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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...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
Protein Folding01:22

Protein Folding

Overview
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
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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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Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Artificial chaperone-assisted refolding in a microchannel.

Etsushi Yamamoto1, Satoshi Yamaguchi, Naoki Sasaki

  • 1Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.

Bioprocess and Biosystems Engineering
|September 4, 2009
PubMed
Summary

Artificial chaperone-assisted (ACA) refolding in microchannels significantly improves protein refolding yields by preventing aggregation. This method enhances yields for model proteins like lysozyme and alpha-glucosidase compared to simple dilution.

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Published on: October 23, 2016

Area of Science:

  • Biochemistry
  • Chemical Engineering
  • Molecular Biology

Background:

  • Protein refolding is crucial for producing functional proteins.
  • Simple dilution methods in microchannels often cause protein aggregation, reducing refolding efficiency.
  • Protein aggregation in microchannels leads to low yields and adherence to channel walls.

Purpose of the Study:

  • To investigate an artificial chaperone-assisted (ACA) refolding method for inhibiting protein aggregation in microchannels.
  • To enhance protein refolding yields using ACA techniques in a microfluidic system.
  • To compare the efficacy of ACA refolding with simple dilution for model proteins.

Main Methods:

  • Utilized an artificial chaperone-assisted (ACA) refolding approach incorporating detergents and beta-cyclodextrin.
  • Employed microchannel systems for protein refolding experiments.
  • Assessed refolding yields and observed protein aggregation using microscopic analysis for hen egg white lysozyme and yeast alpha-glucosidase.

Main Results:

  • ACA refolding successfully suppressed protein aggregation in microchannels for both lysozyme and alpha-glucosidase.
  • Lysozyme refolding yield increased by 40% using the ACA method compared to simple dilution.
  • Alpha-glucosidase refolding yield with ACA was approximately three times higher than with simple dilution, reaching about 50%.

Conclusions:

  • Artificial chaperone-assisted (ACA) refolding is an effective strategy to prevent protein aggregation in microfluidic systems.
  • The ACA method significantly improves protein refolding yields compared to traditional simple dilution.
  • ACA refolding in microchannels offers a promising approach for efficient protein refolding.