Characterizing Thermodynamics of Protein-Glycosaminoglycan Interactions Using Isothermal Titration Calorimetry

Amit K. Dutta, Krishna Mohan Sepuru, Jörg Rösgen, Krishna Rajarathnam

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations


It has now become increasingly clear that a complete atomic description of how biomacromolecules recognize each other requires knowledge not only of the structures of the complexes but also of how kinetics and thermodynamics drive the binding process. In particular, such knowledge is lacking for protein-glycosaminoglycan (GAG) complexes. Isothermal titration calorimetry (ITC) is the only technique that can provide all of the thermodynamic parameters—enthalpy, entropy, free energy (binding constant), and stoichiometry—from a single experiment. Here we describe different factors that must be taken into consideration in carrying out ITC titrations to obtain meaningful thermodynamic data of protein-GAG interactions.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Number of pages11
StatePublished - Jan 2022
Externally publishedYes

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029


  • Enthalpy
  • Entropy
  • Free energy
  • Glycosaminoglycan (GAG)
  • Heparin
  • Isothermal titration calorimetry (ITC)
  • Thermodynamics

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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