title: Isothermal titration calorimetry of membrane proteins - progress and challenges.
abstract: Integral membrane proteins, including G protein-coupled receptors (GPCR) and ion channels, mediate diverse biological functions that are crucial to all aspects of life. The knowledge of the molecular mechanisms, and in particular, the thermodynamic basis of the binding interactions of the extracellular ligands and intracellular effector proteins is essential to understand the workings of these remarkable nanomachines. In this review, we describe how isothermal titration calorimetry (ITC) can be effectively used to gain valuable insights into the thermodynamic signatures (enthalpy, entropy, affinity, and stoichiometry), which would be most useful for drug discovery studies, considering that more than 30% of the current drugs target membrane proteins. This article is part of a Special Issue entitled: Structural and biophysical characterisation of membrane protein-ligand binding.
authors.affiliation: Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, TX 77555, USA; Sealy Center for Structural Biology and Molecular Biophysics, The University of Texas Medical Branch, Galveston, TX 77555, USA. Electronic address: krrajara@utmb.edu.
authors.forename: Krishna
authors.initials: K
authors.lastname: Rajarathnam
authors.forename: Jörg
authors.initials: J
authors.lastname: Rösgen
mesh_terms: D002151:Calorimetry / Q000379:methods*; D003902:Detergents / Q000737:chemistry; D008024:Ligands; D008565:Membrane Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D003902:Detergents; D008024:Ligands; D008565:Membrane Proteins
keywords: Affinity; Drug discovery; Enthalpy; Isothermal titration calorimetry (ITC); Membrane proteins; Thermodynamics