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

Proline inhibits aggregation during protein refolding.

D Samuel1, T K Kumar, G Ganesh

  • 1Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan.

Protein Science : a Publication of the Protein Society
|March 15, 2000
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

The effect of donepezil treatment on cardiovascular mortality.

Clinical pharmacology and therapeutics·2010
Same author

Targeting pancreatic and ovarian carcinomas using the auristatin-based anti-CD70 antibody-drug conjugate SGN-75.

British journal of cancer·2010
Same author

Establishment and characterization of immortalized porcine hepatocytes for the study of hepatocyte xenotransplantation.

Transplantation proceedings·2010
Same author

Association of angiotensin-converting enzyme inhibitor-associated angioedema with transplant and immunosuppressant use.

Allergy·2010
Same author

Constructing defined chromosome segmental duplications in maize.

Cytogenetic and genome research·2010
Same author

Predicting the radiation exposure of terrestrial wildlife in the Chernobyl exclusion zone: an international comparison of approaches.

Journal of radiological protection : official journal of the Society for Radiological Protection·2010

Proline prevents aggregation during hen egg-white lysozyme refolding by stabilizing intermediates. This amino acid may act as a protein folding chaperone, aiding in osmoregulation and preventing aggregation.

Area of Science:

  • Biochemistry
  • Protein Folding
  • Molecular Biology

Background:

  • Protein misfolding and aggregation are critical issues in biological systems.
  • Osmolytes are known to play roles in protein stability and cellular protection.
  • Understanding protein refolding mechanisms is essential for protein engineering and therapeutics.

Purpose of the Study:

  • To investigate the effect of osmolytes on in vitro refolding of hen egg-white lysozyme.
  • To elucidate the mechanism by which proline prevents protein aggregation during refolding.
  • To explore the potential role of proline as a protein folding chaperone.

Main Methods:

  • In vitro refolding experiments using hen egg-white lysozyme.
  • Analysis of protein aggregation in the presence of various osmolytes, including proline.

Related Experiment Videos

  • Characterization of proline's interaction with folding intermediates.
  • Assessment of bacteriolytic activity recovery after proline removal.

    • Main Results:

    • Proline effectively prevented aggregation of lysozyme during in vitro refolding, unlike other tested osmolytes.
    • Proline appears to inhibit aggregation by binding to folding intermediates, rendering them aggregation-insensitive.
    • Removal of proline restored significant bacteriolytic activity, indicating reversible inhibition.
    • At high concentrations, proline forms higher-order, amphipathic molecular aggregates.

    Conclusions:

    • Proline acts as a potent inhibitor of protein aggregation during refolding.
    • Proline's mechanism involves stabilizing folding intermediates into an aggregation-insensitive state.
    • The formation of proline aggregates is crucial for its function as a folding aid.
    • Proline exhibits properties consistent with a protein folding chaperone, beyond its known osmoregulatory role.