Keywords

Peptides And Proteins, Natural Abundance, 15N, Nmr, Heteronuclear Multiple Quantum Coherence Spectroscopy

Abstract

The nuclear magnetic resonance (NMR) study of 15N is a key point in protein solution structure analysis. The first step in using NMR to study the solution conformation of biological macromolecules is often the measurement of the heteronuclear multiple quantum coherence (HMQC) spectrum of 15N To determine the attribution of the amide proton, and then conduct other spectral experiments such as total correlation spectrum (TOCSY) and nuclear Overhauser enhanced spectrum (NOESY). Since the natural abundance of 15N is very low (about 0.37%), it is directly There are almost no reports on NMR studies of naturally abundant 15N in proteins. Three-dimensional and multi-dimensional NMR experiments can more conveniently and effectively determine the structure of protein solutions under the conditions of 15N enrichment treatment of samples, but many proteins are obtained from natural substances. After extraction, the purification process is very complicated, and it is even more difficult to obtain 15N-labeled protein samples. Isotope labeling technology is very cumbersome and expensive, and not every laboratory engaged in protein solution structure research can achieve it. Therefore, for proteins NMR research on natural abundance 15N is of great significance.

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Original research done by Huang He, Mao Xian

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