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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...
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 Folding01:22

Protein Folding

Overview
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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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

Enzyme-mediated protein refolding.

Jun Okada1, Tatsuo Maruyama, Konomi Motomura

  • 1Department of Applied Chemistry, Graduate School of Engineering and Center for Future Chemistry, Kyushu University, 744 Moto-oka, Fukuoka 819-0395, Japan.

Chemical Communications (Cambridge, England)
|November 19, 2009
PubMed
Summary
This summary is machine-generated.

This study shows that a urease-catalyzed reaction can efficiently refold denatured proteins by gradually removing urea. This method avoids the need for large-volume dilution, offering a simpler protein refolding technique.

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Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Enzymology

Background:

  • Protein denaturation often requires chaotropic agents like urea.
  • Removing urea typically involves large-volume dilution, which can be inefficient.
  • Protein refolding is crucial for protein function and biotechnological applications.

Purpose of the Study:

  • To investigate a novel method for protein refolding using a urease-catalyzed reaction.
  • To demonstrate efficient protein refolding by gradually removing urea from denatured protein solutions.
  • To establish a protein refolding technique that avoids large-volume dilution.

Main Methods:

  • Utilized a urease-catalyzed reaction to hydrolyze urea.
  • Applied the method to a denatured protein solution with high urea concentration.
  • Monitored protein refolding efficiency.

Main Results:

  • The urease-catalyzed reaction effectively removed urea from the protein solution.
  • Efficient protein refolding was achieved using this method.
  • The process did not require large-volume dilution.

Conclusions:

  • Urease-catalyzed urea removal is an effective strategy for protein refolding.
  • This method offers an alternative to traditional large-volume dilution techniques.
  • The approach simplifies protein refolding protocols in biochemical research.