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-protein Interfaces02:04

Protein-protein Interfaces

14.1K
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...
14.1K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.1K
4.1K
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

5.1K
Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
5.1K
Protein Networks02:26

Protein Networks

4.3K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.3K
Protein Networks02:26

Protein Networks

2.6K
2.6K
Factors Affecting Protein-Drug Binding: Drug Interactions01:23

Factors Affecting Protein-Drug Binding: Drug Interactions

392
Drug interactions are a critical aspect of pharmacology and can occur when two or more drugs compete for the same binding site. This competition can result in one drug displacing another, altering the effect of the displaced drug. Drug interactions are complex processes that rely heavily on how much of the displacer drug is present and how strongly it can bind to the same sites as the displaced drug.
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...
392

You might also read

Related Articles

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

Sort by
Same author

Visualizing and Braking Protein Ring Flips with Difluorotyrosines.

Analytical chemistry·2026
Same author

BSA kinetically traps protein KH1 in unfolded state.

Physical chemistry chemical physics : PCCP·2026
Same author

Engineered OAA lectins as selective and sensitive high mannose glycan targeting tools.

bioRxiv : the preprint server for biology·2026
Same author

Disaccharide-Presenting Iron(II) Complexes as Synthetic Mimics of Natural Glycan Epitopes for Lectin Recognition.

Inorganic chemistry·2026
Same author

Expanding the Molecular Scope of Photo-CIDNP for Nanomolar <sup>19</sup>F NMR Detection of Amines.

Journal of the American Chemical Society·2026
Same author

Phase Model-Driven Deep Learning for Robust Phase Correction in High-Throughput NMR-Based Metabolomics.

The journal of physical chemistry letters·2026

Related Experiment Video

Updated: Nov 9, 2025

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

17.6K

The intracellular environment affects protein-protein interactions.

Shannon L Speer1, Wenwen Zheng2,3, Xin Jiang2,3

  • 1Department of Chemistry, University of North Carolina, Chapel Hill, NC 27599.

Proceedings of the National Academy of Sciences of the United States of America
|April 10, 2021
PubMed
Summary
This summary is machine-generated.

Protein complex stability is higher in cells than in buffer, with greater stability in oocytes than E. coli. Chemical interactions, not just physical crowding, drive protein complex stability in vivo.

Keywords:
macromolecular crowdingproteinprotein–protein interactionsthermodynamics

More Related Videos

Evaluation of Protein&#8211;Protein Interactions using an On-Membrane Digestion Technique
07:07

Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique

Published on: July 19, 2019

6.9K
Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions
06:01

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Published on: January 7, 2019

7.4K

Related Experiment Videos

Last Updated: Nov 9, 2025

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

17.6K
Evaluation of Protein&#8211;Protein Interactions using an On-Membrane Digestion Technique
07:07

Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique

Published on: July 19, 2019

6.9K
Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions
06:01

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Published on: January 7, 2019

7.4K

Area of Science:

  • Biochemistry
  • Cell Biology
  • Biophysics

Background:

  • Protein-protein interactions are vital for cellular functions but challenging to quantify thermodynamically within living cells.
  • In vitro studies indicate that cosolutes modulate protein complex stability through hard-core repulsions and chemical interactions.
  • Understanding in vivo protein complex stability is crucial for comprehending cellular mechanisms and protein evolution.

Purpose of the Study:

  • To thermodynamically quantify the stability of a model protein complex within different cellular environments.
  • To investigate the roles of hard-core repulsions versus chemical interactions in protein complex stability under physiological conditions.
  • To explore how cellular crowding and chemical properties influence protein complex behavior.

Main Methods:

  • Quantification of the stability of the A34F GB1 homodimer model protein complex.
  • Comparative analysis of complex stability in buffer, Escherichia coli cells, and Xenopus laevis oocytes.
  • Assessment of stability variations in modified homodimer variants with altered surface charges.

Main Results:

  • The A34F GB1 homodimer exhibited increased stability in cellular environments compared to buffer.
  • Protein complex stability was higher in Xenopus laevis oocytes than in Escherichia coli cells.
  • Enhancing the negative charge on the homodimer surface correlated with increased stability within cells.

Conclusions:

  • Chemical interactions play a more significant role than hard-core repulsions in protein complex stability under physiological conditions.
  • Cellular environments, particularly the nature of crowding and chemical milieu, profoundly impact protein complex stability.
  • These findings provide insights into the evolution of protein interactions for optimal function in crowded cellular settings.