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 Concept Videos

Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Protein Organization01:13

Protein Organization

Overview

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Complete enzyme clustering enhances coenzyme Q biosynthesis via substrate channeling.

Nature communications·2026
Same author

Biophysical fitness landscape design traps viral evolution.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Chaperonin recognition of protein dynamics drives drug resistance.

bioRxiv : the preprint server for biology·2026
Same author

Co-targeting Metabolic Neighbours Constraints Bacterial Adaptive Evolution.

bioRxiv : the preprint server for biology·2026
Same author

CASPULE: A computational tool to study sticker spacer polymer condensates.

PLoS computational biology·2026
Same author

Evolutionary dynamics under phenotypic uncertainty.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Jul 18, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Understanding ensemble protein folding at atomic detail.

Isaac A Hubner1, Eric J Deeds, Eugene I Shakhnovich

  • 1Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.

Proceedings of the National Academy of Sciences of the United States of America
|November 11, 2006
PubMed
Summary

Researchers developed an all-atom protein folding model using only sequence information. This model simulates thousands of folding events, revealing common pathways and intermediates for detailed analysis.

More Related Videos

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

Related Experiment Videos

Last Updated: Jul 18, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

Area of Science:

  • Computational Biology
  • Biophysics
  • Protein Folding

Background:

  • Protein structure is determined by amino acid sequence.
  • Understanding protein folding pathways from random coil remains challenging.
  • Current models lack a complete ensemble description under physiological conditions.

Purpose of the Study:

  • To develop an all-atom model for ab initio protein folding.
  • To simulate and analyze thousands of complete protein folding events.
  • To elucidate common folding intermediates and pathways at the ensemble level.

Main Methods:

  • Developed a detailed all-atom model with transferable potential.
  • Performed thousands of microsecond-timescale folding simulations.
  • Applied graph-theoretic analysis to simulation data.

Main Results:

  • Successfully simulated ab initio folding of protein domains using sequence information.
  • Observed thousands of independent, complete folding events.
  • Identified common intermediates and pathways crucial for protein folding.

Conclusions:

  • The model provides an atomically detailed, ensemble-level picture of folding pathways.
  • This general approach enables the study of protein folding on extended timescales.
  • The method offers insights into the fundamental principles of protein structure formation.