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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

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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...

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Updated: Jun 15, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Refolding of difficult-to-fold proteins by a gradual decrease of denaturant using microfluidic chips.

Hiroshi Yamaguchi1, Masaya Miyazaki, Maria Portia Briones-Nagata

  • 1Nanotechnology Research Institute, National Institute of Advanced Industrial Science and Technology, 807-1 Shuku, Tosu, Saga 841-0052, Japan.

Journal of Biochemistry
|March 9, 2010
PubMed
Summary
This summary is machine-generated.

This study introduces a microfluidic chip method for efficient protein refolding from aggregates. The technique rapidly improves active protein recovery compared to traditional dialysis or dilution methods.

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Last Updated: Jun 15, 2026

Microfluidic Mixers for Studying Protein Folding
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Published on: April 10, 2012

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
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Crystallization of Proteins on Chip by Microdialysis for In Situ X-ray Diffraction Studies
12:38

Crystallization of Proteins on Chip by Microdialysis for In Situ X-ray Diffraction Studies

Published on: April 11, 2021

Area of Science:

  • Biochemistry
  • Biotechnology
  • Chemical Engineering

Background:

  • Protein refolding is crucial for active recombinant protein production from inclusion bodies.
  • Conventional methods like dialysis and dilution are slow and yield low active protein recovery.
  • Difficult-to-fold proteins present significant refolding challenges.

Purpose of the Study:

  • To develop a rapid and efficient protein refolding method using microfluidic technology.
  • To optimize denaturant concentration control via laminar flow in microchannels.
  • To evaluate the efficacy of microfluidic chips for refolding challenging proteins.

Main Methods:

  • Utilized controllable diffusion through laminar flow in microchannels to manage denaturant concentration.
  • Employed microfluidic chips with varying flow rates and multi-junctions to control buffer and denatured protein stream ratios.
  • Tested the chips with difficult-to-refold proteins: citrate synthase and zeta-associated protein 70-kDa protein kinase domain.

Main Results:

  • Achieved protein refolding within a short timeframe at room temperature.
  • Demonstrated improved refolding efficiency compared to dialysis and dilution methods.
  • Showcased successful refolding without requiring small molecules or chaperone proteins.

Conclusions:

  • Microfluidic chips offer a miniaturized, rapid, and efficient solution for active protein recovery from inclusion bodies.
  • This strategy significantly enhances protein refolding efficiency and speed.
  • The technology holds promise for broader applications in protein production and biotechnology.