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

Molecular chaperones in cellular protein folding

F U Hartl1, J Martin

  • 1Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.

Current Opinion in Structural Biology
|February 1, 1995
PubMed
Summary

Molecular chaperones, including hsp70 and hsp60 proteins, are essential for protein folding within cells. These proteins prevent polypeptide aggregation and facilitate proper folding through ATP-dependent mechanisms, with recent studies clarifying their action and structures.

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 nucleolus functions as a phase-separated protein quality control compartment.

Science (New York, N.Y.)·2019
Same author

Rubisco condensate formation by CcmM in β-carboxysome biogenesis.

Nature·2019
Same author

Plant RuBisCo assembly in <i>E. coli</i> with five chloroplast chaperones including BSD2.

Science (New York, N.Y.)·2017
Same author

The formation, function and regulation of amyloids: insights from structural biology.

Journal of internal medicine·2016
Same author

Chaperonin-mediated de novo generation of prion protein aggregates.

Journal of molecular biology·2001
Same author

Dual function of protein confinement in chaperonin-assisted protein folding.

Cell·2001

Area of Science:

  • Molecular biology
  • Biochemistry
  • Cell biology

Background:

  • Protein folding is a critical cellular process.
  • Misfolded proteins can lead to aggregation and cellular dysfunction.
  • Molecular chaperones assist in proper protein folding.

Purpose of the Study:

  • To elucidate the mechanistic principles of hsp70 and hsp60 action.
  • To understand the structural basis of chaperonin function.
  • To define pathways of chaperone-mediated protein folding.

Main Methods:

  • Structural biology techniques (e.g., X-ray crystallography).
  • Biochemical assays to study ATP-dependent reactions.
  • Analysis of protein folding pathways.

Related Experiment Videos

Main Results:

  • Detailed understanding of hsp70 and hsp60 mechanistic principles.
  • Crystal structure of the chaperonin GroEL solved.
  • Identification of pathways for chaperone-mediated protein folding.

Conclusions:

  • Hsp70 and hsp60 chaperones are vital for preventing protein aggregation.
  • ATP-dependent reactions are central to chaperone-mediated folding.
  • Advances in structural and mechanistic studies enhance our understanding of protein homeostasis.