title: Using isothermal titration calorimetry to determine thermodynamic parameters of protein-glycosaminoglycan interactions.
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.
authors.affiliation: Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, TX, 77555, USA.
authors.forename: Amit K
authors.initials: AK
authors.lastname: Dutta
authors.forename: Jörg
authors.initials: J
authors.lastname: Rösgen
authors.forename: Krishna
authors.initials: K
authors.lastname: Rajarathnam
mesh_terms: D000818:Animals; D002151:Calorimetry / Q000379:methods*; D002417:Cattle; D003198:Computer Simulation; D006025:Glycosaminoglycans / Q000378:metabolism*; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D013223:Statistics as Topic; D034421:Sus scrofa; D013816:Thermodynamics
chemical_list: D006025:Glycosaminoglycans; D011506:Proteins