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Related Concept Videos

NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

11.2K
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...
11.2K
NMR Spectroscopy of Aromatic Compounds01:14

NMR Spectroscopy of Aromatic Compounds

6.4K
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.
6.4K
NMR Spectroscopy of Benzene Derivatives01:34

NMR Spectroscopy of Benzene Derivatives

11.4K
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...
11.4K
NMR Spectroscopy: Chemical Shift Overview01:15

NMR Spectroscopy: Chemical Shift Overview

3.4K
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...
3.4K
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

3.3K
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...
3.3K
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: Feb 14, 2026

Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor
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Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor

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Interaction proteomics by using in-cell NMR spectroscopy.

Leonard Breindel1, David S Burz1, Alexander Shekhtman1

  • 1Department of Chemistry, University at Albany, State University of New York, Albany, NY 12222, USA.

Journal of Proteomics
|February 11, 2018
PubMed
Summary
This summary is machine-generated.

In-cell NMR spectroscopy reveals high-resolution protein structures and interactions within living cells. This technique aids in understanding how protein interactions regulate biological activity under physiological conditions.

Keywords:
In-cell NMRNMR spectroscopyProtein structureProtein-RNA interactionsProtein-protein interactions

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Understanding macromolecular interactions is key to deciphering biological activity.
  • Protein interactions are complex due to the vast number of proteins and their combinatorial interactions.
  • New methods are needed to structurally characterize protein complexes for a complete understanding of molecular networks.

Purpose of the Study:

  • To present in-cell NMR spectroscopic approaches for studying interaction proteomics.
  • To resolve high-resolution protein structures within prokaryotic and eukaryotic cells.
  • To analyze protein-target structural interactions, including those involving intrinsically disordered proteins.

Main Methods:

  • Utilizing in-cell NMR spectroscopy to study protein structures and interactions.
  • Developing methodologies for determining and analyzing both high and low affinity protein-target interactions.
  • Investigating functional interactions arising from structural protein-target interactions.

Main Results:

  • In-cell NMR spectroscopy enables the study of molecular structures and interactions under physiological conditions.
  • High-resolution protein structures can be resolved using this technique.
  • Methodologies for analyzing protein-target interactions, including those of intrinsically disordered proteins, are discussed.

Conclusions:

  • In-cell NMR spectroscopy offers a powerful approach to study protein interactions in their native cellular environment.
  • This technique sheds light on the structural basis of biological activity.
  • It contributes to a deeper understanding of molecular networks and cellular regulation.