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Related Concept Videos

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...
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...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

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Related Experiment Video

Updated: May 10, 2026

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
10:28

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Published on: November 2, 2018

Screening protein-small molecule interactions by NMR.

Ben Davis1

  • 1Vernalis Ltd (R&D), Great Abington, Cambridge, UK.

Methods in Molecular Biology (Clifton, N.J.)
|June 5, 2013
PubMed
Summary
This summary is machine-generated.

Nuclear magnetic resonance (NMR) is a label-free method for studying ligand-macromolecular receptor interactions. This technique provides atomic-resolution structural insights and identifies sample components without requiring labels.

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Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

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Area of Science:

  • Biophysics
  • Structural Biology
  • Chemical Biology

Background:

  • Nuclear magnetic resonance (NMR) is a powerful technique for investigating molecular interactions.
  • It functions as a label-free method, relying on inherent atomic resonances (e.g., 1H, 19F) in ligands and receptors.
  • NMR offers unique insights into sample composition, identifying contaminants and buffer components.

Purpose of the Study:

  • To highlight the utility of NMR spectroscopy in characterizing ligand-macromolecular receptor interactions.
  • To emphasize NMR's label-free nature and its ability to provide direct information on binding events.
  • To showcase NMR's capability in determining atomic-resolution structures, particularly for challenging protein-ligand systems.

Main Methods:

  • Utilizing observable resonances (1H, 19F) from ligands and receptors to detect binding.
  • Analyzing NMR parameters to differentiate between free and bound ligands.
  • Employing solution-phase NMR to avoid matrix-related artifacts, with mention of solid-state NMR techniques.
  • Leveraging advancements in cryogenic probeheads to enhance sensitivity and reduce sample requirements.

Main Results:

  • NMR directly reports on molecular components involved in binding interactions without labeling artifacts.
  • The technique can analyze interactions across a broad spectrum of affinities and timescales.
  • NMR provides detailed chemical information about all sample constituents.
  • Atomic-resolution structural data can be obtained for ligand-receptor complexes, including those resistant to crystallization.

Conclusions:

  • NMR is a versatile and informative technique for studying ligand-receptor interactions.
  • Its label-free nature, sensitivity improvements, and structural elucidation capabilities make it invaluable in biophysical studies.
  • NMR's ability to analyze sample composition and provide atomic-level structural detail offers significant advantages over other methods.