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

Cross-reactivity00:42

Cross-reactivity

33.1K
Overview
33.1K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.6K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
9.6K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

2.0K
No description available
2.0K
Protein Complex Assembly02:41

Protein Complex Assembly

16.8K
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...
16.8K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.7K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.7K
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

132.0K
G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
132.0K

You might also read

Related Articles

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

Sort by
Same author

Fluorescent Detection of Aqueous <i>N</i>-Nitrosodimethylamine via Photochemical Transformation and Affinity Capture.

Journal of the American Chemical Society·2026
Same author

Boron-Rich Biologics Enabled by Reactive Organic Carboranes.

JACS Au·2026
Same author

Discovery of ferroptosis-inducing R4VP compounds for targeting aggressive cancers.

Oncogene·2026
Same author

Aplastic anaemia with small paroxysmal nocturnal haemoglobinuria clones developing during osimertinib therapy for non-small cell lung cancer.

Leukemia research reports·2026
Same author

Site-Directed Modification of mRNA with Functionalized Platinum(IV)-Ammines.

JACS Au·2026
Same author

Orthogonal Cleavage of the HMPB Linker from Solid Support Using HFIP.

Organic letters·2025

Related Experiment Video

Updated: Feb 5, 2026

Myocardial Infarction by Percutaneous Embolization Coil Deployment in a Swine Model
05:52

Myocardial Infarction by Percutaneous Embolization Coil Deployment in a Swine Model

Published on: November 4, 2021

3.4K

Equimolar Cross-Coupling Using Reactive Coiled Coils for Covalent Protein Assemblies.

Hironori Takeuchi1,2, Elee Shimshoni1, Satish Gandhesiri1

  • 1Massachusetts Institute of Technology, Department of Chemistry, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States.

Bioconjugate Chemistry
|October 3, 2024
PubMed
Summary

This study introduces a novel peptide platform for precise protein cross-coupling, creating stable covalent fusion proteins. This method enhances biomolecule stability and functionality for diverse applications.

More Related Videos

How to Use the H1 Deep Transcranial Magnetic Stimulation Coil for Conditions Other than Depression
07:00

How to Use the H1 Deep Transcranial Magnetic Stimulation Coil for Conditions Other than Depression

Published on: January 23, 2017

24.9K
Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
11:14

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Published on: January 6, 2017

8.4K

Related Experiment Videos

Last Updated: Feb 5, 2026

Myocardial Infarction by Percutaneous Embolization Coil Deployment in a Swine Model
05:52

Myocardial Infarction by Percutaneous Embolization Coil Deployment in a Swine Model

Published on: November 4, 2021

3.4K
How to Use the H1 Deep Transcranial Magnetic Stimulation Coil for Conditions Other than Depression
07:00

How to Use the H1 Deep Transcranial Magnetic Stimulation Coil for Conditions Other than Depression

Published on: January 23, 2017

24.9K
Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
11:14

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Published on: January 6, 2017

8.4K

Area of Science:

  • Biochemistry
  • Chemical Biology
  • Biotechnology

Background:

  • Biocompatible cross-coupling reactions are crucial for attaching biomolecules.
  • Existing methods may compromise biomolecule integrity.

Purpose of the Study:

  • To develop an affinity-based peptide platform for proximity-driven protein cross-coupling.
  • To create stable covalent fusion proteins using engineered coiled coils.

Main Methods:

  • Utilized coiled coils with reactive side chains (cysteine residues) for controlled cross-linking.
  • Employed the E3/R3 coiled coil pair as a scaffold for designing complementary reactive coils.
  • Used 3,4-dibromomaleimide as the cross-linking agent.

Main Results:

  • Achieved >90% conversion to covalent heterodimeric coupling products.
  • Demonstrated near-quantitative heterodimeric cross-coupling with equimolar protein mixtures.
  • Showcased the ability to create orthogonal assemblies of macromolecules.

Conclusions:

  • The developed platform enables efficient and stable covalent attachment of biomolecules.
  • This versatile method facilitates the creation of diverse fusion protein architectures.
  • The approach has significant potential in chemical biology, biotechnology, and medicine.