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Analysis of Cooperativity by Isothermal Titration Calorimetry
Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, UK
Received: 10 June 2009; in revised form: 28 July 2009 / Accepted: 31 July 2009 / Published: 4 August 2009
Abstract: 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.
Keywords: isothermal titration calorimetry; stoichiometry; cooperativity; multiprotein complexes; thermodynamics; global analysis; NMR
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MDPI and ACS Style
Brown, A. Analysis of Cooperativity by Isothermal Titration Calorimetry. Int. J. Mol. Sci. 2009, 10, 3457-3477.
Brown A. Analysis of Cooperativity by Isothermal Titration Calorimetry. International Journal of Molecular Sciences. 2009; 10(8):3457-3477.
Brown, Alan. 2009. "Analysis of Cooperativity by Isothermal Titration Calorimetry." Int. J. Mol. Sci. 10, no. 8: 3457-3477.