A survey of the year 2007 literature on applications of isothermal titration calorimetry.
Elucidation of the energetic principles of binding affinity and specificity is a central task in many branches of current sciences: biology, medicine, pharmacology, chemistry, material sciences, etc. In biomedical research, integral approaches combining structural information with in-solution biophysical data have proved to be a powerful way toward understanding the physical basis of vital cellular phenomena. Isothermal titration calorimetry (ITC) is a valuable experimental tool facilitating quantification of the thermodynamic parameters that characterize recognition processes involving biomacromolecules. The method provides access to all relevant thermodynamic information by performing a few experiments. In particular, ITC experiments allow to by-pass tedious and (rarely precise) procedures aimed at determining the changes in enthalpy and entropy upon binding by van't Hoff analysis. Notwithstanding limitations, ITC has now the reputation of being the "gold standard" and ITC data are widely used to validate theoretical predictions of thermodynamic parameters, as well as to benchmark the results of novel binding assays. In this paper, we discuss several publications from 2007 reporting ITC results. The focus is on applications in biologically oriented fields. We do not intend a comprehensive coverage of all newly accumulated information. Rather, we emphasize work which has captured our attention with originality and far-reaching analysis, or else has provided ideas for expanding the potential of the method.
Bjelić
Sasa
S
Biochemisches Institut der Universität Zürich, Winterthurerstrasse 190, Zürich, Switzerland.
Jelesarov
Ilian
I
D002138:Calibration; D002151:Calorimetry / Q000295:instrumentation / Q000379:methods; D015195:Drug Design; D004734:Energy Metabolism / Q000502:physiology; D004789:Enzyme Activation / Q000502:physiology; D007700:Kinetics; D008024:Ligands; D008962:Models, Theoretical; D009696:Nucleic Acids / Q000378:metabolism; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D017186:Titrimetry / Q000295:instrumentation / Q000379:methods
D008024:Ligands; D009696:Nucleic Acids; D011506:Proteins