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Related Concept Videos

Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

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Related Experiment Video

Updated: May 18, 2026

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
14:25

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Published on: December 12, 2017

Protein refolding using chemical refolding additives.

Satoshi Yamaguchi1, Etsushi Yamamoto, Teruhisa Mannen

  • 1Department of Chemistry & Biotechnology, School of Engineering, The University of Tokyo, Tokyo, Japan. yamaguchi@bio.t.u-tokyo.ac.jp

Biotechnology Journal
|September 12, 2012
PubMed
Summary
This summary is machine-generated.

Developing new synthetic refolding additives is key to improving protein production yields. These chemical additives help overcome challenges in protein refolding, making research more efficient.

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Area of Science:

  • Biochemistry
  • Protein Science
  • Chemical Engineering

Background:

  • Protein production is vital for research and industry, but low yields during refolding limit progress.
  • Inclusion bodies offer high upstream yields, yet downstream refolding remains a significant bottleneck.
  • Current refolding methods are protein-specific and require extensive trial-and-error, increasing costs and time.

Purpose of the Study:

  • To review novel synthetic refolding additives and chemical-additive-based methods.
  • To explore strategies for improving protein refolding efficiency and yield.
  • To advance towards a universal method for protein refolding.

Main Methods:

  • Focus on synthetic refolding additives and their development concepts.
  • Analysis of chemical additives that promote productive refolding over aggregation.
  • Review of novel technologies and materials for refolding optimization.

Main Results:

  • Synthetic additives can significantly enhance protein refolding yields.
  • Chemical additives help shift the balance towards productive refolding pathways.
  • Development of additive-based methods offers a more rational approach to refolding.

Conclusions:

  • Synthetic refolding additives represent a promising avenue for universal protein refolding.
  • These additives address the protein-dependency challenge of traditional methods.
  • Advancements in this area can streamline protein production for research and manufacturing.