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

14.4K
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...
14.4K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.4K
4.4K
Conserved Binding Sites01:49

Conserved Binding Sites

5.0K
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...
5.0K
Protein Folding01:22

Protein Folding

125.7K
Overview
125.7K
Protein Folding01:25

Protein Folding

10.8K
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...
10.8K
Ligand Binding Sites02:40

Ligand Binding Sites

14.8K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
14.8K

You might also read

Related Articles

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

Sort by
Same author

From extracellular entry to intracellular release: A water-assisted transport cycle for creatine in SLC6A8.

Protein science : a publication of the Protein Society·2026
Same author

Functional and Structural Characterization of Pathogenicity of Human Arginine-Histidine Variants.

Journal of computational biophysics and chemistry·2026
Same author

Accurate and Scalable Continuum Electrostatics for Large Biomolecular Systems: The <i>pyDelPhi</i> Poisson-Boltzmann Framework.

Journal of chemical information and modeling·2025
Same author

On generalizing the induced surface charge method to heterogeneous Poisson-Boltzmann models for electrostatic free energy calculation.

Journal of computational physics·2025
Same author

PKAD-R: curated, redesigned and expanded database of experimental pKa values in proteins.

Journal of computational biophysics and chemistry·2025
Same author

Gatifloxacin detection in the nanoscale: a review exploring current biosensing technologies and future opportunities.

RSC advances·2025
Same journal

Mesenchymal stem cells-derived extracellular vesicles as a novel drug delivery carrier: engineering strategies and clinical safety estimation.

Frontiers in molecular biosciences·2026
Same journal

Preparation and analysis of tobacco glycosides, and the relationship between glycoside aglycones and pyrolysis products: a review.

Frontiers in molecular biosciences·2026
Same journal

Peritoneal metastasis in pancreatic cancer: molecular mechanisms, microenvironmental remodeling, and emerging intraperitoneal interventions.

Frontiers in molecular biosciences·2026
Same journal

Insights from LC-MS-based cerebrospinal fluid metabolomics in tuberculous meningitis.

Frontiers in molecular biosciences·2026
Same journal

Emerging roles of Notch signaling in the tumor microenvironment of digestive system cancers.

Frontiers in molecular biosciences·2026
Same journal

Adenosine metabolism as an endogenous protective mechanism in response to upstream ischemic injury.

Frontiers in molecular biosciences·2026
See all related articles

Related Experiment Video

Updated: Jan 5, 2026

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

7.1K

Modeling Electrostatic Force in Protein-Protein Recognition.

H B Mihiri Shashikala1, Arghya Chakravorty1, Emil Alexov1

  • 1Department of Physics, Clemson University, Clemson, SC, United States.

Frontiers in Molecular Biosciences
|October 15, 2019
PubMed
Summary
This summary is machine-generated.

Electrostatic forces guide molecular binding. This study reveals how these forces change with distance, identifying a "soft landing" phenomenon where initial attraction transitions to repulsion, influencing binding dynamics.

Keywords:
bindingelectrostatic forceelectrostaticsmolecular recognitionpolar solvation energy

More Related Videos

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

11.5K
Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy
05:44

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

Published on: March 6, 2017

8.5K

Related Experiment Videos

Last Updated: Jan 5, 2026

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

7.1K
Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

11.5K
Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy
05:44

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

Published on: March 6, 2017

8.5K

Area of Science:

  • Molecular Biology
  • Biophysics
  • Computational Chemistry

Background:

  • Electrostatic interactions are crucial for molecular recognition due to their long-range nature.
  • Understanding these forces is key to predicting how molecules bind correctly.

Purpose of the Study:

  • To investigate the role and behavior of electrostatic forces in protein-protein interactions.
  • To analyze electrostatic force profiles as a function of separation distance in protein complexes.

Main Methods:

  • Calculated electrostatic forces between protein binding partners at various distances using the DelPhiForce tool.
  • Evaluated total electrostatic force via electrostatic association energy.
  • Developed a method to determine force direction and magnitude as separation distance changes.

Main Results:

  • At large distances, electrostatic force is consistent and driven by net charge and interface properties.
  • At short distances, specific interactions and de-solvation penalties dictate the force balance.
  • Four distinct electrostatic force profiles were identified, including the
  • soft landing
  • category.

Conclusions:

  • Electrostatic forces play a dual role in molecular binding, initially attracting and later potentially repelling partners.
  • "Soft landing" describes a scenario where favorable long-range forces become opposing at close range, modulating binding speed.