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

Cooperativity in two-state protein folding kinetics.

Thomas R Weikl1, Matteo Palassini, Ken A Dill

  • 1Department of Pharmaceutical Chemistry, University of California, San Francisco, 94143, USA. Thomas. Weikl@mpikg-golm.mpg.de

Protein Science : a Publication of the Protein Society
|February 24, 2004
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

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
Same journal

Macromolecular crowding inhibits degradation of alpha-synuclein amyloid fibrils induced by cathepsins and MMP9.

Protein science : a publication of the Protein Society·2026
Same journal

Sequence-encoded differences in the conformational ensembles of CITED transcriptional activation domains impact coactivator binding.

Protein science : a publication of the Protein Society·2026
Same journal

The phospholipid biosynthesis enzyme PlsB contains three distinct domains for membrane association, lysophosphatidic acid synthesis, and dimerization.

Protein science : a publication of the Protein Society·2026
Same journal

Structural basis of ligand selectivity in FAD/NAD(P)H-dependent dehydrogenases: insights from trypanothione reductase and type II NADH dehydrogenase.

Protein science : a publication of the Protein Society·2026
Same journal

Achieving protease substrate-specific inhibition by mAb dual functional selections.

Protein science : a publication of the Protein Society·2026
Same journal

How important are quantum mechanical effects in controlling biological functions: Enzymes, electron transfer and bird navigation.

Protein science : a publication of the Protein Society·2026
See all related articles

We developed a new model to predict protein folding kinetics using native structures. This approach identifies local structures as key to the folding process, improving our understanding of protein dynamics.

Area of Science:

  • Biophysics
  • Computational Biology
  • Structural Biology

Background:

  • Protein folding is crucial for biological function.
  • Predicting folding kinetics from structure remains a challenge.
  • Two-state protein folding is a fundamental process.

Purpose of the Study:

  • To present a solvable model for predicting protein folding kinetics.
  • To infer folding pathways from native protein structures.
  • To validate the model against known protein folding data.

Main Methods:

  • The model utilizes conditional chain entropies.
  • It assumes folding is driven by small-loop closure events.
  • Inferences are drawn directly from native protein structures.

Related Experiment Videos

Main Results:

  • The model successfully reproduces two-state folding kinetics for CI2, src SH3 domain, TNfn3, and protein L.
  • It accurately predicts average Phi-values for secondary structures.
  • Identified local structure formation (helices, hairpins) as a folding barrier.

Conclusions:

  • The developed model offers a predictive framework for protein folding kinetics.
  • Native structures contain sufficient information to infer folding pathways.
  • Understanding local structure formation is key to overcoming folding barriers.