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

Protein Complex Assembly02:41

Protein Complex Assembly

11.1K
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...
11.1K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.6K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.6K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.0K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.0K
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
Mechanical Protein Functions01:58

Mechanical Protein Functions

5.1K
Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
5.1K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

3.6K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
3.6K

You might also read

Related Articles

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

Sort by
Same author

Assessing probe reliability: Functional group-specific biases revealed by interactome-wide docking of general anesthetics.

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

Terminal-Directed Supramolecular Liquid Crystal Formation by Designed Coiled-Coil Interparticle Stacking.

ACS nano·2026
Same author

Patchy peptide particles for pH-responsive assembly into liquid crystals or lattices.

Science (New York, N.Y.)·2026
Same author

Explicit particle kinetics simulations of reactive diffusion at air-water interfaces.

The Journal of chemical physics·2026
Same author

Cavity acidification limits ferritin iron biomineralization.

Journal of inorganic biochemistry·2026
Same author

Electrostatic Coassembly of Coiled-Coil Peptide Bundlemers with Complementary Charges into Porous 2D Lattices.

Journal of the American Chemical Society·2025

Related Experiment Video

Updated: Sep 18, 2025

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
11:33

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

6.3K

Correction: Charge engineering controls cooperative assembly and loading in protein host-guest complexes.

Zhiheng Wang1, Dai-Bei Yang1, Joshua A Bulos1

  • 1Department of Chemistry, University of Pennsylvania, 231 S. 34th Street, Philadelphia, Pennsylvania 19104-6323, USA. ivandmo@sas.upenn.edu.

Journal of Materials Chemistry. B
|June 23, 2025
PubMed
Summary

This correction clarifies how charge engineering influences the assembly and loading of protein host-guest complexes. It ensures accurate understanding of molecular interactions in supramolecular chemistry.

More Related Videos

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.5K
Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
12:43

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Published on: July 27, 2016

11.8K

Related Experiment Videos

Last Updated: Sep 18, 2025

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
11:33

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

6.3K
Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.5K
Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
12:43

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Published on: July 27, 2016

11.8K

Area of Science:

  • Supramolecular Chemistry
  • Materials Science
  • Biophysical Chemistry

Context:

  • Protein host-guest complexes are crucial for molecular recognition and self-assembly.
  • Understanding the factors governing their formation is essential for designing advanced materials.
  • Previous work explored charge engineering's role, necessitating this correction for accuracy.

Purpose:

  • To correct and clarify the findings presented in the original publication.
  • To provide accurate data and interpretations regarding charge engineering in protein assembly.
  • To ensure the scientific community has precise information on controlling host-guest complex formation.

Summary:

  • This correction addresses specific points within the original study on charge engineering.
  • It refines the understanding of how electrostatic interactions dictate the cooperative assembly and guest loading.
  • Accurate charge distribution is confirmed as a key determinant for complex stability and function.

Impact:

  • Ensures the integrity and reliability of research in supramolecular chemistry.
  • Facilitates more accurate design of protein-based functional materials.
  • Supports advancements in areas like drug delivery and molecular sensing.