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

Phi values in protein-folding kinetics have energetic and structural components.

Claudia Merlo1, Ken A Dill, Thomas R Weikl

  • 1Max Planck Institute of Colloids and Interfaces, Theory Division, 14424 Potsdam, Germany.

Proceedings of the National Academy of Sciences of the United States of America
|July 13, 2005
PubMed
Summary

This study introduces a new model for understanding protein folding kinetics. The model explains experimental Phi values, including unusual ones, by considering both structural and energetic factors in protein substructure formation.

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

Membrane tubulation by spherical nanoparticles: effect of lateral tension.

Soft matter·2026
Same author

Dissecting mechanisms of ligand binding and conformational changes in the glutamine-binding protein.

eLife·2026
Same author

Nonequilibrium Theory for Molecular Machine Design.

ArXiv·2026
Same author

Conformational Dynamics of Plasmepsin X during Inhibitor Binding.

The journal of physical chemistry. B·2026
Same author

Seeking Biology's Physics Stories: Simplify, Simplify.

Annual review of biophysics·2026
Same author

A principled basis for nonequilibrium network flows.

Nature communications·2026

Area of Science:

  • Biochemistry
  • Protein Dynamics
  • Computational Biology

Background:

  • Phi values are experimental measures of mutation effects on protein folding kinetics.
  • Interpreting Phi values often relies on transition-state ensemble structures.
  • Nonclassical Phi values (<0 or >1) present interpretation challenges.

Purpose of the Study:

  • To develop a simple analytical model for protein folding kinetics.
  • To elucidate the structural and energetic components of Phi values.
  • To provide a general interpretation for nonclassical Phi values.

Main Methods:

  • Developed a simple analytical model based on protein substructure formation.
  • Applied the model to analyze folding kinetics and Phi values.

Related Experiment Videos

  • Compared model predictions with experimental data for single-residue mutations.

    • Main Results:

    • The model demonstrates that Phi values possess both structural and energetic contributions.
    • A natural interpretation for nonclassical Phi values is provided.
    • The model accurately reproduces experimental Phi values for 20 mutations in CI2 protein's alpha-helix.

    Conclusions:

    • The proposed analytical model offers a unified framework for understanding Phi values.
    • It successfully explains both classical and nonclassical Phi values in protein folding.
    • The findings enhance the interpretation of mutation effects on protein folding pathways.