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...
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

You might also read

Related Articles

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

Sort by
Same author

A two-pronged strategy eliminates dissociation artifacts for high-fidelity neuroimmune single-cell transcriptomics.

Communications biology·2026
Same author

Differential effects of antibiotic exposure on gut microbiota homeostasis and functional dynamics in a stable real-time simulated intestinal system.

Journal of hazardous materials·2026
Same author

Rapid Far-Infrared Radiation and Physiotherapeutic Effects of Carbon Nanotube Flexible Thin-Film Heaters.

Nanomaterials (Basel, Switzerland)·2026
Same author

Kiwifruit genomics and applications: recent advances, current challenges, and future prospects.

Horticulture research·2026
Same author

DDA-BERT: end-to-end training for data-dependent acquisition mass spectrometry-based proteomics.

Nature communications·2026
Same author

A novel TaqMan probe-based qPCR method for rapid detection of the bacteria-associated amoeba <i>Heterostelium pallidum</i>.

Microbiology spectrum·2026

Related Experiment Video

Updated: Jul 14, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Nanoscale dewetting transition in protein complex folding.

Lan Hua1, Xuhui Huang, Pu Liu

  • 1Department of Chemistry, Columbia University, New York, New York 10027, USA.

The Journal of Physical Chemistry. B
|July 5, 2007
PubMed
Summary

Researchers discovered that protein complexes, like tetramers and dimers, can undergo a nanoscale dewetting transition during protein folding. This finding expands on previous observations in melittin tetramers, identifying new candidates for studying this phenomenon.

More Related Videos

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 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

Related Experiment Videos

Last Updated: Jul 14, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 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

Area of Science:

  • Biophysics
  • Computational Biology
  • Protein Science

Background:

  • A previous study observed a nanoscale drying transition within the melittin protein tetramer.
  • This phenomenon, known as dewetting, occurs during the final stages of protein folding.

Purpose of the Study:

  • To identify other protein complexes exhibiting dewetting transitions during folding.
  • To investigate the structural features that promote dewetting in protein complexes.

Main Methods:

  • Searched the Protein Data Bank (PDB) for potential protein candidates (tetramers, dimers, two-domain proteins).
  • Utilized molecular dynamics (MD) simulations on candidates identified by a hydrophobic scoring function.
  • Evaluated the robustness of dewetting with different water models and electrostatic interaction treatments.

Main Results:

  • Identified several new protein complexes, including three tetramers, six dimers, and two two-domain proteins, that display nanoscale dewetting.
  • Found that large, aligned, and connected hydrophobic surface areas are crucial for dewetting.
  • Confirmed that the dewetting phenomenon is robust across different simulation conditions.

Conclusions:

  • Dewetting is not unique to melittin tetramers and occurs in various protein complex types.
  • The identified structural features provide insights for predicting and studying protein dewetting.
  • These findings offer new protein candidates for experimental validation of dewetting's role in protein folding.