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

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

18.1K
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...
18.1K
Protein Folding01:25

Protein Folding

8.4K
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...
8.4K
Protein Organization01:13

Protein Organization

141.0K
Overview
141.0K
Step-Growth Polymerization: Overview01:03

Step-Growth Polymerization: Overview

3.6K
Step-growth or condensation polymerization is a stepwise reaction of bi or multifunctional monomers to form long-chain polymers. As all the monomers are reactive, most of the monomers are consumed at the early stages of the reaction to form small chains of reactive oligomers, which then combine to form long polymer chains in the late stages. Hence, the reaction has to proceed for a long time to achieve high molecular weight polymers.
Many natural and synthetic polymers are produced by...
3.6K
Condensins02:15

Condensins

3.6K
Condensins are large protein complexes that use ATP to fuel the assembly of chromosomes during mitosis. They transform the tangled, shapeless mass of post-interphase DNA into individualized chromosomes by compacting, organizing, and segregating chromosomal DNA.
The plant and animal cells contain two types of condensin complexes—condensin I and condensin II. Both complexes have five subunits: two SMC (Structural Maintenance of Chromosomes) subunits, a kleisin subunit, and two HEAT-repeat...
3.6K
Protein Complex Assembly02:41

Protein Complex Assembly

10.8K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
10.8K

You might also read

Related Articles

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

Sort by
Same author

Imaging Approach to DNA Damage Induction and Quantification.

Methods in molecular biology (Clifton, N.J.)·2026
Same author

Resolving protein condensates and aggregates in vivo by boxcar-enhanced Fluorescence-detected mid-Infrared photothermaL Microscopy (FILM).

Communications chemistry·2026
Same author

Microporous Immune-Isolating Capsule with Improved Diffusion for Restored Dynamic Bidirectional Hormone Signaling in a Murine Model of Premature Ovarian Insufficiency.

bioRxiv : the preprint server for biology·2026
Same author

Recombinant Protein Nanoparticles for Dual-Stage Inhibition of SARS-CoV‑2 Infection.

ACS nanoscience Au·2026
Same author

Predictability of a dental implant prognosis system: A retrospective study.

Journal of periodontology·2026
Same author

Delivery of peptide coacervates to form stable interaction hubs in cells.

Nature communications·2026

Related Experiment Video

Updated: Sep 2, 2025

Chemical Dimerization-Induced Protein Condensates on Telomeres
08:52

Chemical Dimerization-Induced Protein Condensates on Telomeres

Published on: April 12, 2021

3.2K

Protein Condensate Formation via Controlled Multimerization of Intrinsically Disordered Sequences.

Mikael V Garabedian1, Zhihui Su2, Jorge Dabdoub1

  • 1Department of Cell and Developmental Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.

Biochemistry
|August 2, 2022
PubMed
Summary

Researchers developed new noncovalent methods to control the assembly of protein condensates using intrinsically disordered regions (IDRs). These strategies enable tunable regulation of phase separation for synthetic biology applications.

More Related Videos

Author Spotlight: Developing Synthetic Cells from Programmable Amphiphilic DNA Nanostructures
08:02

Author Spotlight: Developing Synthetic Cells from Programmable Amphiphilic DNA Nanostructures

Published on: May 31, 2024

886
Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
06:48

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

4.0K

Related Experiment Videos

Last Updated: Sep 2, 2025

Chemical Dimerization-Induced Protein Condensates on Telomeres
08:52

Chemical Dimerization-Induced Protein Condensates on Telomeres

Published on: April 12, 2021

3.2K
Author Spotlight: Developing Synthetic Cells from Programmable Amphiphilic DNA Nanostructures
08:02

Author Spotlight: Developing Synthetic Cells from Programmable Amphiphilic DNA Nanostructures

Published on: May 31, 2024

886
Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
06:48

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

4.0K

Area of Science:

  • Biochemistry
  • Cell Biology
  • Synthetic Biology

Background:

  • Intrinsically disordered regions (IDRs) drive liquid-liquid phase separation (LLPS) to form functional cellular condensates.
  • Controlling LLPS is crucial for engineering synthetic membraneless organelles.
  • Previous methods focused on enzymatic control of valency.

Purpose of the Study:

  • To develop noncovalent strategies for regulating the phase separation of a specific IDR, the LAF-1 RGG domain.
  • To demonstrate tunable control over condensate formation in vitro and in live cells.
  • To explore modular tools for promoting IDR phase separation.

Main Methods:

  • Modular dimerization of RGG domains using high-affinity coiled-coil pairs.
  • Temporal control of phase separation using FKBP-rapamycin-FRB system.
  • Optically induced condensation using photocaged dimerizers in cell-sized emulsions and live cells.

Main Results:

  • Stable condensates formed via RGG domain dimerization in vitro.
  • Temporal control of phase separation achieved using chemical dimerizers.
  • Optical control of condensation demonstrated in cellular environments.

Conclusions:

  • Noncovalent strategies provide versatile tools for controlling IDR-based condensate assembly.
  • These methods enable tunable and inducible formation of synthetic organelles.
  • The developed tools advance the engineering of biomolecular condensates for cellular regulation.