Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Preparative protein refolding.

Anton P J Middelberg1

  • 1Department of Chemical Engineering, University of Cambridge, Pembroke Street, Cambridge CB2 3RA, UK. antonm@cheng.cam.ac.uk

Trends in Biotechnology
|September 11, 2002
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

An integrated and continuous downstream process for microbial virus-like particle vaccine biomanufacture.

Biotechnology and bioengineering·2022
Same author

Control strategy for multi-column continuous periodic counter current chromatography subject to fluctuating inlet stream concentration.

Journal of chromatography. A·2022
Same author

Chimeric Virus-Like Particles and Capsomeres Induce Similar CD8<sup>+</sup> T Cell Responses but Differ in Capacity to Induce CD4<sup>+</sup> T Cell Responses and Antibody Responses.

Frontiers in immunology·2020
Same author

Foaming properties of a peptide designed to form stimuli-responsive interfacial films.

Soft matter·2020
Same author

Nanoparticle elasticity regulates phagocytosis and cancer cell uptake.

Science advances·2020
Same author

Magnetic mesoporous silica nanoparticles end-capped with hydroxyapatite for pH-responsive drug release.

Journal of materials chemistry. B·2020
Same journal

Bacterial spores as a modular platform for the production of amyloids for materials.

Trends in biotechnology·2026
Same journal

The oriGen case and Mexico's regulatory blind spots in genomic biobanking.

Trends in biotechnology·2026
Same journal

A caspase-3-activated protein expression system for apoptosis visualization and apoptosis-pyroptosis conversion to boost antitumor activity.

Trends in biotechnology·2026
Same journal

Over 4 months of ethylene production using solid-state photosynthetic cell factories.

Trends in biotechnology·2026
Same journal

Closing the nitrogen loop in groundwater with biohybrid technologies.

Trends in biotechnology·2026
Same journal

Engineering environmental bacteria for whole-cell PET hydrolysis and assimilation.

Trends in biotechnology·2026
See all related articles

Efficient protein refolding from inclusion bodies is crucial for structural biology and biopharmaceutical development. Recent advancements in column-based methods and refolding analysis streamline this process, enabling rapid, automated condition determination and simplified scale-up.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biotechnology

Background:

  • Purified native protein is essential for structural biology and biopharmaceutical development.
  • Escherichia coli is a common host for protein expression but often produces insoluble inclusion bodies.
  • Efficient methods are needed to solubilize and refold these inclusion bodies.

Purpose of the Study:

  • To review and highlight recent advancements in protein refolding technologies.
  • To discuss methods that are scale-invariant, automatable, generic, and economical.
  • To identify developments that facilitate rapid, automated refolding condition determination and scale-up.

Main Methods:

  • Denaturant dilution techniques for protein refolding.
  • Column-based chromatography approaches for protein refolding.

Related Experiment Videos

  • Analysis of protein refolding products.

    • Main Results:

    • Column-based methods show promise for extending the range of refoldable proteins.
    • Developments in preparing denatured protein and analyzing refolding products address process bottlenecks.
    • Combined advancements facilitate automated refolding condition optimization.

    Conclusions:

    • Recent technological improvements enhance the efficiency and scope of protein refolding from inclusion bodies.
    • These advancements support the rapid and automated production of purified native proteins.
    • Simplified scale-up of refolding processes is a key outcome.