron Road
[2] Materials Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, 1 Cyclotron Road
关键词
Nitrogen-14; NMR spectroscopy; Peptides; Proteins; Solid state;
D O I
10.1016/j.ssnmr.2008.04.006
中图分类号
学科分类号
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. © 2008 Elsevier Inc. All rights reserved.
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页码:82 / 87
页数:5
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