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Related Concept Videos

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
The...
NMR Spectroscopy of Aromatic Compounds01:14

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. Consider...
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other axis.
NMR Spectrometers: Overview01:20

NMR Spectrometers: Overview

NMR spectrometers consist of a strong magnet, a radiofrequency transmitter, and a detector attached to a computer console for recording spectra of samples containing NMR-active nuclei. In first-generation NMR instruments called continuous-wave spectrometers, the resonance frequencies of the nuclei are determined by frequency-sweep or field-sweep methods. The magnetic field strength is fixed and the rf signal is swept in the former, while the radiofrequency signal is fixed and the magnetic field...
¹H NMR Signal Integration: Overview00:58

¹H NMR Signal Integration: Overview

The intensity of a signal, which can be represented by the area under the peak, depends on the number of protons contributing to that signal. The area under each peak is shown as a vertical line called an integral, with the integral value listed under it, as seen in the proton NMR spectrum of benzyl acetate. Each integral value is divided by the smallest integral value to obtain the ratio of the number of protons producing each signal. The ratio reveals the relative number of protons and not...

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Related Experiment Video

Updated: Jul 3, 2026

Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor
10:25

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

Published on: March 9, 2021

In-cell biochemistry using NMR spectroscopy.

David S Burz1, Alexander Shekhtman

  • 1Department of Chemistry, State University of New York at Albany, Albany, New York, United States of America.

Plos One
|July 16, 2008
PubMed
Summary
This summary is machine-generated.

This study introduces an in-cell NMR method to map protein interaction sites. The novel technique reveals how ubiquitin binding affects receptor tyrosine kinase sorting machinery, particularly when proteins are phosphorylated.

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Metabolomic Analysis of Rat Brain by High Resolution Nuclear Magnetic Resonance Spectroscopy of Tissue Extracts

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Last Updated: Jul 3, 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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Metabolomic Analysis of Rat Brain by High Resolution Nuclear Magnetic Resonance Spectroscopy of Tissue Extracts
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Metabolomic Analysis of Rat Brain by High Resolution Nuclear Magnetic Resonance Spectroscopy of Tissue Extracts

Published on: September 21, 2014

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cellular Biochemistry

Background:

  • Traditional in vitro methods study biological processes in conditions distant from the cellular environment.
  • A need exists for high-resolution techniques to study molecular interactions within living cells.

Purpose of the Study:

  • To develop a novel in-cell methodology for post-translational modification and interaction surface mapping.
  • To investigate the role of ubiquitin in the receptor tyrosine kinase (RTK) endocytic sorting machinery.

Main Methods:

  • Developed a novel in-cell methodology utilizing post-translational modification of interactor proteins.
  • Employed in-cell Nuclear Magnetic Resonance (NMR) to monitor structural changes on target proteins.
  • Studied the interaction of ubiquitin with phosphorylated and non-phosphorylated STAM2, Hrs, and the STAM2-Hrs heterodimer.

Main Results:

  • Demonstrated that ubiquitin binding is crucial for the processivity of the RTK sorting machinery network.
  • Observed a weakening of interaction networks when interactor proteins are phosphorylated.
  • Successfully mapped interaction surfaces of target proteins with modified interactors in-cell.

Conclusions:

  • The novel in-cell NMR methodology provides high-resolution insights into cellular biochemistry.
  • The findings elucidate the role of ubiquitin and phosphorylation in RTK endocytic sorting.
  • The method is adaptable for various post-translational modifications like ubiquitination and sumoylation.