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

Two-state folding over a weak free-energy barrier.

Giorgio Favrin1, Anders Irbäck, Björn Samuelsson

  • 1Complex Systems Division, Department of Theoretical Physics, Lund University, Sölvegatan 14A, SE-223 62 Lund, Sweden.

Biophysical Journal
|August 29, 2003
PubMed
Summary

This Monte Carlo study reveals a 54-amino acid protein model folds directly to its native state. Its folding dynamics exhibit two-state behavior and near-single exponential relaxation, with diffusive motion on longer timescales.

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

Investigating the Function of C‑Terminal Tails of Human Tubulin Isotypes in the Motility Regulation of Cytoplasmic Dynein.

ACS omega·2026
Same author

Folding lattice proteins confined on minimal grids using a quantum-inspired encoding.

Physical review. E·2025
Same author

Impact of N-Terminal Domain Conformation and Domain Interactions on RfaH Fold Switching.

Proteins·2024
Same author

Simulations of a protein fold switch reveal crowding-induced population shifts driven by disordered regions.

Communications chemistry·2023
Same author

Crowding-induced protein destabilization in the absence of soft attractions.

Biophysical journal·2022
Same author

Limitations of field-theory simulation for exploring phase separation: The role of repulsion in a lattice protein model.

The Journal of chemical physics·2022

Area of Science:

  • Computational biophysics
  • Protein folding dynamics
  • Statistical mechanics

Background:

  • Understanding protein folding mechanisms is crucial for molecular biology and disease research.
  • Many proteins fold via complex pathways involving intermediate states.

Purpose of the Study:

  • To investigate the folding pathway of a model protein with 54 amino acids.
  • To characterize the free-energy landscape and relaxation dynamics of the protein.

Main Methods:

  • Monte Carlo simulations were employed to model protein folding.
  • Analysis focused on free-energy barriers, melting curves, and reaction coordinate dynamics.

Main Results:

  • The protein model folds directly to its native three-helix-bundle state without intermediates.

Related Experiment Videos

  • A weak free-energy barrier was observed even at the folding temperature.
  • Melting curves approximated a two-state system with near-single exponential relaxation.
  • Protein motion exhibited diffusive behavior on timescales beyond single helix reconfiguration.

    • Conclusions:

    • The model protein demonstrates a simplified folding mechanism.
    • The observed dynamics can be approximated by simple models, aiding in the understanding of protein folding principles.