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

Competition02:34

Competition

24.6K
When organisms require the same limited resources within an environment, they may have to compete for them. Competition is a net-negative interaction. Even if two competing individuals or populations do not interact directly, the overall fitness of both competitors is lowered as a result of not having full access to the limited resource.
24.6K
Diffusion01:12

Diffusion

217.8K
Diffusion is the passive movement of substances down their concentration gradients—requiring no expenditure of cellular energy. Substances, such as molecules or ions, diffuse from an area of high concentration to an area of low concentration in the cytosol or across membranes. Eventually, the concentration will even out, with the substance moving randomly but causing no net change in concentration. Such a state is called dynamic equilibrium, which is essential for maintaining overall...
217.8K
Diffusion01:21

Diffusion

6.4K
Diffusion is a type of passive transport. In passive transport, a substance tends to move from an area of high concentration to an area of low concentration until the concentration is equal across the space. For example, take the diffusion of substances through the air. When someone opens a perfume bottle in a room filled with people, the perfume is at its highest concentration in the bottle and is at its lowest at the edges of the room. The perfume vapor will diffuse, or spread away, from the...
6.4K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

15.0K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
15.0K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

10.0K
10.0K
Ligand Binding Sites02:40

Ligand Binding Sites

15.0K
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...
15.0K

You might also read

Related Articles

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

Sort by
Same author

Studying exercise-induced affect in older adults: how the circumplex model could enhance theoretical and practical advances in the field.

Frontiers in aging·2026
Same author

Primitive reflexes as candidate quantitative readouts of hierarchical inhibitory control across the lifespan.

Frontiers in human neuroscience·2026
Same author

Cultural and Sex-Related Differences in Free-Word Associations with "Sweets": A Multinational Online Study.

Nutrients·2026
Same author

From social media to body image distress: Problematic internet use, exercise addiction, and enhancement drugs use across countries.

Journal of behavioral addictions·2026
Same author

An AI-Generated Integrated Exercise Addiction Screening Scale (EASS-10): A Methodological Demonstration.

Behavioral sciences (Basel, Switzerland)·2026
Same author

<i>ACTN3</i> rs1815739 and <i>BDNF</i> rs6265 Polymorphisms May Not Be Associated with Handgrip Strength in Elite Wrestlers.

Genes·2026
Same journal

Quantum simulation of alignment dependent differential cross sections in co-propagating molecular beams at cold collision energies.

The Journal of chemical physics·2026
Same journal

Non-additive ion effects on the coil-globule equilibrium of a generic polymer in aqueous salt solutions.

The Journal of chemical physics·2026
Same journal

Insights into the unexpected small reduction of the temperature of maximum density of water by lithium chloride addition.

The Journal of chemical physics·2026
Same journal

Optical frequency comb double-resonance spectroscopy of the 9030-9175 cm-1 states of ethylene.

The Journal of chemical physics·2026
Same journal

Time reversal breaking of colloidal particles in cells.

The Journal of chemical physics·2026
Same journal

Photodynamics of amino acids under UV excitation: Extraterrestrial amino acids.

The Journal of chemical physics·2026
See all related articles

Related Experiment Video

Updated: Jan 28, 2026

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
10:37

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

9.6K

Diffusion-induced competitive two-site binding.

Irina V Gopich1, Attila Szabo1

  • 1Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.

The Journal of Chemical Physics
|March 10, 2019
PubMed
Summary
This summary is machine-generated.

Diffusion significantly impacts ligand binding kinetics in macromolecules with multiple sites. A new reaction channel, influenced by ligand rebinding probability, must be introduced beyond simple rate constant renormalization.

More Related Videos

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions
08:40

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions

Published on: March 14, 2016

20.2K
High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy
06:38

High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy

Published on: February 7, 2019

9.2K

Related Experiment Videos

Last Updated: Jan 28, 2026

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
10:37

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

9.6K
An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions
08:40

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions

Published on: March 14, 2016

20.2K
High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy
06:38

High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy

Published on: February 7, 2019

9.2K

Area of Science:

  • Biophysical Chemistry
  • Chemical Kinetics
  • Macromolecular Science

Background:

  • Ligand binding to macromolecules is fundamental in biological processes.
  • Understanding diffusion's role in binding kinetics is crucial for complex systems.
  • Existing models often simplify multi-site interactions.

Purpose of the Study:

  • To investigate the influence of diffusion on ligand binding kinetics to a two-site macromolecule.
  • To develop a formalism for coupled diffusion-influenced reactions.
  • To analyze the impact of site interactions on binding rates.

Main Methods:

  • Application of a novel formalism for coupled diffusion-influenced reactions.
  • Utilizing the encounter complex model for rederivation.
  • Comparative kinetic calculations for fractional saturation.

Main Results:

  • Diffusion necessitates a new reaction channel connecting singly occupied states, not just renormalized rate constants.
  • The rate constants of this new channel depend on ligand rebinding probability (committor).
  • Site competition slows binding when sites are empty; occupied sites can accelerate binding due to diffusion-induced transitions.

Conclusions:

  • Diffusion introduces complex dynamics in multi-site ligand binding.
  • A new reaction channel is essential for accurately modeling these systems.
  • The interplay between diffusion and binding is context-dependent (initial site occupancy).