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 Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

2.1K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.1K
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
Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

5.4K
Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
5.4K
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
Protein Folding01:22

Protein Folding

118.3K
Overview
118.3K
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

You might also read

Related Articles

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

Sort by
Same author

Detangling knots: the intricate roles of G-quadruplexes in herpesvirus replication.

Journal of virology·2026
Same author

Intramolecular Interactions between Folded and Disordered Regions Shape Ubiquilin Structure and Function.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

Global emergence and rapid spread of <i>Candidozyma auris</i> (syn. <i>Candida auris</i>): epidemiology, biology, and antifungal resistance.

Clinical microbiology reviews·2026
Same author

Accurate predictions of disordered protein ensembles with STARLING.

Nature·2026
Same author

Sequence and chemical specificity define the functional landscape of intrinsically disordered regions.

Nature cell biology·2026
Same author

STI1 domain engages transient helices to mediate Dsk2 phase separation and proteasome condensation.

The EMBO journal·2026

Related Experiment Video

Updated: Jul 11, 2025

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

3.7K

Sequence-ensemble-function relationships for disordered proteins in live cells.

Ryan J Emenecker1,2, Karina Guadalupe3,4, Nora M Shamoon4,5

  • 1Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO.

Biorxiv : the Preprint Server for Biology
|November 14, 2023
PubMed
Summary
This summary is machine-generated.

Intrinsically disordered protein regions (IDRs) link sequence to cellular function. This study reveals how IDR sequence and structure influence function in live cells, enabling synthetic IDR design.

More Related Videos

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.1K
Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses
05:13

Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses

Published on: January 12, 2024

1.0K

Related Experiment Videos

Last Updated: Jul 11, 2025

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

3.7K
Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.1K
Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses
05:13

Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses

Published on: January 12, 2024

1.0K

Area of Science:

  • Biophysics
  • Molecular Biology
  • Systems Biology

Background:

  • Intrinsically disordered protein regions (IDRs) are crucial for cellular functions and exist as dynamic ensembles.
  • The relationship between an IDR's amino acid sequence, its ensemble structure, and its molecular function in cells remains unclear.

Approach:

  • Developed a novel computational method (GOOSE) for rational design of IDR libraries by varying sequence properties.
  • Utilized ensemble Förster Resonance Energy Transfer (FRET) to measure IDR ensemble dimensions in human cell lines.
  • Investigated how specific sequence variations impact IDR ensemble dimensions in situ.

Key Points:

  • Demonstrated that IDR sequence directly influences ensemble dimensions within living cells.
  • Showed that the interplay between sequence and ensemble can confer a de novo function: sensing cell volume changes.
  • Established biophysical rules governing intracellular sequence-ensemble relationships for IDRs.

Conclusions:

  • The study provides a framework for understanding how IDR sequences dictate function in live cells.
  • Paves the way for designing synthetic IDRs with novel, engineered functions.
  • Highlights the importance of protein dynamics and sequence in cellular processes.