@inbook{d9249f64d4f545c2bb956f9015f89262,
title = "Characterizing Thermodynamics of Protein-Glycosaminoglycan Interactions Using Isothermal Titration Calorimetry",
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 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.",
keywords = "Enthalpy, Entropy, Free energy, Glycosaminoglycan (GAG), Heparin, Isothermal titration calorimetry (ITC), Thermodynamics",
author = "Dutta, {Amit K.} and Sepuru, {Krishna Mohan} and J{\"o}rg R{\"o}sgen and Krishna Rajarathnam",
note = "Publisher Copyright: {\textcopyright} 2022, Springer Science+Business Media, LLC, part of Springer Nature.",
year = "2022",
doi = "10.1007/978-1-0716-1398-6_25",
language = "English (US)",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "307--317",
booktitle = "Methods in Molecular Biology",
}