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Related Concept Videos

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: Jun 4, 2026

Protein Complex Affinity Capture from Cryomilled Mammalian Cells
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Published on: December 9, 2016

CoESPRIT: a library-based construct screening method for identification and expression of soluble protein complexes.

Yingfeng An1, Patrick Meresse, Philippe J Mas

  • 1Grenoble Outstation, European Molecular Biology Laboratory, BP181 Grenoble, France.

Plos One
|March 3, 2011
PubMed
Summary

CoESPRIT enables efficient co-expression of soluble protein complexes. This method aids in obtaining stable protein complexes for structural and biophysical studies, even for poorly understood proteins.

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Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular biology

Background:

  • Protein complex studies require large amounts of soluble protein.
  • Co-expression is vital for stabilizing unstable subunits.
  • Defining constructs for co-expression is challenging for poorly understood proteins.

Purpose of the Study:

  • To develop an efficient method for expressing soluble protein complexes.
  • To overcome challenges in defining co-expression constructs for unknown proteins.
  • To facilitate structural, biophysical, and functional studies of protein complexes.

Main Methods:

  • CoESPRIT, a modified random library construct screen, was developed.
  • A library of target constructs was screened against a fixed bait protein.
  • Proof-of-principle studies involved influenza polymerase subunits and importin alpha.

Main Results:

  • CoESPRIT successfully identified and isolated stable protein complexes.
  • C-terminal fragments of influenza PB2 were isolated using importin alpha as bait.
  • Co-folded complexes of PB1 and PB2 subunits were identified.

Conclusions:

  • CoESPRIT is an efficient, automated strategy for obtaining recombinant protein complexes.
  • The method yields sufficient protein for structural and biophysical analyses.
  • CoESPRIT aids in studying protein complexes with individually unstable or co-folding subunits.