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

Affinity and Avidity01:41

Affinity and Avidity

39.0K
Overview
39.0K
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
Electron Affinity03:07

Electron Affinity

43.3K
The electron affinity (EA) is the energy change for adding an electron to a gaseous atom to form an anion (negative ion).
43.3K
pH Scale02:41

pH Scale

79.7K
Hydronium and hydroxide ions are present both in pure water and in all aqueous solutions, and their concentrations are inversely proportional as determined by the ion product of water (Kw). The concentrations of these ions in a solution are often critical determinants of the solution’s properties and the chemical behaviors of its other solutes. Two different solutions can differ in their hydronium or hydroxide ion concentrations by a million, billion, or even trillion times. A common means of...
79.7K
Calculating the Equilibrium Constant02:46

Calculating the Equilibrium Constant

38.0K
The equilibrium constant for a reaction is calculated from the equilibrium concentrations (or pressures) of its reactants and products. If these concentrations are known, the calculation simply involves their substitution into the Kc expression.
For example, gaseous nitrogen dioxide forms dinitrogen tetroxide according to this equation:
38.0K
Calculating Standard Free Energy Changes02:49

Calculating Standard Free Energy Changes

24.9K
The free energy change for a reaction that occurs under the standard conditions of 1 bar pressure and at 298 K is called the standard free energy change. Since free energy is a state function, its value depends only on the conditions of the initial and final states of the system. A convenient and common approach to the calculation of free energy changes for physical and chemical reactions is by use of widely available compilations of standard state thermodynamic data. One method involves the...
24.9K

You might also read

Related Articles

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

Sort by
Same author

Chronic Hypertension in the ED: Physician Response When Hypertension Is or Is not a Reason for the ED Visit.

Academic emergency medicine : official journal of the Society for Academic Emergency Medicine·2026
Same author

DiffDock-Glide: A Hybrid Physics-Based and Data-Driven Approach to Molecular Docking.

Journal of chemical information and modeling·2026
Same author

An Open-Source, Open Data Approach to Activity Classification from Triaxial Accelerometry in an Ambulatory Setting.

ArXiv·2026
Same author

Nonmydriatic Ocular Fundus Imaging in Consecutive Patients With Headache in an Emergency Department.

Neurology. Clinical practice·2026
Same author

Exploration of Antiplasmodium Chemical Space Identifies New Inhibitors of β-Hematin Formation from Areas of Enrichment.

ChemMedChem·2026
Same author

Brain Trauma Foundation Guidelines for the Management of Penetrating Traumatic Brain Injury, Second Edition.

Neurosurgery·2026

Related Experiment Video

Updated: Jan 31, 2026

Determining Binding Affinity KD of Radiolabeled Antibodies to Immobilized Antigens
07:39

Determining Binding Affinity KD of Radiolabeled Antibodies to Immobilized Antigens

Published on: June 23, 2022

7.2K

High-throughput binding affinity calculations at extreme scales.

Jumana Dakka1, Matteo Turilli1, David W Wright2

  • 1Department Electrical and Computer Engineering, Rutgers University, 94 Brett Road, Piscataway, NJ, USA.

BMC Bioinformatics
|December 23, 2018
PubMed
Summary
This summary is machine-generated.

The High-throughput Binding Affinity Calculator (HTBAC) enables rapid, scalable analysis of drug-target interactions, aiding personalized cancer treatment and drug discovery by predicting binding affinity and residence time.

More Related Videos

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis
10:22

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis

Published on: August 15, 2013

31.3K
Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
15:27

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms

Published on: April 17, 2017

21.5K

Related Experiment Videos

Last Updated: Jan 31, 2026

Determining Binding Affinity KD of Radiolabeled Antibodies to Immobilized Antigens
07:39

Determining Binding Affinity KD of Radiolabeled Antibodies to Immobilized Antigens

Published on: June 23, 2022

7.2K
Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis
10:22

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis

Published on: August 15, 2013

31.3K
Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
15:27

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms

Published on: April 17, 2017

21.5K

Area of Science:

  • Computational Chemistry
  • Pharmacology
  • Bioinformatics

Background:

  • Cancer treatment effectiveness is limited by drug resistance, often due to genetic changes in target proteins.
  • Understanding molecular determinants of drug binding is crucial for overcoming resistance.
  • Molecular simulations offer insights into ligand binding free energy and residence time.

Purpose of the Study:

  • To introduce a scalable, adaptive, and automated computational tool for binding free energy calculations.
  • To enhance the flexibility and performance of molecular simulation workflows.
  • To support personalized cancer treatment and drug discovery.

Main Methods:

  • Development of the High-throughput Binding Affinity Calculator (HTBAC).
  • Utilizing a multi-stage pipeline approach for binding affinity calculations.
  • Leveraging high-performance computing resources for automated calculations.

Main Results:

  • Demonstrated near-perfect weak scaling for concurrent binding affinity calculation pipelines.
  • Achieved a rapid time-to-solution, largely independent of calculation protocol, ligand size, and simulation ensemble size.
  • Validated the performance and scalability of the HTBAC platform.

Conclusions:

  • HTBAC represents an advancement in binding affinity calculation methods and protocols.
  • The platform facilitates the study of diverse cancer drugs and ligands.
  • Enables personalized clinical decisions informed by genomic data and accelerates drug discovery.