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...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

You might also read

Related Articles

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

Sort by
Same author

Contrasting Effects of Tagging Turnip Mosaic Virus Proteins.

Pathogens (Basel, Switzerland)·2026
Same author

Alanine Rewires the Communication Pathways Established During the Allosteric Activation of Liver Pyruvate Kinase by Fructose Bisphosphate.

Journal of chemical information and modeling·2026
Same author

Subsets of adjacent nodes (SOAN): A fast method for computing suboptimal paths in protein dynamic networks.

Molecular physics·2026
Same author

Effect of phosphorylation barcodes on arrestin binding to a chemokine receptor.

Nature·2025
Same author

Uncovering the Role of Distal Regions in PDK1 Allosteric Activation.

ACS bio & med chem Au·2025
Same author

Dissecting the Allosteric Fine-Tuning of Enzyme Catalysis.

JACS Au·2024

Related Experiment Video

Updated: Jul 4, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

Key residue-dominated protein folding dynamics.

Xin-Qiu Yao1, Zhen-Su She

  • 1State Key Laboratory for Turbulence and Complex Systems and Department of Biomedical Engineering, College of Engineering, Peking University, No. 5 Yihe Yuan Street, Haidan, Beijing 100871, China.

Biochemical and Biophysical Research Communications
|June 14, 2008
PubMed
Summary

A key-residue hypothesis suggests a few protein residues control overall dynamics. Molecular dynamics revealed key residues in Trp-cage folding, with Trp6 showing a faster reconfiguration process vital for folding dynamics.

More Related Videos

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Related Experiment Videos

Last Updated: Jul 4, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Area of Science:

  • Protein dynamics
  • Computational biophysics

Background:

  • Understanding protein folding dynamics is crucial for molecular biology.
  • The "key-residue" hypothesis proposes limited residues dictate protein behavior.

Purpose of the Study:

  • To investigate the "key-residue" hypothesis in protein side-chain relaxation.
  • To identify key residues and their role in Trp-cage folding dynamics.

Main Methods:

  • Utilized molecular dynamics simulations for protein folding.
  • Analyzed side-chain relaxation and geometrical properties of residues.
  • Characterized residue dynamics using order parameters and phase planes.

Main Results:

  • Identified four key residues highly sensitive to protein state changes.
  • Demonstrated key residue order parameters can distinguish reaction pathways.
  • Observed Trp6 exhibiting two distinct reconfiguration processes, one significantly faster than predicted by existing models.

Conclusions:

  • The "key-residue" hypothesis is supported by simulation data.
  • Key residues, particularly Trp6, play a critical role in protein folding dynamics.
  • A faster reconfiguration mechanism involving Trp6 torsion may be a significant folding pathway.