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

Caspases01:24

Caspases

12.7K
Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...
12.7K
Protein Folding01:25

Protein Folding

8.8K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.8K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.5K
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...
18.5K
The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

6.9K
Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
6.9K
Conserved Binding Sites01:49

Conserved Binding Sites

4.4K
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...
4.4K
Evolutionary Relationships through Genome Comparisons02:54

Evolutionary Relationships through Genome Comparisons

6.2K
Genome comparison is one of the excellent ways to interpret the evolutionary relationships between organisms. The basic principle of genome comparison is that if two species share a common feature, it is likely encoded by the DNA sequence conserved between both species. The advent of genome sequencing technologies in the late 20th century enabled scientists to understand the concept of conservation of domains between species and helped them to deduce evolutionary relationships across diverse...
6.2K

You might also read

Related Articles

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

Sort by
Same author

Structure of the human HIRA histone chaperone with a nucleosome suggests a stepwise nucleosome assembly mechanism.

bioRxiv : the preprint server for biology·2026
Same author

RNA-induced PRC2 inhibition depends on the sequence of bound RNA.

Nature communications·2026
Same author

RNA-induced PRC2 inhibition depends on the sequence of bound RNA.

Research square·2025
Same author

Evolution of the conformational ensemble and allosteric networks of apoptotic caspases in chordates.

The Biochemical journal·2025
Same author

Structure-guided design and development of cyclic peptide allosteric activators of Polycomb Repressive Complex 2.

bioRxiv : the preprint server for biology·2025
Same author

RNA-induced PRC2 inhibition depends on the sequence of bound RNA.

bioRxiv : the preprint server for biology·2024

Related Experiment Video

Updated: Sep 20, 2025

Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry
05:29

Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry

Published on: March 24, 2023

4.7K

Comparing the folding landscapes of evolutionarily divergent procaspase-3.

Liqi Yao1, A Clay Clark1

  • 1Department of Biology, University of Texas at Arlington, Arlington, Texas 76019, U.S.A.

Bioscience Reports
|June 7, 2022
PubMed
Summary

The folding landscape of apoptotic caspases is conserved across species, though differences exist in folding intermediates. This conservation suggests a common evolutionary path for caspase function.

Keywords:
apoptosiscaspasedimerizationfluorescence spectroscopyprotein foldingzebrafish

More Related Videos

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
05:56

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches

Published on: October 13, 2022

1.4K
Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation
08:47

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation

Published on: March 5, 2018

9.2K

Related Experiment Videos

Last Updated: Sep 20, 2025

Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry
05:29

Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry

Published on: March 24, 2023

4.7K
Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
05:56

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches

Published on: October 13, 2022

1.4K
Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation
08:47

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation

Published on: March 5, 2018

9.2K

Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Molecular Biology

Background:

  • Caspases, crucial for apoptosis and inflammation, evolved from a common ancestor.
  • The caspase-hemoglobinase fold is conserved in both monomeric (initiator) and dimeric (effector) apoptotic caspases.

Purpose of the Study:

  • To investigate the evolutionary conservation of the folding landscape in effector caspases.
  • To compare the folding and assembly of zebrafish procaspase-3b with human effector procaspases.

Main Methods:

  • Urea-induced equilibrium folding/unfolding experiments were performed on zebrafish procaspase-3b.
  • Comparative analysis of effector caspases across different species was conducted.

Main Results:

  • Zebrafish procaspase-3b exhibits a three-state folding pathway, differing from human procaspase-3 by the underpopulation of a monomeric intermediate.
  • Effector procaspase dimers undergo a conserved pH-dependent conformational change, impacting their stability and activity.

Conclusions:

  • The caspase-hemoglobinase fold landscape is conserved, allowing for species-specific adaptations in stability.
  • A pH-dependent conformational change offers a reversible mechanism for regulating caspase activity.