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

Screening protein refolding using surface plasmon resonance.

Daniel B Jones1, Matthew H Hutchinson, Anton P J Middelberg

  • 1Department of Chemical Engineering, University of Cambridge, Cambridge, UK. daniel.jones@contab.net

Proteomics
|March 30, 2004
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

Integrating virtual reality and large language models for team-based non-technical skills training and evaluation in the operating room.

npj digital surgery·2026
Same author

Preoperative 24-hour movement behaviors and early weight loss after metabolic bariatric surgery: a compositional analysis.

International journal of obesity (2005)·2025
Same author

Introducing Novel Surgical Clinical Correlations Into an Undergraduate Medical Anatomy Course.

Clinical anatomy (New York, N.Y.)·2025
Same author

Surgical journal clubs in the digital world: Old wine in new barrels.

Surgery·2025
Same author

Examining the Impact of Eliminating the X Waiver on Buprenorphine Dispensation in 63 Counties in Pennsylvania.

Substance use & addiction journal·2024
Same author

In Brief.

Current problems in surgery·2024
Same journal

Light-Induced Proteomic Changes in Pseudomonas aeruginosa Biofilms.

Proteomics·2026
Same journal

Decade-Resolved Proteomic Profiling of Gastric Cancer FFPE Archives: Evaluating Storage-Associated Shifts and Signal Stability Over 50 Years.

Proteomics·2026
Same journal

Proteome-Scale Mining of Metal-Associated Proteins of Monkeypox Virus.

Proteomics·2026
Same journal

Optimized Sample Handling Minimizes Peptide Adsorption to Plastics to Enable High Sensitivity Evosep Based Chemical Proteomics.

Proteomics·2026
Same journal

Toward Predicting Pandemic Potential: A Comparative Analysis of Virus-Host Interactions Between Diverse Influenza A Viruses and the Human Innate Immune System.

Proteomics·2026
Same journal

Functional Divergence of Mucus in Pacific Oyster (Crassostrea gigas): Insights From Integrated Proteomic and Rheological Study.

Proteomics·2026
See all related articles

Surface plasmon resonance (SPR) screening efficiently identifies optimal refolding conditions for denatured glutathione-S-transferase (GST). This method enables rapid optimization of protein refolding yields for biotechnological applications.

Area of Science:

  • Biochemistry
  • Biotechnology
  • Analytical Chemistry

Background:

  • Protein refolding is crucial for obtaining active proteins from denatured or insoluble forms.
  • Glutathione-S-transferase (GST) is a common recombinant protein often expressed in inclusion bodies, requiring refolding.
  • Screening refolding conditions is typically time-consuming and labor-intensive.

Purpose of the Study:

  • To develop and validate a Surface Plasmon Resonance (SPR) based method for screening protein refolding conditions.
  • To identify optimal physicochemical environments for refolding denatured glutathione-S-transferase (GST).
  • To assess the suitability of SPR for high-throughput screening of protein refolding.

Main Methods:

  • Utilized Surface Plasmon Resonance (SPR) on carboxymethylcellulose coated chips.

Related Experiment Videos

  • Employed a dual-derivatized chip with immobilized glutathione and anti-GST antibody to detect GST presence and activity.
  • Developed a two-step chip regeneration procedure for repeated analysis of refolding conditions.

    • Main Results:

    • SPR successfully screened various refolding conditions for denatured GST.
    • The dual-derivatized chip allowed simultaneous assessment of GST binding and enzyme activity.
    • Demonstrated high sensitivity, chip regenerability, and suitability for control incorporation in experimental design.

    Conclusions:

    • SPR is a sensitive and efficient technique for screening protein refolding conditions.
    • The dual-derivatized chip approach provides a comprehensive measure of refolding success.
    • Automated SPR systems offer a valuable high-throughput approach for optimizing protein refolding, particularly for proteins expressed in bacterial hosts.