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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 31, 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

Refolding your protein with a little help from REFOLD.

Jennifer Phan1, Nasrin Yamout, Jason Schmidberger

  • 1Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC, Australia.

Methods in Molecular Biology (Clifton, N.J.)
|June 30, 2011
PubMed
Summary

Recombinant protein production often involves refolding proteins from inclusion bodies. This study offers practical guidance and standard protocols, leveraging the REFOLD database to aid scientists in designing effective refolding procedures.

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Last Updated: May 31, 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

Intracellular Refolding Assay
07:18

Intracellular Refolding Assay

Published on: January 24, 2012

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
13:52

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae

Published on: July 9, 2013

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Chemistry

Background:

  • Recombinant protein production frequently involves isolating proteins from insoluble inclusion bodies.
  • Solubilization and refolding are critical steps, but existing literature offers fragmented, ad hoc protocols.
  • This heterogeneity presents significant challenges for protein scientists seeking to optimize refolding.

Purpose of the Study:

  • To provide practical considerations and standardized protocols for protein refolding.
  • To introduce the REFOLD database as a resource for designing and modifying refolding procedures.
  • To address the challenges posed by diverse and inconsistent refolding protocols in the literature.

Main Methods:

  • Review and synthesis of practical considerations in protein refolding.
  • Presentation of several standard refolding protocols.
  • Demonstration of how to utilize the REFOLD database for protocol design and modification.

Main Results:

  • A framework for understanding practical aspects of protein refolding is presented.
  • Standardized protocols are offered to streamline the refolding process.
  • The REFOLD database is highlighted as a valuable, accessible resource for optimizing recombinant protein refolding.

Conclusions:

  • Effective protein refolding is crucial for recombinant protein production.
  • Standardized protocols and accessible databases like REFOLD can overcome challenges posed by fragmented literature.
  • The REFOLD database empowers scientists to design and adapt refolding strategies for diverse proteins.