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

Amyloid Fibrils03:03

Amyloid Fibrils

9.6K
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,...
9.6K
Protein Complex Assembly02:41

Protein Complex Assembly

10.6K
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...
10.6K
Protein Folding01:22

Protein Folding

118.2K
Overview
118.2K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

20.0K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
20.0K
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.1K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.1K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.5K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.5K

You might also read

Related Articles

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

Sort by
Same author

The morphogenetic activity of dAnk genes in the diatom Thalassiosira pseudonana is sensitive to Si availability.

Communications biology·2026
Same author

The stage-wise macromolecular assembly and structure evolution of silk along the silk gland.

Nature communications·2026
Same author

Templateless crystallization of holococcolith crystals visualized by intracellular site-specific three-dimensional microscopy.

PNAS nexus·2026
Same author

Spatial Relations between Coccoliths and Their Confining Membrane During Crystal Morphogenesis.

Journal of the American Chemical Society·2026
Same author

3D cryoimaging of cell-mediated cholesterol crystal clearance in human atherosclerotic lesions.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

pH variations enable guanine crystal formation within iridosomes.

Nature chemical biology·2025
Same journal

A Droplet-Microarray Platform for Multiplex Profiling of Breast Cancer Exosome Subtypes in Patients' Blood Plasma Samples.

Small (Weinheim an der Bergstrasse, Germany)·2026
Same journal

Material-Dependent Functionalization of CVD-Grown TMDC Monolayers Probed by Vibrational Nanospectroscopy.

Small (Weinheim an der Bergstrasse, Germany)·2026
Same journal

BandGap Modulated Charge Gating of Semiconductor Coatings Stabilizes Zinc Metal Anodes.

Small (Weinheim an der Bergstrasse, Germany)·2026
Same journal

For High Capacity: Upcycling of Spent Graphite Catalytic via Precisely Tailoring Water-Gas Reaction.

Small (Weinheim an der Bergstrasse, Germany)·2026
Same journal

Electronic Engineering of Donor-Acceptor Covalent Organic Frameworks via Fluorine Substitution for Efficient Solar Hydrogen Production.

Small (Weinheim an der Bergstrasse, Germany)·2026
Same journal

Correction to: "A Gold Nanocage/Cluster Hybrid Structure for Whole-Body Multispectral Optoacoustic Tomography Imaging, EGFR Inhibitor Delivery, and Photothermal Therapy".

Small (Weinheim an der Bergstrasse, Germany)·2026
See all related articles

Related Experiment Video

Updated: Jul 7, 2025

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

11.0K

Protein Compartments Modulate Fibrillar Self-Assembly.

Shay Karger1, Marco E Miali1, Aleksei Solomonov1

  • 1Department of Molecular Chemistry and Materials Science, Weizmann Institute of Science, Rehovot, 7610001, Israel.

Small (Weinheim an Der Bergstrasse, Germany)
|December 26, 2023
PubMed
Summary
This summary is machine-generated.

Biomolecular condensates, formed by liquid-liquid phase separation, influence protein aggregation kinetics. Controlling compartment volume can accelerate or decelerate fibrillar protein self-assembly, impacting neurodegenerative disease research.

Keywords:
amyloid fibrillationliquid‐liquid phase separationlysozyme proteinmicrofluidicsself‐assembly

More Related Videos

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

9.8K
4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

17.4K

Related Experiment Videos

Last Updated: Jul 7, 2025

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

11.0K
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

9.8K
4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

17.4K

Area of Science:

  • Cellular Biology
  • Biophysics
  • Biochemistry

Background:

  • Complex cellular environments feature protein-rich compartments formed via liquid-liquid phase separation.
  • These biomolecular condensates can promote or inhibit fibrillar protein self-assembly, a process implicated in neurodegenerative diseases like Alzheimer's and Parkinson's.
  • The precise regulatory role of these condensates in protein aggregation remains unclear.

Purpose of the Study:

  • To investigate the role of protein-rich compartments in regulating fibrillar protein self-assembly.
  • To characterize the self-assembly behavior of lysozyme within artificial protein compartments.
  • To determine how volumetric parameters of these compartments affect protein aggregation kinetics.

Main Methods:

  • Utilized microfluidics to construct artificial protein compartments.
  • Characterized the self-assembly of the fibrillar protein lysozyme within these compartments.
  • Analyzed the impact of compartment volumetric parameters on fibrillation kinetics, nucleation, growth, and phase crosstalk.

Main Results:

  • Observed that volumetric parameters of protein-rich compartments significantly alter protein self-assembly kinetics.
  • Demonstrated that changes in compartment parameters can either accelerate or decelerate lysozyme fibrillation.
  • Confirmed that volumetric parameters influence nucleation, growth, and phase crosstalk, with nearby phase-separated compartments accelerating aggregation.

Conclusions:

  • Protein-rich phases exhibit complex behaviors and functions within cellular environments.
  • Volumetric parameters of biomolecular condensates are critical regulators of protein aggregation.
  • Understanding these interactions provides insights into the mechanisms underlying protein-misfolding diseases.