Isothermal titration calorimetry.
Isothermal titration calorimetry is an ideal technique for measuring biological binding interactions. It does not rely on the presence of chromophores or fluorophores, nor does it require an enzymatic assay. Because the technique relies only on the detection of a heat effect upon binding, it can be used to measure the binding constant, K, the enthalpy of binding, DeltaH degrees and the stoichiometry, or number of binding sites, n. This chapter describes instrumentation, experimental design, and the theoretical underpinnings necessary to run and analyze a calorimetric binding experiment.
Lewis
Edwin A
EA
Dept. of Chemistry and Biochemistry, Northern Arizona University, Flagstaff, AZ, USA.
Murphy
Kenneth P
KP
D002151:Calorimetry / Q000295:instrumentation / Q000379:methods* / Q000706:statistics & numerical data; D003627:Data Interpretation, Statistical; D066298:In Vitro Techniques; D008024:Ligands; D017711:Nonlinear Dynamics; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D012996:Solutions; D013816:Thermodynamics
D008024:Ligands; D011506:Proteins; D012996:Solutions