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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
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...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Related Experiment Video

Updated: Jul 16, 2026

The MultiBac Protein Complex Production Platform at the EMBL
13:51

The MultiBac Protein Complex Production Platform at the EMBL

Published on: July 11, 2013

Multiprotein expression strategy for structural biology of eukaryotic complexes.

Daniel J Fitzgerald1, Christiane Schaffitzel, Philipp Berger

  • 1ETH Zürich, Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg, CH-8093 Zürich, Switzerland.

Structure (London, England : 1993)
|March 16, 2007
PubMed
Summary

Researchers developed a rapid, automatable DNA recombination strategy for producing and modifying large eukaryotic protein complexes. This method enables efficient generation of multiple variants for structural biology studies.

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The Multifaceted Benefits of Protein Co-expression in Escherichia coli
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Related Experiment Videos

Last Updated: Jul 16, 2026

The MultiBac Protein Complex Production Platform at the EMBL
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Published on: July 11, 2013

Recombinant Protein Expression for Structural Biology in HEK 293F Suspension Cells: A Novel and Accessible Approach
11:20

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The Multifaceted Benefits of Protein Co-expression in Escherichia coli
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The Multifaceted Benefits of Protein Co-expression in Escherichia coli

Published on: February 5, 2015

Area of Science:

  • Molecular biology
  • Structural biology
  • Biochemistry

Background:

  • The cell is increasingly understood as a system of complex, multisubunit protein machines.
  • Studying these molecular machines at a detailed level necessitates efficient recombinant production methods.

Purpose of the Study:

  • To present and validate a novel strategy for the rapid production and modification of large, eukaryotic multiprotein complexes.
  • To demonstrate the utility of DNA recombination for creating diverse protein complex variants.

Main Methods:

  • Utilized a fully automatable DNA recombination process.
  • Engineered a system for rapid permutation and posttranslational modification of protein complexes.
  • Produced multiple variants of large, eukaryotic multiprotein complexes.

Main Results:

  • Successfully generated 12 distinct protein complex variants in parallel within weeks.
  • Achieved sufficient quantity and homogeneity of produced specimens for structural biology applications.
  • Validated the efficiency and scalability of the DNA recombination strategy.

Conclusions:

  • The developed DNA recombination strategy offers a rapid and automatable approach for producing and modifying complex eukaryotic protein machines.
  • This method significantly accelerates the generation of protein complex variants, facilitating structural biology research.