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Analysis of Cooperativity by Isothermal Titration Calorimetry

Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, UK
Int. J. Mol. Sci. 2009, 10(8), 3457-3477; https://doi.org/10.3390/ijms10083457
Received: 10 June 2009 / Revised: 28 July 2009 / Accepted: 31 July 2009 / Published: 4 August 2009
(This article belongs to the Special Issue 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. View Full-Text
Keywords: isothermal titration calorimetry; stoichiometry; cooperativity; multiprotein complexes; thermodynamics; global analysis; NMR isothermal titration calorimetry; stoichiometry; cooperativity; multiprotein complexes; thermodynamics; global analysis; NMR
MDPI and ACS Style

Brown, A. Analysis of Cooperativity by Isothermal Titration Calorimetry. Int. J. Mol. Sci. 2009, 10, 3457-3477.

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