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

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:
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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:
Quantitative Aspects of Drug-Receptor Interaction01:30

Quantitative Aspects of Drug-Receptor Interaction

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 Kd...

You might also read

Related Articles

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

Sort by
Same author

Insight into the relationship between type IV pilus function and biofilm formation.

Biochemical Society transactions·2026
Same author

HLA micropolymorphisms confine neoantigen conformational adaptability and guide T cell receptor selectivity.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Measuring C. difficile Adhesion to Mucosal Surfaces.

Methods in molecular biology (Clifton, N.J.)·2026
Same author

An In Vitro Model for Studying Interactions Between Gastrointestinal Microbes and Planktonic and Sessile Clostridioides difficile Populations.

Methods in molecular biology (Clifton, N.J.)·2026
Same author

Dynamic Allostery in T Cell Receptor Specificity: A Role for Peptides and MHC Polymorphisms in Allosterically Tuning Immune Recognition.

BioEssays : news and reviews in molecular, cellular and developmental biology·2026
Same author

HLA micropolymorphisms confine neoantigen conformational adaptability and guide T cell receptor selectivity.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Jun 1, 2026

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens
09:53

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens

Published on: February 6, 2017

Methods for quantifying T cell receptor binding affinities and thermodynamics.

Kurt H Piepenbrink1, Brian E Gloor, Kathryn M Armstrong

  • 1Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA.

Methods in Enzymology
|May 26, 2011
PubMed
Summary

Quantifying T cell receptor (TCR) interactions with peptide-MHC ligands is crucial for understanding immune responses. This study enhances methods for accurately measuring weak TCR-ligand binding affinities, aiding research into T cell recognition. Keywords: T cell receptor, peptide-MHC, binding affinity, immune response.

More Related Videos

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity
08:45

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

Published on: September 7, 2011

Measuring TCR-pMHC Binding In Situ using a FRET-based Microscopy Assay
19:05

Measuring TCR-pMHC Binding In Situ using a FRET-based Microscopy Assay

Published on: October 30, 2015

Related Experiment Videos

Last Updated: Jun 1, 2026

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens
09:53

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens

Published on: February 6, 2017

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity
08:45

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

Published on: September 7, 2011

Measuring TCR-pMHC Binding In Situ using a FRET-based Microscopy Assay
19:05

Measuring TCR-pMHC Binding In Situ using a FRET-based Microscopy Assay

Published on: October 30, 2015

Area of Science:

  • Immunology and Molecular Biology
  • Biophysics and Biochemistry

Background:

  • Alpha-beta T cell receptors (TCRs) recognize peptide antigens presented by major histocompatibility complex (MHC) proteins, initiating cellular immune responses.
  • Accurate quantification of TCR-peptide/MHC interactions is vital for understanding T cell repertoire development and immune response propagation.

Purpose of the Study:

  • To discuss and highlight methods for quantifying the affinities and thermodynamics of soluble TCR ectodomains binding to peptide/MHC ligands.
  • To focus on enhancing the accuracy and precision of low-affinity measurements, critical for TCR-ligand interactions.

Main Methods:

  • Titration calorimetry
  • Surface plasmon resonance (SPR)
  • Fluorescence anisotropy

Main Results:

  • The study focuses on the methodologies for measuring weak-to-moderate binding affinities characteristic of TCR-ligand interactions.
  • Emphasis is placed on improving the precision and accuracy of these low-affinity measurements.

Conclusions:

  • Improved low-affinity measurement techniques will advance the understanding of T cell-mediated immune responses.
  • Enhanced measurements will facilitate studies on TCR mutants and altered peptides, revealing the physical basis of TCR recognition.