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 Experiment Videos

ITC in the post-genomic era...? Priceless.

Adrián Velázquez Campoy1, Ernesto Freire

  • 1Department of Biology, The Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA. adrianvc@unizar.es

Biophysical Chemistry
|March 9, 2005
PubMed
Summary

Isothermal titration calorimetry (ITC) accurately measures macromolecular interactions, crucial for understanding diseases. This technique is vital for advancing drug design and studying protein networks.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

The mitochondrial catastrophe induced by NUPR1 inhibitors as a novel strategy to fight against cancer.

Critical reviews in oncology/hematology·2025
Same author

Extrapolating differential scanning calorimetry data for monoclonal antibodies to low temperatures.

Analytical biochemistry·2024
Same author

Development of high-affinity nanobodies specific for Na<sub>V</sub>1.4 and Na<sub>V</sub>1.5 voltage-gated sodium channel isoforms.

The Journal of biological chemistry·2022
Same author

Reversibility and irreversibility in the temperature denaturation of monoclonal antibodies.

Analytical biochemistry·2021
Same author

Binding Thermodynamics to Intrinsically Disordered Protein Domains.

Methods in molecular biology (Clifton, N.J.)·2020
Same author

Synthesis of glutamic acid and glutamine peptides possessing a trifluoromethyl ketone group as SARS-CoV 3CL protease inhibitors.

Tetrahedron·2020

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Genomic data reveals numerous protein interactions critical for health and disease.
  • Accurate measurement of macromolecular interactions is essential for biological research and drug development.
  • Existing analytical techniques have limitations in characterizing diverse binding interactions.

Purpose of the Study:

  • To highlight the advantages of isothermal titration calorimetry (ITC) for characterizing intermolecular interactions.
  • To emphasize ITC's suitability for both low and high affinity binding events.
  • To project the future role of ITC in rational drug design and protein network regulation.

Main Methods:

  • Isothermal titration calorimetry (ITC) is presented as a key analytical technique.
  • ITC is described for its ability to measure binding equilibria and intermolecular interactions.
  • The technique is applicable to various macromolecular interactions, including protein/ligand, protein/protein, and protein/nucleic acid.

Main Results:

  • ITC offers advantages over other analytical methods for characterizing binding.
  • The technique accurately measures both low affinity (e.g., protein network regulation) and high affinity (e.g., drug design) interactions.
  • ITC provides high-quality data for understanding molecular interactions.

Conclusions:

  • Isothermal titration calorimetry is a reliable method for measuring macromolecular interactions.
  • ITC is versatile, applicable to a wide range of binding affinities and interaction types.
  • ITC is poised to significantly impact rational drug design and protein network regulation studies.

Related Experiment Videos