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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
Other Stress Responses in Bacteria01:30

Other Stress Responses in Bacteria

Bacteria have global regulatory systems that control several types of stress mechanisms. These include Pho regulon and the heat shock response, which are essential systems for environmental adaptation, such as nutrient limitation and proteotoxic stress. The Pho regulon and the heat shock response exemplify bacterial resilience, enabling rapid adaptation to fluctuating environmental conditions.Pho RegulonBacteria require phosphorus for essential cellular processes, including nucleic acid...

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Related Experiment Video

Updated: Jun 15, 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

The high pH and pH-shift refolding technology.

Xinli Lin1, Tomomi Umetsu

  • 1GeneCopoeia, Inc., 9620 Medical Center Dr., Rockville, MD 20850, USA. xllin@genecopoeia.com

Current Pharmaceutical Biotechnology
|March 10, 2010
PubMed
Summary
This summary is machine-generated.

We developed Ph-Fold technology for refolding difficult proteins. This high-pH, pH-shift method aids academic research and industrial drug development for important protein targets.

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Last Updated: Jun 15, 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:

  • Biotechnology
  • Protein Chemistry
  • Drug Discovery

Background:

  • Many therapeutic proteins are difficult to refold.
  • Inclusion bodies from E. coli expression pose refolding challenges.
  • Efficient refolding methods are crucial for protein drug development.

Purpose of the Study:

  • To develop a novel high-pH, pH-shift refolding technology (Ph-Fold).
  • To demonstrate the efficacy of Ph-Fold for difficult-to-refold proteins.
  • To facilitate protein drug development and structural genomics.

Main Methods:

  • E. coli production of inclusion bodies.
  • High-pH solubilization followed by pH-shift refolding screening.
  • Automated screening of refolding conditions.
  • Protein refolding assessment without functional assays.

Main Results:

  • Successfully refolded several 'difficult-to-refold' proteins.
  • Identified important drug targets and protein drug candidates.
  • Developed an automated refolding system based on Ph-Fold technology.

Conclusions:

  • Ph-Fold technology offers a robust solution for refolding challenging proteins.
  • The automated system accelerates structural genomics and proteomics.
  • This technology supports genomic-scale drug development efforts.