Analysis of cooperativity by isothermal titration calorimetry.
Cooperative binding pervades Nature. This review discusses the use of isothermal titration calorimetry (ITC) in the identification and characterisation of cooperativity in biological interactions. ITC has broad scope in the analysis of cooperativity as it determines binding stiochiometries, affinities and thermodynamic parameters, including enthalpy and entropy in a single experiment. Examples from the literature are used to demonstrate the applicability of ITC in the characterisation of cooperative systems.
Brown
Alan
A
Department of Biochemistry, University of Cambridge, UK. alan@cryst.bioc.cam.ac.uk
D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D002151:Calorimetry; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D050556:Fatty Acid-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D005768:Gastrointestinal Hormones / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D013816:Thermodynamics; D013880:Thioredoxin-Disulfide Reductase / Q000737:chemistry / Q000378:metabolism
D019843:Archaeal Proteins; D004268:DNA-Binding Proteins; D050556:Fatty Acid-Binding Proteins; D005768:Gastrointestinal Hormones; D008024:Ligands; C057275:fatty acid-binding protein 6; C095116:Sac7 protein, Sulfolobus; D004247:DNA; D013880:Thioredoxin-Disulfide Reductase