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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...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Related Experiment Video

Updated: May 25, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

In-cell solid-state NMR as a tool to study proteins in large complexes.

Sina Reckel1, Jakob J Lopez, Frank Löhr

  • 1Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt, Germany.

Chembiochem : a European Journal of Chemical Biology
|February 3, 2012
PubMed
Summary

Detecting proteins in cells using nuclear magnetic resonance (NMR) spectroscopy is challenging due to slow molecular tumbling. This study shows solid-state NMR with flash-frozen cells successfully detects proteins and reveals backbone chemical shifts.

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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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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

Related Experiment Videos

Last Updated: May 25, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

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

Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Solution Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique for studying molecular structure and dynamics.
  • A significant limitation of solution NMR is slow molecular tumbling, which hinders the detection of large molecules or proteins within complex environments like cells.
  • Efficient detection of proteins in their native cellular milieu remains a challenge for biophysical characterization.

Purpose of the Study:

  • To overcome the limitations of solution NMR for detecting proteins in cellular environments.
  • To explore the utility of solid-state NMR spectroscopy combined with flash-freezing for protein detection within intact cells.
  • To obtain information on protein backbone chemical shifts directly from the cellular environment.

Main Methods:

  • Utilizing solid-state NMR spectroscopy, a technique less sensitive to molecular tumbling than solution NMR.
  • Implementing flash-freezing of cells to preserve their native structure and protein integrity.
  • Analyzing the resulting NMR spectra to identify protein signals and extract chemical shift information.

Main Results:

  • Demonstrated successful detection of proteins within the cellular environment using the described method.
  • Obtained valuable information regarding protein backbone chemical shifts directly from intact cells.
  • Overcame the challenge posed by slow molecular tumbling in solution NMR.

Conclusions:

  • Solid-state NMR spectroscopy in combination with flash-freezing is a viable approach for detecting proteins in cellular environments.
  • This technique provides insights into protein structure and dynamics within the complex cellular milieu.
  • The method offers a promising alternative for studying proteins in their native biological context.