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NMR Spectroscopy Of Amines

NMR Spectroscopy Of Amines

In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...

Isotopes

Isotopes

Elements have a set number of protons that determines their atomic number (Z). For example, all atoms with eight protons are oxygen; however, the number of neutrons can vary for atoms of the same element. The sum of the number of protons and the number of neutrons is the mass number (A). Atoms with the same atomic number but different mass numbers are called isotopes. Elements can have multiple isotopes, for example, carbon-12, carbon-13, and carbon-14.
An element's atomic mass, or weight,...

NMR Spectroscopy of Aromatic Compounds

NMR Spectroscopy of Aromatic Compounds

Aromatic compounds can be identified or analyzed using proton NMR and carbon‐13 NMR. Typically, aromatic hydrogens or hydrogens directly bonded to the aromatic rings are strongly deshielded by the aromatic ring current. Therefore, they absorb in the range of 6.5–8.0 ppm in proton NMR spectra. For instance, aromatic hydrogens directly bonded to the benzene ring absorb at 7.3 ppm. However, aromatic hydrogens of larger rings absorb farther upfield or downfield than the ideal range.

NMR Spectroscopy of Benzene Derivatives

NMR Spectroscopy of Benzene Derivatives

Simple unsubstituted benzene has six aromatic protons, all chemically equivalent. Therefore, benzene exhibits only a singlet peak at δ 7.3 ppm in the 1H NMR spectrum. The observed shift is far downfield because the aromatic ring current strongly deshields the protons. Any substitution on the benzene ring makes the aromatic protons nonequivalent, and the protons split each other. The peak is, therefore, no longer a singlet and the splitting pattern and their associated coupling...

NMR Spectroscopy: Chemical Shift Overview

NMR Spectroscopy: Chemical Shift Overview

The position of the absorption signal of a sample is reported relative to the position of the signal of tetramethylsilane (TMS), which is added as an internal reference while recording spectra. The difference between the absorption frequencies of the sample and TMS (in Hz) is divided by the spectrometer operating frequency (in MHz) to obtain a dimensionless quantity called the chemical shift. It is reported on the δ (delta) scale and expressed in parts per million.
For instance, the proton...

NMR Spectroscopy: Spin–Spin Coupling

NMR Spectroscopy: Spin–Spin Coupling

The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved...

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Related Experiment Video

Updated: Feb 12, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Isotope labeling for studying RNA by solid-state NMR spectroscopy.

Alexander Marchanka¹, Christoph Kreutz², Teresa Carlomagno^3,4

¹Centre for Biomolecular Drug Research (BMWZ) and Institute of Organic Chemistry, Leibniz University Hannover, Schneiderberg 38, 30167, Hanover, Germany.

Journal of Biomolecular NMR

|April 14, 2018

Summary

Isotope labeling enhances solid-state nuclear magnetic resonance spectroscopy (ssNMR) for studying RNA structure. This technique overcomes challenges in analyzing large ribonucleoprotein complexes, enabling detailed molecular insights.

Keywords:

Atom selective-labelling of nucleotides Chemical synthesis of RNA In vitro RNA transcription RNA structure and dynamics Solid-state NMR

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Last Updated: Feb 12, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones

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Published on: March 26, 2017

Preparation of Fungal and Plant Materials for Structural Elucidation Using Dynamic Nuclear Polarization Solid-State NMR

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Published on: February 12, 2019

Area of Science:

Biochemistry and Molecular Biology
Structural Biology
Biophysical Chemistry

Background:

Nucleic acids are vital biomolecules, but their dynamic nature and high molecular weight pose challenges for structural studies.
Solid-state nuclear magnetic resonance (ssNMR) spectroscopy offers atomic resolution for large biomolecules in non-crystalline states.
ssNMR application to RNA is developing, facing hurdles like broad resonances and poor spectral dispersion.

Purpose of the Study:

To review methods for RNA production, purification, and isotope labeling for ssNMR.
To highlight the role of isotope labeling in overcoming ssNMR challenges for RNA analysis.
To demonstrate the utility of ssNMR and isotope labeling in studying RNA within large ribonucleoprotein complexes.

Main Methods:

Discusses RNA production and purification techniques.
Details various isotope labeling strategies (nucleotide-specific, atom-specific, segmental).
Emphasizes the application of ssNMR for structural analysis of RNA and ribonucleoprotein complexes.

Main Results:

Isotope labeling effectively resolves resonance overlaps and reduces line width in ssNMR spectra of RNA.
This enables detailed ssNMR studies of RNA domains within larger biomolecular assemblies.
Successful application of ssNMR and labeling to investigate ribonucleoprotein complexes is demonstrated.

Conclusions:

Isotope labeling is instrumental in advancing ssNMR applications for RNA structural biology.
ssNMR, enhanced by isotope labeling, provides atomic-level insights into RNA structure and function in complex biological systems.
This approach is crucial for understanding the role of RNA in large ribonucleoprotein complexes.