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-facilitated RNA folding

K M Weeks1

  • 1Department of Chemistry, University of North Carolina, Chapel Hill 27599-3290, USA. weeks@unc.edu

Current Opinion in Structural Biology
|June 1, 1997
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

Protein-dependent transition states for ribonucleoprotein assembly.

Journal of molecular biology·2001
Same author

Visualizing induced fit in early assembly of the human signal recognition particle.

Nature structural biology·2001
Same author

A collapsed state functions to self-chaperone RNA folding into a native ribonucleoprotein complex.

Nature structural biology·2001
Same author

van't Hoff enthalpies without baselines.

Protein science : a publication of the Protein Society·2000
Same author

Tagging DNA mismatches by selective 2'-amine acylation.

Chemistry & biology·2000
Same author

A collapsed non-native RNA folding state.

Nature structural biology·2000
Same journal

Tomogram exploration through template matching and deep learning.

Current opinion in structural biology·2026
Same journal

A comparative review of cryo-electron ptychography: Biological applications and future perspectives.

Current opinion in structural biology·2026
Same journal

Metabolic disruptions through a three-dimensional genomic lens.

Current opinion in structural biology·2026
Same journal

Collective variable design for biomolecular conformational dynamics.

Current opinion in structural biology·2026
Same journal

Polymer scaling in protein crowding: From dilute coils to semidilute meshes.

Current opinion in structural biology·2026
Same journal

Tuning the physicochemical properties of rationally designed protein-based biomolecular condensates.

Current opinion in structural biology·2026
See all related articles

RNA folding often requires protein assistance to achieve correct structures. Proteins act as chaperones and cofactors, guiding RNA folding through multi-step processes and influencing thermodynamic stability.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • RNA molecules frequently misfold without protein interactions.
  • Chaperone and cofactor proteins are essential for the biological function of many complex RNAs.
  • Understanding RNA-protein interactions is crucial for deciphering cellular processes.

Purpose of the Study:

  • To elucidate the principles governing the formation and stability of RNA-protein complexes.
  • To highlight the role of proteins in facilitating correct RNA folding.
  • To describe the dynamic and thermodynamic aspects of ribonucleoprotein assembly.

Main Methods:

  • Review of recent findings on RNA folding mechanisms.
  • Analysis of induced fit models in RNA-protein complex formation.

Related Experiment Videos

  • Examination of kinetic and thermodynamic factors in ribonucleoprotein assembly.

    • Main Results:

    • RNA folding is often protein-dependent, requiring chaperones and cofactors.
    • The formation of RNA-protein complexes involves induced fit and multiple assembly steps.
    • Large RNA molecules exhibit slow folding kinetics.
    • Protein binding can significantly alter the thermodynamic properties of RNA.

    Conclusions:

    • Protein collaboration is vital for the proper folding and function of biologically relevant RNAs.
    • The assembly of ribonucleoprotein complexes is a complex, multi-step process.
    • Protein binding introduces thermodynamic consequences that influence RNA structure and function.