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Related Concept Videos

Formation of Complex Ions03:45

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A type of Lewis acid-base chemistry involves the formation of a complex ion (or a coordination complex) comprising a central atom, typically a transition metal cation, surrounded by ions or molecules called ligands. These ligands can be neutral molecules like H2O or NH3, or ions such as CN− or OH−. Often, the ligands act as Lewis bases, donating a pair of electrons to the central atom. These types of Lewis acid-base reactions are examples of a broad subdiscipline called coordination...
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Enthalpy changes are typically tabulated for reactions in which both the reactants and products are at the same conditions. A standard state is a commonly accepted set of conditions used as a reference point for the determination of properties under other different conditions. For chemists, the IUPAC standard state refers to materials under a pressure of 1 bar and solutions at 1 M and does not specify a temperature. Many thermochemical tables list values with a standard state of 1 atm. Because...
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Related Experiment Video

Updated: Jan 31, 2026

Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein GST-RhoAG17A from Epithelial Cell Lysates
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GST Pull-Down Assay to Measure Complex Formations.

Sun-Yong Kim1, Toshio Hakoshima2

  • 1Structural Biology Laboratory, Nara Institute of Science and Technology, Nara, Japan.

Methods in Molecular Biology (Clifton, N.J.)
|December 20, 2018
PubMed
Summary
This summary is machine-generated.

The GST pull-down assay is a quick in vitro method to study protein interactions. It uses a "bait" protein to identify and quantify binding "prey" molecules.

Keywords:
Direct protein–protein interactionGST pull-down assayGlutathione S-transferaseGlutathione-conjugated resinIn vitro assayScreening of binding partners

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Protein-protein interactions are fundamental to cellular processes.
  • Understanding these interactions is crucial for drug discovery and disease research.
  • In vitro methods offer controlled environments to study specific molecular interactions.

Purpose of the Study:

  • To describe the GST pull-down assay as a method for analyzing protein interactions.
  • To highlight its utility in studying direct protein-protein or protein-ligand binding.
  • To explain its application in estimating binding affinity.

Main Methods:

  • Utilizes a "bait" protein fused to Glutathione S-transferase (GST).
  • Expresses the GST-fusion "bait" protein using E. coli or baculovirus systems.
  • Incubates the "bait" with putative binding partner "prey" proteins or ligands.

Main Results:

  • Successfully identifies and captures binding partners.
  • Allows for the qualitative and quantitative assessment of interactions.
  • Enables estimation of the binding affinity between interacting molecules.

Conclusions:

  • The GST pull-down assay is an effective and rapid in vitro technique.
  • It is suitable for validating direct interactions between purified proteins.
  • Provides a reliable method for assessing protein-ligand binding extent.