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Analysis of Cooperativity by Isothermal Titration Calorimetry

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      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.

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      THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS

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        Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice.

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          Rapid measurement of binding constants and heats of binding using a new titration calorimeter.

          A new titration calorimeter is described and results are presented for the binding of cytidine 2'-monophosphate (2'CMP) to the active site of ribonuclease A. The instrument characteristics include very high sensitivity, rapid calorimetric response, and fast thermal equilibration. Convenient software is available for instrument operation, data collection, data reduction, and deconvolution to obtain least-squares estimates of binding parameters n, delta H degree, delta S degree, and the binding constant K. Sample through-put for the instrument is high, and under favorable conditions binding constants as large as 10(8) M-1 can be measured. The bovine ribonuclease A (RNase)/2'CMP system was studied over a 50-fold range of RNase concentration and at two different temperatures. The binding constants were in the 10(5) to 10(6) M-1 range, depending on conditions, and heats of binding ca. -15,000 cal/mol. Repeat determinations suggested errors of only a few percent in n, delta H degree, and K values over the most favorable concentration range.
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            Author and article information

            Affiliations
            Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, UK; E-Mail: alan@ 123456cryst.bioc.cam.ac.uk
            Journal
            Int J Mol Sci
            ijms
            International Journal of Molecular Sciences
            Molecular Diversity Preservation International (MDPI)
            1422-0067
            August 2009
            4 August 2009
            : 10
            : 8
            : 3457-3477
            2812830
            20111687
            10.3390/ijms10083457
            ijms-10-03457
            © 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.

            This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

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