Int. J. Mol. Sci. 2009, 10(8), 3457-3477; doi:10.3390/ijms10083457

Analysis of Cooperativity by Isothermal Titration Calorimetry

Received: 10 June 2009; in revised form: 28 July 2009 / Accepted: 31 July 2009 / Published: 4 August 2009
(This article belongs to the Special Issue Isothermal Titration Calorimetry)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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.

AMA Style

Brown A. Analysis of Cooperativity by Isothermal Titration Calorimetry. International Journal of Molecular Sciences. 2009; 10(8):3457-3477.

Chicago/Turabian Style

Brown, Alan. 2009. "Analysis of Cooperativity by Isothermal Titration Calorimetry." Int. J. Mol. Sci. 10, no. 8: 3457-3477.

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