2008
DOI: 10.1002/jmr.909
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A survey of the year 2007 literature on applications of isothermal titration calorimetry

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Cited by 59 publications
(44 citation statements)
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“…ITC is most commonly used to study the interaction between small ligands, or protein interactions with DNA in drug therapy, see, e.g., Bjelic and Jelesarov. 34 Here, the interaction between xanthan and a chitosan polymer, a polymer-polymer interaction, is compared with the interaction between xanthan and a tri-glucosamine. The various chain lengths of the cationic component are expected to represent different valencies in the possible lattice-like type interactions.…”
Section: Introductionmentioning
confidence: 99%
“…ITC is most commonly used to study the interaction between small ligands, or protein interactions with DNA in drug therapy, see, e.g., Bjelic and Jelesarov. 34 Here, the interaction between xanthan and a chitosan polymer, a polymer-polymer interaction, is compared with the interaction between xanthan and a tri-glucosamine. The various chain lengths of the cationic component are expected to represent different valencies in the possible lattice-like type interactions.…”
Section: Introductionmentioning
confidence: 99%
“…Extensive reviews have been published on the basic thermodynamic formalism, calorimeters' design and application of DSC [17][18][19][20] and ITC [18,[20][21][22][23][24]. Moreover, surveys on ITC application are published annually since 2002 [25][26][27][28]. Calorimetry on proteins in general will be briefly summarized here and examples for NP will be thoroughly reviewed.…”
Section: Calorimetry: Protein Folding/unfolding and Binding Energeticsmentioning
confidence: 99%
“…Recently a protocol for novel application of the technique has been elaborated, in which ITC is used as a tracking tool, combined with chromatography, for identification of target protein in biomolecular mixture [77] and it has been suggested to be valuable when the target protein or ligand is unknown. References for the wide spectrum and examples of novel applications of ITC can be found in the surveys published each year in the Journal of Molecular Recognition [25][26][27][28].…”
Section: Calorimetry: Protein Folding/unfolding and Binding Energeticsmentioning
confidence: 99%
“…The binding constant K b (and therefore the binding free energy DG ) is determined by nonlinear fitting of the curve described by the heat signals decreasing during the experiment. Once DG and DH are determined, the entropy change (DS) associated with the interaction can be calculated [59,60]. Prediction of these values has proven to be difficult due to numerous contributions arising from protein, ligand, and solvent molecules.…”
Section: Experimental Approaches For Analyzing Water Moleculesmentioning
confidence: 99%
“…The key problem for rational drug design is to identify reliable correlations between structure, energetics, and dynamics. The possibility of detecting the full thermodynamic profile of an interaction within a few experiments leads to the establishment of ITC as standard for validating theoretical predictions of thermodynamic parameters [60].…”
Section: Experimental Approaches For Analyzing Water Moleculesmentioning
confidence: 99%