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-Drug Binding: Mechanism and Kinetics01:16

Protein-Drug Binding: Mechanism and Kinetics

1.8K
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,...
1.8K
Antibody Structure01:10

Antibody Structure

65.6K
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
65.6K
Enzyme Kinetics01:19

Enzyme Kinetics

104.2K
Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
104.2K
Resonance02:52

Resonance

65.6K
The Lewis structure of a nitrite anion (NO2−) may actually be drawn in two different ways, distinguished by the locations of the N-O and N=O bonds.
65.6K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

15.1K
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:
15.1K
Kinetic Energy00:23

Kinetic Energy

43.5K
Kinetic energy is the ability of an object in motion to do work or enact change. It can take on many forms. For instance, water flowing down a waterfall has kinetic energy. In biological systems, particles of light travel and are absorbed by plants to create chemical energy. Animals consume the chemical energy and give off molecules that carry their scent through the air. They also generate kinetic energy when they run away from predators. Entire systems also possess kinetic energy, like the...
43.5K

You might also read

Related Articles

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

Sort by
Same author

Enhancement in catalytic activity of CotA-laccase from Bacillus pumilus W3 via site-directed mutagenesis.

Journal of bioscience and bioengineering·2019
Same author

Characteristics and evaluation of urban soundscapes worthy of preservation.

Journal of environmental management·2019
Same author

A DNAH17 missense variant causes flagella destabilization and asthenozoospermia.

The Journal of experimental medicine·2019
Same author

[Determination of pesticide residues in wolfberry using QuEChERS-gas chromatography-tandem mass spectrometry].

Se pu = Chinese journal of chromatography·2019
Same author

Amentoflavone induces cell cycle arrest, apoptosis, and autophagy in BV-2 cells.

Frontiers in bioscience (Landmark edition)·2019
Same author

Biosynthesis of Novel Shikonin Glucosides by Enzymatic Glycosylation.

Chemical & pharmaceutical bulletin·2019

Related Experiment Video

Updated: Feb 5, 2026

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

Measuring Antibody-Antigen Binding Kinetics Using Surface Plasmon Resonance.

Stephen Hearty1,2, Paul Leonard1,2, Hui Ma1

  • 1School of Biotechnology, Dublin City University, Dublin, Ireland.

Methods in Molecular Biology (Clifton, N.J.)
|September 10, 2018
PubMed
Summary
This summary is machine-generated.

Surface plasmon resonance (SPR) enables real-time monitoring of antibody-antigen interactions without labeling. This technology efficiently screens antibody panels, identifying candidates with optimal kinetic binding characteristics.

Keywords:
AffinityAntibodyAntigenAssociation rateDissociation rateScreeningSurface plasmon resonance (SPR)

More Related Videos

Engineering Antiviral Agents via Surface Plasmon Resonance
13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

2.8K
Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
10:41

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance

Published on: January 3, 2012

13.8K

Related Experiment Videos

Last Updated: Feb 5, 2026

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
Engineering Antiviral Agents via Surface Plasmon Resonance
13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

2.8K
Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
10:41

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance

Published on: January 3, 2012

13.8K

Area of Science:

  • Biophysical techniques
  • Immunology
  • Biochemistry

Background:

  • Surface plasmon resonance (SPR) is a label-free technology widely used for studying molecular interactions.
  • It is particularly valuable for characterizing antibody-antigen interactions in real-time.
  • SPR is suitable for screening crude, unpurified antibody samples from early selection stages.

Purpose of the Study:

  • To outline generic SPR-based configurations and methodologies for antibody screening.
  • To expedite the data-rich ranking of candidate antibody panels.
  • To ensure reliable identification of antibodies with optimal kinetic binding characteristics.

Main Methods:

  • Utilizing SPR to monitor binding events between antibodies and antigens in real-time.
  • Applying SPR to analyze crude, unpurified antibody samples.
  • Employing SPR to resolve kinetic parameters (association and dissociation rate constants) and affinity data.

Main Results:

  • SPR provides concentration, affinity, and kinetic data for antibody-antigen interactions.
  • The technique allows for label-free, real-time visualization of binding events.
  • Generic SPR configurations facilitate efficient screening and ranking of antibody candidates.

Conclusions:

  • SPR is an essential technology for characterizing antibody-antigen interactions.
  • SPR-based methodologies expedite the selection of high-quality antibody candidates.
  • The technology enables the identification of antibodies with superior kinetic binding properties.