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

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
The Spindle Assembly Checkpoint02:19

The Spindle Assembly Checkpoint

The spindle assembly checkpoint is a molecular surveillance mechanism ensuring the fidelity of chromosome segregation during anaphase. The checkpoint monitors the completion of all the prerequisite steps before chromosome segregation to determine whether the segregation process should proceed or be delayed.
Many proteins function together to control the spindle assembly checkpoint. Mutations affecting these proteins may allow cells to proceed into anaphase prematurely, resulting in the...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...

You might also read

Related Articles

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

Sort by
Same author

Polyphosphate modulates the stress-responsive formation of functional RNA-protein condensates in bacteria and mammalian cells.

PLoS biology·2026
Same author

Microprotein Regulates G-quadruplex Driven RNA Aggregation.

bioRxiv : the preprint server for biology·2026
Same author

Checking in on proteostasis.

Nature structural & molecular biology·2026
Same author

Visualization of liquid-liquid phase transitions using a tiny G-quadruplex binding protein.

Nature communications·2025
Same author

Identification of host genetic factors modulating β-lactam resistance in <i>Escherichia coli</i> harbouring plasmid-borne β-lactamase through transposon-sequencing.

Emerging microbes & infections·2025
Same author

Polyphosphate: a cellular Swiss army knife.

Current opinion in biotechnology·2025
Same journal

Metabolic control of RNA splicing by polyamines.

Trends in biochemical sciences·2026
Same journal

The role of glycan modifications in health and disease.

Trends in biochemical sciences·2026
Same journal

Strengthening the philosophical basis of graduate science education.

Trends in biochemical sciences·2026
Same journal

CycloPepper learns cyclization sites in therapeutic peptides.

Trends in biochemical sciences·2026
Same journal

Glycosphingolipids in cell identity: Biosynthesis, functions, and emerging tools.

Trends in biochemical sciences·2026
Same journal

Cap in hand: giant viruses, stolen translation, and a road to endosymbiosis?

Trends in biochemical sciences·2026
See all related articles

Related Experiment Video

Updated: May 18, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

Conditional disorder in chaperone action.

James C A Bardwell1, Ursula Jakob

  • 1Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI 48109, USA.

Trends in Biochemical Sciences
|September 29, 2012
PubMed
Summary
This summary is machine-generated.

Protein disorder is a complex concept, but conditionally disordered proteins, like molecular chaperones, are vital for cellular stress response. Their disorder enables crucial interactions for cell protection.

More Related Videos

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
08:32

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Published on: October 23, 2016

Related Experiment Videos

Last Updated: May 18, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
08:32

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Published on: October 23, 2016

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein disorder is an abstract concept, challenging to study and understand its functional significance.
  • Establishing the in vivo importance of protein disorder is difficult.

Purpose of the Study:

  • To investigate the functional role of protein disorder in molecular recognition.
  • To explore conditionally disordered proteins, specifically molecular chaperones, and their role in cellular stress response.

Main Methods:

  • Identification of conditionally disordered proteins, specifically molecular chaperones.
  • Analysis of conformational changes in chaperones under stress conditions.
  • Assessment of the role of disorder in client protein binding and cellular protection.

Main Results:

  • Several molecular chaperones identified as conditionally disordered proteins.
  • These chaperones adopt a partially disordered state under stress, essential for function.
  • Disordered chaperones bind aggregation-sensitive client proteins and protect cells from stressors.

Conclusions:

  • Conditionally disordered chaperones are crucial for cellular defense against stress.
  • Protein disorder plays a vital role in molecular recognition and cellular function.
  • Studying these chaperones offers insights into the functional significance of protein disorder.