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Related Concept Videos

NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

11.1K
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...
11.1K
NMR Spectroscopy of Aromatic Compounds01:14

NMR Spectroscopy of Aromatic Compounds

6.3K
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.
6.3K
NMR Spectroscopy of Benzene Derivatives01:34

NMR Spectroscopy of Benzene Derivatives

11.1K
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...
11.1K
NMR Spectroscopy: Chemical Shift Overview01:15

NMR Spectroscopy: Chemical Shift Overview

3.3K
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...
3.3K
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

3.2K
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...
3.2K
NMR and Mass Spectroscopy of Carboxylic Acids01:30

NMR and Mass Spectroscopy of Carboxylic Acids

5.3K
In ¹H NMR spectroscopy, acidic protons (–COOH) of carboxylic acids are highly deshielded and absorb far downfield, at around 9–12 ppm. The chemical shift value depends on the concentration and solvent used.
While α protons of carboxylic acids absorb at 2–2.5 ppm, β protons absorb further upfield.
Carboxylic acids are easily identified by dissolving them in deuterium oxide, which results in a rapid exchange of the acidic protons with deuterium. This leads to the...
5.3K

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Related Experiment Video

Updated: Jan 30, 2026

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

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Solid-State NMR Spectroscopy of RNA.

Alexander Marchanka1, Teresa Carlomagno2

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

Methods in Enzymology
|January 15, 2019
PubMed
Summary
This summary is machine-generated.

Solid-state NMR overcomes limitations of solution-state NMR for studying large RNA-protein complexes. This method enables detailed structural analysis of both RNA and protein components, revealing crucial interfaces.

Keywords:
MethodologyProtein–RNA complexesRNA–protein complexRibonucleic acidsSolid-state NMRStructure determination

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

  • Structural Biology
  • Biophysics
  • Molecular Biology

Background:

  • Understanding RNA structure is critical for elucidating its function and regulation in cellular processes.
  • RNA molecules, whether isolated or in complexes with proteins, present significant challenges for structural determination due to their complex conformational landscapes and inherent dynamics.
  • Solution-state Nuclear Magnetic Resonance (NMR) is ideal for studying dynamic RNA structures but is limited by the large molecular weights of RNA-protein complexes.

Purpose of the Study:

  • To present a developed methodology for determining RNA structure using solid-state NMR.
  • To highlight the advantages of solid-state NMR for studying large RNA-protein complexes, overcoming the limitations of solution-state NMR.
  • To detail methods for structural analysis of both RNA and protein components within these complexes.

Main Methods:

  • Application of solid-state NMR spectroscopy to analyze RNA structure.
  • Development and implementation of methods for resonance assignments in large biomolecular systems.
  • Collection of RNA-specific distance restraints to define structural constraints.
  • Techniques for detecting and characterizing protein-RNA interfaces.

Main Results:

  • Solid-state NMR effectively determines the structure of RNA, even within large complexes.
  • The methodology is not limited by molecular weight, enabling the study of previously intractable systems.
  • Successful application to both RNA and protein components, including the identification of interaction sites.

Conclusions:

  • Solid-state NMR is a powerful and versatile technique for elucidating the structures of large RNA-protein complexes.
  • This approach provides crucial insights into RNA function, regulation, and molecular interactions.
  • The described methods advance the field of structural biology for complex biomolecular assemblies.