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Related Concept Videos

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...
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
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 8, 2026

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
08:04

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

Structural proteomics by NMR spectroscopy.

Joon Shin1, Woonghee Lee, Weontae Lee

  • 1Department of Biochemistry, College of Life Science & Biotechnology, Yonsei University, Seodaemoon-Gu, Shinchon-dong, Seoul 120-740, Korea. joonee@spin.yonsei.ac.kr

Expert Review of Proteomics
|September 3, 2008
PubMed
Summary
This summary is machine-generated.

Structural proteomics uses 3D protein structures to uncover gene functions and identify drug targets. Nuclear Magnetic Resonance (NMR) spectroscopy is key to this high-throughput research, enabling genomic-scale studies.

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Last Updated: May 8, 2026

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Area of Science:

  • Structural biology
  • Proteomics
  • Genomics

Background:

  • Postgenomic era research focuses on elucidating structure-function relationships.
  • Uncharacterized proteins require functional annotation and target identification for drug design and engineering.

Purpose of the Study:

  • To highlight the role of structural proteomics in assigning functions to hypothetical proteins.
  • To emphasize the contribution of Nuclear Magnetic Resonance (NMR) spectroscopy in this field.

Main Methods:

  • Predicting 3D protein structures for unannotated proteins.
  • Utilizing NMR spectroscopy for high-throughput structure determination.
  • Leveraging advances in NMR hardware, data acquisition, sample preparation, and automated analysis.

Main Results:

  • Successful prediction of 3D structures for hypothetical proteins, leading to the identification of their biological functions.
  • Demonstration of NMR spectroscopy's effectiveness in structural proteomics over the past decade.
  • Development of advanced techniques for high-throughput structure determination.

Conclusions:

  • NMR spectroscopy is crucial for genomic-scale structural proteomics.
  • NMR-based structural proteomics, combined with X-ray crystallography, will build a comprehensive database for functional prediction.
  • This approach aids in understanding hypothetical proteins identified by genome projects.