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

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

13.2K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
13.2K
Conservation of Protein Domains02:26

Conservation of Protein Domains

3.3K
3.3K
Conserved Binding Sites01:49

Conserved Binding Sites

4.7K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.7K
Membrane Domains01:18

Membrane Domains

6.2K
The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the...
6.2K
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

3.4K
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
3.4K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.6K
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...
2.6K

You might also read

Related Articles

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

Sort by
Same author

Association between congenital uterine anomalies and placenta accreta spectrum: an exploratory retrospective observational study.

The journal of maternal-fetal & neonatal medicine : the official journal of the European Association of Perinatal Medicine, the Federation of Asia and Oceania Perinatal Societies, the International Society of Perinatal Obstetricians·2026
Same author

Aging of Phosphorylated Cellulose Nanofibers under Moist-Heat Conditions.

Biomacromolecules·2025
Same author

The Enigma of Protein Domains of Low-Sequence Complexity: 2025 Albert Lasker Basic Medical Research Award.

JAMA·2025
Same author

A novel dose-based intra-preplan method for high-dose-rate brachytherapy in cervical cancer using modeling and optimization algorithms.

Brachytherapy·2025
Same author

A simple method for mapping the location of cross-β-forming regions within protein domains of low sequence complexity.

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

Optically Pumped and Electrically Switchable Microlaser Array Based on Elliptic Deformation and Q-Attenuation of Organic Droplet Oscillators.

Advanced materials (Deerfield Beach, Fla.)·2024

Related Experiment Video

Updated: Oct 16, 2025

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing
12:04

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing

Published on: October 3, 2018

9.1K

How do protein domains of low sequence complexity work?

Masato Kato1,2, Xiaoming Zhou1, Steven L McKnight1

  • 1Department of Biochemistry, UT Southwestern Medical Center, Dallas, Texas 75390, USA.

RNA (New York, N.Y.)
|October 21, 2021
PubMed
Summary

Low complexity (LC) domains drive phase separation, a key mechanism for cellular organization. This review explores their function in cells, offering insights into protein behavior and early evolution.

Keywords:
cross-β polymershydrogellow-complexity sequencesneurodegenerative diseasesphase separation

More Related Videos

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.1K
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.4K

Related Experiment Videos

Last Updated: Oct 16, 2025

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing
12:04

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing

Published on: October 3, 2018

9.1K
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.1K
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.4K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Cells utilize material condensates for compartmentalization.
  • Macromolecular condensation mechanisms are well-studied.
  • The function of intrinsically disordered proteins, particularly low complexity (LC) domains, remains poorly understood.

Purpose of the Study:

  • To review research on LC domain self-association and phase separation.
  • To examine phase separation as a biochemical assay for LC domain function.
  • To elucidate the role of LC domains in cellular organization and dynamics.

Main Methods:

  • Review of decade-long research findings on LC domains.
  • Analysis of phase separation phenomena in biological systems.
  • Biochemical and structural biology approaches to study protein self-association.

Main Results:

  • LC domains exhibit self-association leading to phase separation from aqueous solutions.
  • Phase separation serves as a valuable assay for studying LC domain function in vitro.
  • LC domains contribute to cellular organization by dynamically switching between ordered and disordered states.

Conclusions:

  • LC domains are crucial for providing both specificity and flexibility to cellular organization.
  • Understanding LC domains sheds light on the function of a significant portion of the proteome.
  • Ancient proteins with LC sequences may have played a role in early RNA organization.