Using isothermal titration calorimetry to determine thermodynamic parameters of protein–glycosaminoglycan interactions

Amit K. Dutta, Jörg Rösgen, Krishna Rajarathnam

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

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 various 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)
Pages (from-to)315-324
Number of pages10
JournalMethods in Molecular Biology
Volume1229
DOIs
StatePublished - Jan 1 2015
Externally publishedYes

Keywords

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

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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