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Related Concept Videos

Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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...
Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
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,...
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...

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Related Experiment Video

Updated: Jun 6, 2026

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Recent developments in protein-ligand affinity mass spectrometry.

Niels Jonker1, Jeroen Kool, Hubertus Irth

  • 1BioMolecular Analysis, Department of Chemistry and Pharmaceutical Sciences, Faculty of Sciences, VU University Amsterdam, The Netherlands.

Analytical and Bioanalytical Chemistry
|November 9, 2010
PubMed
Summary

This review covers mass spectrometry techniques for screening protein-ligand interactions. These methods aid in identifying bioactive compounds from natural products and chemical libraries for drug discovery.

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Pharmacology

Background:

  • Protein-ligand interactions are crucial in biological processes and drug discovery.
  • Mass spectrometry offers sensitive detection for analyzing these interactions.
  • Existing methods require optimization for screening diverse compound libraries.

Purpose of the Study:

  • To review direct and indirect mass spectrometry-based technologies for screening protein-ligand interactions.
  • To highlight recent advancements in these screening technologies.
  • To discuss their applicability in drug lead generation and development.

Main Methods:

  • Overview of direct screening methods using mass spectrometry.
  • Discussion of indirect methods involving affinity purification prior to mass spectrometry detection.
  • Focus on techniques applicable to metabolic profiling, natural product screening, and combinatorial chemistry libraries.

Main Results:

  • Mass spectrometry-based screening enables selection or affinity purification of ligands from complex mixtures.
  • These technologies are valuable for identifying bioactive metabolites and compounds from various sources.
  • Recent developments have enhanced the efficiency and scope of these screening approaches.

Conclusions:

  • Mass spectrometry-based screening technologies are powerful tools for identifying novel drug leads.
  • The discussed methods facilitate the analysis of protein-ligand interactions in diverse chemical contexts.
  • Continued innovation in these techniques will accelerate drug discovery and development pipelines.