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Related Concept Videos

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 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 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...
Micelles01:30

Micelles

Micelle formation is an intricate process that hinges on the properties of amphiphilic or amphipathic molecules and the conditions of the system in which they are found. Amphiphilic molecules, which have both hydrophilic (water-attracting) and hydrophobic (water-repelling) parts, play a critical role in this process.In aqueous environments, these molecules arrange themselves such that their hydrophilic heads are turned towards the water phase, while their hydrophobic tails are oriented away...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

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Related Experiment Video

Updated: Jul 4, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

Protein refolding in reversed micelles.

A J Hagen1, T A Hatton, D I Wang

  • 1Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.

Biotechnology and Bioengineering
|April 25, 1990
PubMed
Summary

This study introduces a novel reversed micelle process for individual protein refolding, preventing aggregation. This method successfully refolded bovine pancreatic ribonuclease A, recovering its full activity.

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Related Experiment Videos

Last Updated: Jul 4, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
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Published on: July 4, 2016

Real-time Analyses of Retinol Transport by the Membrane Receptor of Plasma Retinol Binding Protein
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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

Area of Science:

  • Biochemistry
  • Chemical Engineering
  • Biotechnology

Background:

  • Protein misfolding and aggregation are significant challenges in biotechnology.
  • Existing refolding methods often suffer from low yields due to intermolecular interactions.

Purpose of the Study:

  • To develop a novel method for isolating and refolding denatured proteins individually.
  • To prevent protein aggregation during the refolding process.

Main Methods:

  • Utilizing reversed micelles (aqueous droplets of AOT surfactant in isooctane) to encapsulate single protein molecules.
  • Transferring denatured bovine pancreatic ribonuclease A into reversed micelles.
  • Reducing denaturant concentration via extractive stages.
  • Facilitating disulfide bond reoxidation using glutathione.
  • Extracting refolded protein back into an aqueous solution.

Main Results:

  • Achieved isolation of single denatured protein molecules within reversed micelles, enabling independent refolding.
  • Demonstrated successful refolding and recovery of full enzymatic activity of bovine pancreatic ribonuclease A.
  • Showcased efficient transfer of denatured enzyme into reversed micelles and subsequent extraction of refolded enzyme.

Conclusions:

  • Reversed micelle encapsulation provides an effective strategy to prevent protein aggregation during refolding.
  • This novel process offers a promising approach for high-yield protein refolding in biotechnological applications.