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Protein Folding

Protein Folding

Protein Folding

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...

Molecular Chaperones and Protein Folding

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...

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Related Experiment Video

Updated: Mar 3, 2026

Microfluidic Mixers for Studying Protein Folding

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Protein Folding Using a Vortex Fluidic Device.

Joshua Britton^1,2, Joshua N Smith³, Colin L Raston⁴

¹Department of Chemistry, University of California, Irvine, 1102 Natural Sciences 2, Irvine, CA, 92697-2025, USA.

Methods in Molecular Biology (Clifton, N.J.)

|May 5, 2017

Summary

This summary is machine-generated.

Researchers developed a novel vortex fluidic device (VFD) for rapid protein folding. This VFD method efficiently refolds proteins from inclusion bodies, significantly reducing time and buffer volumes.

Keywords:

Bacterial protein expression Continuous flow Inclusion bodies Misfolded proteins Protein folding Vortex fluidics

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Last Updated: Mar 3, 2026

Microfluidic Mixers for Studying Protein Folding

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Published on: April 10, 2012

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Area of Science:

Biochemistry
Molecular Biology
Protein Engineering

Background:

Recombinant proteins are essential for biochemistry and molecular biology experiments.
Large, hydrophobic proteins often form insoluble inclusion bodies, hindering their use.
Existing methods for refolding proteins from inclusion bodies are inefficient and time-consuming.

Purpose of the Study:

To introduce a novel, rapid, and efficient method for protein folding.
To address the limitations of current protein refolding techniques.

Main Methods:

Utilized a vortex fluidic device (VFD) to apply mechanical energy to protein solutions.
Employed a continuous flow mode for processing large volumes of protein.
Investigated the VFD's efficacy in refolding proteins from inclusion bodies.

Main Results:

Achieved rapid and efficient protein folding using the VFD.
Demonstrated a 100-fold reduction in protein folding times.
Showcased a 100-fold reduction in buffer volumes required for folding.
Enabled processing of large protein solution volumes per day.

Conclusions:

The vortex fluidic device (VFD) offers a significantly improved method for recombinant protein refolding.
This VFD-based approach enhances efficiency and reduces resource consumption in protein production.
The VFD technology has broad implications for biochemical and molecular biology research and biopharmaceutical production.