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 Networks02:26

Protein Networks

4.0K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.0K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

17.9K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
17.9K
Protein-protein Interfaces02:04

Protein-protein Interfaces

12.5K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K
Energy to Drive Translocation01:37

Energy to Drive Translocation

2.1K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
2.1K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.0K
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...
18.0K
Protein Folding01:22

Protein Folding

118.4K
Overview
118.4K

You might also read

Related Articles

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

Sort by
Same author

Droplet Fusion as a Relaxation Process: Comparison with Shape Recovery of Newtonian and Viscoelastic Droplets.

ArXiv·2026
Same author

Complex Effects of Salt on Small-Angle X-ray Scattering of BSA Originate from the Interplay of Ions and Hydration Water.

The journal of physical chemistry letters·2026
Same author

Counteraction of HMGB1 at ss-dsDNA junctions maintains liquidity of protamine-DNA co-condensates.

bioRxiv : the preprint server for biology·2026
Same author

Complex Effects of Salt on Small-Angle X-ray Scattering of BSA Originate From the Interplay of Ions and Hydration Water.

ArXiv·2026
Same author

A membrane insertion code for intrinsically disordered proteins.

bioRxiv : the preprint server for biology·2026
Same author

Conformations and sequence determinants in the lipid binding of an adhesive peptide derived from Vibrio cholerae biofilms.

PLoS pathogens·2026

Related Experiment Video

Updated: Jul 17, 2025

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

2.1K

ATP Mediates Phase Separation of Disordered Basic Proteins by Bridging Intermolecular Interaction Networks.

Divya Kota1, Ramesh Prasad1, Huan-Xiang Zhou1,2

  • 1Department of Chemistry, University of Illinois Chicago, Chicago IL 60607, USA.

Biorxiv : the Preprint Server for Biology
|August 30, 2023
PubMed
Summary

Adenosine triphosphate (ATP) drives the phase separation of basic intrinsically disordered proteins (bIDPs), forming unique condensates. These ATP-bridged protein networks exhibit rapid fusion and extreme shear thinning.

More Related Videos

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

18.6K
Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.0K

Related Experiment Videos

Last Updated: Jul 17, 2025

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

2.1K
Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

18.6K
Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.0K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Adenosine triphosphate (ATP) is vital for cellular energy and nucleic acid synthesis.
  • Intrinsically disordered proteins (IDPs) play roles in cellular regulation and organization.
  • Phase separation is a key mechanism for cellular compartmentalization.

Approach:

  • Investigated the role of ATP in the phase separation of basic intrinsically disordered proteins (bIDPs).
  • Characterized the biophysical properties of ATP-mediated bIDP condensates, including concentration, interfacial tension, and viscosity.
  • Analyzed the dynamics of condensate fusion and shear-thinning behavior.

Key Points:

  • ATP mediates the phase separation of bIDPs, forming concentrated condensates.
  • ATP acts as a molecular bridge between bIDP chains within these droplets.
  • The condensates display low interfacial tension, high zero-shear viscosity, and rapid fusion.
  • Rapid fusion is linked to extreme shear thinning due to dynamic ATP bridges.
  • High ATP concentrations can lead to aggregation and fibril formation instead of dissolution.

Conclusions:

  • ATP is a critical regulator of bIDP phase separation and condensate properties.
  • ATP-mediated condensates exhibit unique dynamic behaviors, including rapid fusion and shear thinning.
  • Understanding these ATP-driven processes is crucial for comprehending cellular organization and function.