Characterizing Thermodynamics of Protein-Glycosaminoglycan Interactions Using Isothermal Titration Calorimetry

• Published in: Methods in molecular biology (Clifton, N.J.) Vol. 2303; p. 307
• Main Authors: Dutta, Amit K, Sepuru, Krishna Mohan, Rösgen, Jörg, Rajarathnam, Krishna
• Format: Journal Article
• Language: English
• Published: United States 2022
• Subjects: Calorimetry; Entropy; Glycosaminoglycans; Protein Binding; Thermodynamics; Thermodynamics; Enthalpy; Glycosaminoglycan (GAG); Isothermal titration calorimetry (ITC); Entropy; Heparin; Free energy
• DOI: 10.1007/978-1-0716-1398-6_25

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.