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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: Jun 9, 2026

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
06:09

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry

Published on: July 31, 2011

NMR-Based Methods for Protein Analysis.

Yunfei Hu1,2, Kai Cheng1, Lichun He1,2

  • 1Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences-Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430071, China.

Analytical Chemistry
|January 13, 2021
PubMed
Summary
This summary is machine-generated.

Nuclear magnetic resonance (NMR) spectroscopy enables atomic-level protein analysis in complex systems. Recent advancements, particularly in-cell NMR, provide crucial insights into protein dynamics and structure within living cells.

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Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
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Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
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Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

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Last Updated: Jun 9, 2026

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
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Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
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Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins

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07:40

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Published on: May 17, 2024

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Nuclear magnetic resonance (NMR) spectroscopy is a powerful tool for analyzing protein structure, interactions, and dynamics.
  • Recent advancements allow NMR studies in increasingly complex and physiological environments, including living cells.
  • In-cell NMR bridges structural biology and cell biology by enabling protein analysis within native cellular contexts.

Purpose of the Study:

  • To review recent developments in NMR methods for protein analysis in near-physiological environments.
  • To highlight the application of these methods, especially in-cell NMR, for structural determination and dynamics analysis.
  • To emphasize the unique insights gained from studying proteins in complex cellular systems.

Main Methods:

  • Advanced NMR spectroscopy techniques.
  • In-cell NMR methodologies.
  • Analysis of protein structure and dynamics in solution, solid-state, and cellular environments.

Main Results:

  • NMR methods have expanded to study proteins in complex systems like membrane mimetics and living cells.
  • In-cell NMR allows for structural determination and dynamics analysis of proteins within their native cellular environment.
  • These approaches offer unique insights into protein functional mechanisms that are difficult to obtain with traditional methods.

Conclusions:

  • NMR spectroscopy, particularly in-cell NMR, is a key technology for understanding protein function in physiological settings.
  • Continued development of NMR methods will further enhance our ability to study complex biological systems.
  • This approach is crucial for bridging the gap between structural and cell biology.