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

18.6K
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...
18.6K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.7K
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...
18.7K
Protein Folding01:22

Protein Folding

123.5K
Overview
123.5K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

8.2K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
8.2K
Amyloid Fibrils03:03

Amyloid Fibrils

10.8K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
10.8K

You might also read

Related Articles

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

Sort by
Same author

Deep learning of functional perturbations from condensate morphology.

Cell·2026
Same author

Ribosome biogenesis bottlenecks reveal vulnerabilities in cancer.

bioRxiv : the preprint server for biology·2026
Same author

Ribosome Molecular Aging Shapes Translation Dynamics.

bioRxiv : the preprint server for biology·2026
Same author

Kinase KEY1 controls pyrenoid condensate size throughout the cell cycle by disrupting phase separation interactions.

Nature cell biology·2026
Same author

Metabolism of Epigenetic Ribonucleosides Leads to Nucleolar Stress and Cytotoxicity.

ACS chemical biology·2026
Same author

Design of de novo nucleolar surface proteins.

Biophysical journal·2025
Same journal

Polaron transformed canonically consistent quantum master equation.

The Journal of chemical physics·2026
Same journal

The x-ray absorption spectrum of the propargyl radical C3H3●.

The Journal of chemical physics·2026
Same journal

Transient hydroperoxyalkyl intermediates (•QOOH) in isopentane oxidation. I. Conformer- and isomer-resolved infrared spectra.

The Journal of chemical physics·2026
Same journal

Transient hydroperoxyalkyl intermediates (•QOOH) in isopentane oxidation. II. Isomer-resolved unimolecular dynamics.

The Journal of chemical physics·2026
Same journal

Quantum state-to-state dynamics studies of the C(3P) + OH(X2Π) → CO(a3Π) + H(2S) reaction based on a new HCO(12A″) potential energy surface.

The Journal of chemical physics·2026
Same journal

Time-resolved ultrabroadband far-to-mid-infrared spectroscopy directly reveals doorway-mediated vibrational energy flow in an energetic crystal (β-HMX).

The Journal of chemical physics·2026
See all related articles

Related Experiment Video

Updated: Oct 18, 2025

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

10.0K

Phase separation vs aggregation behavior for model disordered proteins.

Ushnish Rana1, Clifford P Brangwynne1, Athanassios Z Panagiotopoulos1

  • 1Department of Chemical and Biological Engineering, Princeton University, Princeton, New Jersey 08544, USA.

The Journal of Chemical Physics
|October 2, 2021
PubMed
Summary
This summary is machine-generated.

Sequence properties control protein phase separation. A normalized sequence charge decoration (SCD) parameter predicts whether proteins form large phases or small aggregates, linking sequence to cellular organization.

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

1.9K
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

2.3K

Related Experiment Videos

Last Updated: Oct 18, 2025

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

10.0K
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

1.9K
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

2.3K

Area of Science:

  • Biophysics
  • Computational Biology
  • Cell Biology

Background:

  • Liquid-liquid phase separation (LLPS) is crucial for cellular organization and biochemical regulation.
  • Protein LLPS is sequence-dependent, but sequence features dictating phase transition and morphology remain unclear.

Purpose of the Study:

  • To investigate how sequence distribution, sticker fraction, and chain length influence protein phase separation versus finite aggregation.
  • To identify sequence properties that predict the type of phase transition in disordered proteins.

Main Methods:

  • Employed grand canonical Monte Carlo simulations.
  • Utilized a coarse-grained model for disordered proteins.
  • Systematically varied sequence distribution, sticker fraction, and chain length.

Main Results:

  • Introduced a normalized sequence charge decoration (SCD) parameter as a predictive criterion for macroscopic phase separation versus finite aggregation.
  • Demonstrated a strong correlation between the SCD parameter and the critical density for phase separation.
  • Found that longer chain lengths generally favor macroscopic phase separation for most sequences.

Conclusions:

  • The SCD parameter provides a quantitative link between protein sequence properties and phase behavior.
  • Macroscopic LLPS is likely the dominant phase transition for disordered proteins with dominant short-ranged attractive interactions.
  • Findings offer insights into the widespread observation of LLPS in cellular environments.