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

Protein biogenesis: chaperones for nascent polypeptides

J Rassow1, N Pfanner

  • 1Institut für Biochemie und Molekularbiologie, Universität Freiburg, Germany.

Current Biology : CB
|February 1, 1996
PubMed
Summary

Molecular chaperones associate with newly synthesized proteins on ribosomes. This interaction is crucial for proper protein folding and cellular targeting, ensuring protein function.

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

Shaping the mitochondrial inner membrane in health and disease.

Journal of internal medicine·2020
Same author

Advantage and limitations of weighting factors and weighted dose quantities and their units in boron neutron capture therapy.

Medical physics·2004
Same author

Absolute dosimetry in a d(14 MeV) + Be fast neutron beam.

Medical physics·2004
Same author

Validation of a pencil beam model-based treatment planning system for fast neutron therapy.

Medical physics·2003
Same author

Empirical description and Monte Carlo simulation of fast neutron pencil beams as basis of a treatment planning system.

Medical physics·2002
Same author

Hsp70 proteins in protein translocation.

Advances in protein chemistry·2002

Area of Science:

  • Molecular biology
  • Cell biology
  • Biochemistry

Background:

  • Nascent polypeptides emerging from ribosomes require assistance for correct folding.
  • Protein folding and targeting are essential cellular processes.
  • Molecular chaperones are known to aid protein maturation.

Purpose of the Study:

  • To investigate the role of molecular chaperones in ribosome-associated protein folding.
  • To understand how chaperones interact with nascent polypeptides.
  • To elucidate the contribution of chaperones to protein targeting.

Main Methods:

  • Studying the interaction between ribosomes and nascent polypeptide chains.
  • Utilizing biochemical assays to detect chaperone binding.
  • Employing techniques to monitor protein folding in real-time.

Main Results:

  • Multiple molecular chaperones were identified to bind to nascent polypeptides.
  • Evidence suggests chaperones associate with ribosomes during protein synthesis.
  • Chaperone interaction facilitates the folding of newly synthesized proteins.

Conclusions:

  • Ribosome-associated molecular chaperones are key players in cotranslational folding.
  • These chaperones are integral to the protein synthesis machinery.
  • Their involvement ensures the fidelity of protein folding and localization.

Related Experiment Videos