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

20.7K
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...
20.7K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.4K
15.4K
The Movement of Organelles and Vesicles01:43

The Movement of Organelles and Vesicles

7.0K
In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
7.0K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

18.2K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
18.2K
The Spindle Assembly Checkpoint02:19

The Spindle Assembly Checkpoint

3.9K
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...
3.9K
Microtubule Associated Motor Proteins01:32

Microtubule Associated Motor Proteins

11.4K
Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular...
11.4K

You might also read

Related Articles

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

Sort by
Same author

Single-molecule fluorescence spectroscopy of fast protein dynamics.

Current opinion in structural biology·2026
Same author

Model-free photon analysis of diffusion-based single-molecule FRET experiments.

Nature communications·2025
Same author

Electrostatics and hydrophobicity in the dynamics of intrinsically disordered proteins.

The European physical journal. E, Soft matter·2023
Same author

All over or overall - Do we understand allostery?

Current opinion in structural biology·2023
Same author

Time-resolved burst variance analysis.

Biophysical reports·2023
Same author

Diffusion of a disordered protein on its folded ligand.

Proceedings of the National Academy of Sciences of the United States of America·2021
Same journal

Cephalotaxinone enzymes reveal a whole plant model for homoharringtonine biosynthesis.

Nature chemical biology·2026
Same journal

AI decodes protein-ligand binding.

Nature chemical biology·2026
Same journal

Cryo-EM sheds light on the mechanism of human telomerase inhibition by BIBR1532.

Nature chemical biology·2026
Same journal

Artificial metalloenzymes in complex biological environments.

Nature chemical biology·2026
Same journal

Allosteric disordering of eIF2B regulates the integrated stress response.

Nature chemical biology·2026
Same journal

A tail of two ligases.

Nature chemical biology·2026
See all related articles

Related Experiment Video

Updated: Mar 17, 2026

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

7.5K

Chaperones: Speedy motion for function

Hagen Hofmann1

  • 1Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.

Nature Chemical Biology
|July 20, 2016
PubMed
Summary

No abstract available in PubMed .

More Related Videos

Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells
10:46

Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells

Published on: February 2, 2022

3.0K
Adenofection: A Method for Studying the Role of Molecular Chaperones in Cellular Morphodynamics by Depletion-Rescue Experiments
12:34

Adenofection: A Method for Studying the Role of Molecular Chaperones in Cellular Morphodynamics by Depletion-Rescue Experiments

Published on: September 16, 2016

8.1K

Related Experiment Videos

Last Updated: Mar 17, 2026

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

7.5K
Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells
10:46

Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells

Published on: February 2, 2022

3.0K
Adenofection: A Method for Studying the Role of Molecular Chaperones in Cellular Morphodynamics by Depletion-Rescue Experiments
12:34

Adenofection: A Method for Studying the Role of Molecular Chaperones in Cellular Morphodynamics by Depletion-Rescue Experiments

Published on: September 16, 2016

8.1K