Characterizing Thermodynamics of Protein-Glycosaminoglycan Interactions Using Isothermal Titration Calorimetry

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 pro...

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Bibliographic Details
Published inMethods 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
LanguageEnglish
Published United States 2022
Subjects
Calorimetry
Entropy
Glycosaminoglycans
Protein Binding
Thermodynamics
Thermodynamics
Enthalpy
Glycosaminoglycan (GAG)
Isothermal titration calorimetry (ITC)
Entropy
Heparin
Free energy
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Summary: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.
ISSN:1940-6029
DOI:10.1007/978-1-0716-1398-6_25