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

The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

12.9K
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:
12.9K
Quantitative Aspects of Drug-Receptor Interaction01:30

Quantitative Aspects of Drug-Receptor Interaction

972
The receptor occupancy theory connects a drug's response to the number of occupied receptors. With higher drug concentrations, more receptors are occupied, leading to increased responses. The formation of drug-receptor complexes involves association and dissociation rates, which reach equilibrium when the forward and backward reactions are equal. The equilibrium association constant (Ka) and its inverse, the equilibrium dissociation constant (Kd), indicate drug affinity. Higher Ka and lower...
972
Physiological Pharmacokinetic Models: Assumption with Protein Binding01:13

Physiological Pharmacokinetic Models: Assumption with Protein Binding

41
Physiological models with protein binding in pharmacokinetics offer a sophisticated approach to understanding drug disposition. These models consider drug-protein interactions, enabling them to effectively predict drug concentrations in different organs and tissues. This precision aids in accurate drug dosing, providing a significant advantage over conventional models. A key process within these models is equilibration, which ensures that drug concentrations achieve a steady state within the...
41
Nonlinear Pharmacokinetics: Bioavailability and Protein-Drug Binding01:22

Nonlinear Pharmacokinetics: Bioavailability and Protein-Drug Binding

156
When a drug follows nonlinear pharmacokinetics, its bioavailability, the amount of the drug that reaches the systemic circulation, can change with different doses. This is due to the presence of a saturable pathway. The pathway becomes saturated as the drug concentration increases, decreasing the absorption rate. Consequently, the drug's bioavailability may be lower than expected at higher doses.
To quantify the extent of bioavailability, pharmacologists often use a parameter called .
156
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

7.9K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
7.9K
Protein-Drug Binding: Mechanism and Kinetics01:16

Protein-Drug Binding: Mechanism and Kinetics

406
Protein-drug binding refers to the interaction between drugs and proteins within the body. This binding process can occur intracellularly, involving drug interactions with enzymes or receptors within cells, or extracellularly, involving plasma proteins in the blood.
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
406

You might also read

Related Articles

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

Sort by
Same author

Switch-like Behavior in the Heme Receptor for Vibrio Vulnificus.

Bulletin of mathematical biology·2025
Same author

DEVELOPMENT OF FIBRIN BRANCH STRUCTURE BEFORE AND AFTER GELATION.

SIAM journal on applied mathematics·2022
Same author

Modeling and Simulation of the Ion-Binding-Mediated Swelling Dynamics of Mucin-like Polyelectrolyte Gels.

Gels (Basel, Switzerland)·2021
Same author

Bifurcation Analysis of a Heat-Sensitive Epigenetic Regulatory Network.

Bulletin of mathematical biology·2021
Same author

Principles of slowed hydrogen diffusion through a mucus layer.

Physical review. E·2021
Same author

Initiation and entrainment of multicellular automaticity via diffusion limited extracellular domains.

Biophysical journal·2021
Same journal

Mathematical Modeling Shows that Overall Infection Burden is Reduced More by Vaccines that Decrease Spread or Accelerate Recovery than those that Lower Severe Infections or Death.

Bulletin of mathematical biology·2026
Same journal

Effects of Seasonal Births and Predation on Disease Spread.

Bulletin of mathematical biology·2026
Same journal

Identifiability, Sensitivity, and Genetic Algorithms in Bacterial Biofilm Selection Models.

Bulletin of mathematical biology·2026
Same journal

Slow Evolution Towards Generalism in a Model of Variable Dietary Range.

Bulletin of mathematical biology·2026
Same journal

CBINN: Cancer Biology-Informed Neural Network for Unknown Parameter Estimation and Missing Physics Identification.

Bulletin of mathematical biology·2026
Same journal

A Cost-Sensitive Behavioral Modeling Analysis of the Early Identification and Control of Infectious Diseases.

Bulletin of mathematical biology·2026
See all related articles

Related Experiment Video

Updated: Jun 23, 2025

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
06:48

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

3.5K

Dimensional Dependence of Binding Kinetics.

Megan G Dixon1, James P Keener2

  • 1Mathematics Department, Brigham Young University, 275 TMCB, Provo, UT, 84602, USA. mdixon@math.byu.edu.

Bulletin of Mathematical Biology
|June 14, 2024
PubMed
Summary
This summary is machine-generated.

Dimensionality impacts protein-protein binding kinetics. This study introduces a stochastic method to calculate binding rates in 1, 2, and 3 dimensions, providing a formula to convert 3D to 2D dissociation constants for membrane interactions.

Keywords:
DimensionsDissociation constantsMembranesProtein binding

More Related Videos

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
13:57

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Published on: February 18, 2014

29.3K
Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface
13:22

Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface

Published on: November 2, 2011

15.0K

Related Experiment Videos

Last Updated: Jun 23, 2025

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
06:48

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

3.5K
Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
13:57

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Published on: February 18, 2014

29.3K
Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface
13:22

Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface

Published on: November 2, 2011

15.0K

Area of Science:

  • Biophysics
  • Biochemistry
  • Computational Biology

Background:

  • Protein-protein interactions are crucial in biological processes.
  • Dissociation constants quantify protein binding affinity, typically in volume concentration (3D).
  • Membrane-bound protein interactions occur in areal concentration (2D), requiring different models.

Purpose of the Study:

  • To investigate the effect of dimensionality on protein-protein binding kinetics.
  • To develop a novel stochastic approach for analyzing binding rates in various dimensions.
  • To provide a method for converting 3D dissociation constants to 2D for membrane-bound interactions.

Main Methods:

  • Stochastic exit time calculations in discrete and continuous spaces.
  • Derivation of general reaction rates for protein-protein binding in 1D, 2D, and 3D.
  • Development of a formula to transform 3D to 2D dissociation constants.

Main Results:

  • Dimensionality significantly influences protein-protein binding kinetics.
  • The study provides a theoretical framework for understanding dimension-dependent binding.
  • A practical formula for converting 3D to 2D dissociation constants is presented.

Conclusions:

  • The dimensionality of the binding environment is a critical factor in protein-protein interactions.
  • The developed stochastic method and conversion formula offer new tools for studying membrane-bound protein binding.
  • This work facilitates more accurate mathematical modeling of biological processes occurring on membrane surfaces.