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

Structural Protein Function01:56

Structural Protein Function

29.8K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
29.8K
Structural Protein Function01:56

Structural Protein Function

3.2K
3.2K
Fruit Development, Structure, and Function01:58

Fruit Development, Structure, and Function

25.0K
Fruits form from a mature flower ovary. As seeds develop from the ovules contained within, the ovary wall undergoes a series of complex changes to form fruit. In some fruits, such as soybeans, the ovary wall dries; in other fruits, such as grapes, it remains fleshy. In some cases, organs other than the ovary contribute to fruit formation; such fruits are called accessory fruits.
25.0K
Structure and Function of Erythrocytes01:29

Structure and Function of Erythrocytes

5.1K
There are between 4.2 and 6 million erythrocytes, also known as red blood cells, in every microliter of blood. These cells are small, flattened biconcave discs with centers that are depressed.
The erythrocyte plasma membrane is associated with proteins such as spectrin, which forms a flexible cytoplasmic meshwork. This meshwork allows erythrocytes to twist, turn, become cup-shaped, and regain their biconcave shape as they pass through narrow capillaries. Additionally, erythrocytes can form...
5.1K
Structure and Function of Platelets01:18

Structure and Function of Platelets

3.0K
The cell fragments known as platelets are disc-shaped, with an average diameter of about 3 μm and a thickness of roughly 1 μm. They play a crucial role in the body's vascular clotting system, which also involves plasma proteins, blood cells, and blood vessel tissues.
Platelets are continually replenished, circulating in the bloodstream for 9-12 days before being removed by phagocytes, primarily in the spleen. A microliter of circulating blood contains between 150,000 and 450,000...
3.0K
Range00:59

Range

13.8K
The range is one of the measures of variation. It can be defined as the difference between a dataset's highest and lowest values. For example, in the study of seven 16-ounce soda cans, the filled volume of soda was measured, thus producing the following amount (in ounces) of soda:
15.9; 16.1; 15.2; 14.8; 15.8; 15.9; 16.0; 15.5
Measurements of the amount of soda in a 16-ounce can vary since different subjects record these measurements or since the exact amount - 16 ounces of liquid, was not...
13.8K

You might also read

Related Articles

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

Sort by
Same author

Enzyme-Free Phosphorylation with Kinetic Gating in a De Novo Coiled-Coil System.

Journal of the American Chemical Society·2026
Same author

Beyond a Passive Tether: Structural Insights into the Disordered Tail of Hsp90.

Journal of the American Chemical Society·2026
Same author

A bridge-like lipid transfer protein is critical for generation of invasive stages in malaria parasites.

Nature communications·2026
Same author

An ancient monoaminergic signaling system coordinates contractility in a nerveless sponge.

bioRxiv : the preprint server for biology·2026
Same author

Evolutionary remodeling of a remnant GET pathway factor into PEX38, an essential peroxin.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Association of high-risk CT coronary artery plaque features with major adverse cardiovascular events: a prespecified secondary analysis of the DISCHARGE trial.

European radiology·2026
Same journal

Demonstration of a quantum C-NOT gate in a time-multiplexed fully reconfigurable photonic processor.

Nature communications·2026
Same journal

Nonlinear quantum light source with van der Waals ferroelectric NbOX<sub>2</sub> (X = Br, I).

Nature communications·2026
Same journal

Antagonistic histone H2A variants and autonomous heterochromatin formation shape epigenomic patterns in Arabidopsis.

Nature communications·2026
Same journal

The long tail of nitrate pollution in groundwater challenges governance of global water quality.

Nature communications·2026
Same journal

Select microbial metabolites promote tau aggregation in a murine tauopathy model.

Nature communications·2026
Same journal

Warming climate has lengthened global intense tropical cyclone seasons.

Nature communications·2026
See all related articles

Related Experiment Video

Updated: Jan 21, 2026

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology
09:39

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Published on: March 31, 2022

3.7K

The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range.

Hannah Girstmair1, Franziska Tippel1, Abraham Lopez1,2

  • 1Center for Integrated Protein Science at the Department of Chemistry, Technische Universität München, 85748, Garching, Germany.

Nature Communications
|August 11, 2019
PubMed
Summary
This summary is machine-generated.

Saccharomyces cerevisiae has two Hsp90 proteins, Hsc82 and Hsp82. Despite high sequence similarity, Hsp82 is more stable and efficient under stress, showcasing isoform-specific adaptations in molecular chaperone function.

More Related Videos

Genome-wide Analysis using ChIP to Identify Isoform-specific Gene Targets
11:19

Genome-wide Analysis using ChIP to Identify Isoform-specific Gene Targets

Published on: July 7, 2010

15.0K
A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

69.7K

Related Experiment Videos

Last Updated: Jan 21, 2026

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology
09:39

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Published on: March 31, 2022

3.7K
Genome-wide Analysis using ChIP to Identify Isoform-specific Gene Targets
11:19

Genome-wide Analysis using ChIP to Identify Isoform-specific Gene Targets

Published on: July 7, 2010

15.0K
A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

69.7K

Area of Science:

  • Molecular Biology
  • Protein Dynamics
  • Cellular Stress Response

Background:

  • The molecular chaperone Hsp90 is crucial for maintaining proteostasis.
  • S. cerevisiae has two Hsp90 isoforms: Hsc82 (constitutive) and Hsp82 (stress-inducible).
  • The functional distinctions between these highly similar isoforms were previously unclear.

Purpose of the Study:

  • To investigate the functional and mechanistic differences between Hsp90 isoforms Hsc82 and Hsp82.
  • To understand how isoform-specific properties contribute to cellular proteostasis under varying conditions.

Main Methods:

  • Comparative analysis of Hsp90 isoform stability and refolding efficiency.
  • Characterization of ATPase activity and conformational cycles.
  • Analysis of client protein interactions under physiological and heat shock conditions.

Main Results:

  • Hsp82 exhibits greater stability and refolding efficiency compared to Hsc82, aligning with its stress-inducible role.
  • Distinct differences in ATPase activity and conformational dynamics were observed, with Hsc82 being more processive.
  • While client interactomes are largely shared, isoform-specific interactors were identified under different conditions.
  • N-terminal domain variations significantly influence Hsp90 isoform dynamics and activity profiles.

Conclusions:

  • Hsp90 isoforms Hsc82 and Hsp82 possess distinct biochemical properties despite high sequence identity.
  • These differences, particularly in the N-domain, confer stress-specific resilience and activity profiles.
  • The fine-tuning of Hsp90 isoforms allows adaptation of the chaperone mechanism to specific cellular needs, optimizing proteostasis.