A survey of the year 2002 literature on applications of isothermal titration calorimetry

Abstract

Isothermal titration calorimetry (ITC) is becoming widely accepted as a key instrument in any laboratory in which quantification of biomolecular interactions is a requisite. The method has matured with respect to general acceptance and application development over recent years. The number of publications on ITC has grown exponentially over the last 10 years, reflecting the general utility of the method. Here all the published works of the year 2002 in this area have been surveyed. We review the broad range of systems to which ITC is being directed and classify these into general areas highlighting key publications of interest. This provides an overview of what can be achieved using this method and what developments are likely to occur in the near future.

Modulation of the Leishmania donovani Peroxin 5 Quaternary Structure by Peroxisomal Targeting Signal 1 Ligands

“…To further characterize the LdPEX5-PTS1 interaction, we used ITC to determine the stoichiometry, the number of AKL PTS1 peptide molecules bound to each LdPEX5 subunit, and the K d for the LdPEX5-AKL PTS1, ldpex5 ⌬269-291-AKL PTS1, and His 6 -CT-ldpex5-AKL PTS1 complexes (9,31). The For all LdPEX5 variants, the molar ratio of peptideLdPEX5 subunit was measured to be ϳ1:1.…”

Thermodynamic Signatures of Macromolecular Complexes ‒ Insights on the Stability and Interactions of Nucleoplasmin, a Nuclear Chaperone

“…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.…”

“…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].…”

Water-Soluble Calix[4]arene Derivatives: Binding Stoichiometry and Spectroscopic Evaluation of the Host-Guest Recognition Mechanism

“…20,21,22 The gradient of the ITC curve can be fitted to determine the binding constant and ΔG complex . Integration of the total area under the ITC plot gives the complexation enthalpy (ΔH complex )which allows for all the system thermodynamic parameters evaluation, being ΔG complex = ΔH complex -TΔS complex .…”