Survey of the year 2009: applications of isothermal titration calorimetry
Article first published online: 14 DEC 2010
Copyright © 2010 John Wiley & Sons, Ltd.
Journal of Molecular Recognition
Volume 24, Issue 1, pages 1–16, January/February 2011
How to Cite
Falconer, R. J. and Collins, B. M. (2011), Survey of the year 2009: applications of isothermal titration calorimetry. J. Mol. Recognit., 24: 1–16. doi: 10.1002/jmr.1073
- Issue published online: 30 DEC 2010
- Article first published online: 14 DEC 2010
- Manuscript Accepted: 9 JUL 2010
- Manuscript Revised: 8 JUL 2010
- Manuscript Received: 10 MAY 2010
- enzyme kinetics;
- free energy;
- heat capacity;
Isothermal titration calorimetry (ITC) is now an established and invaluable method for determining the thermodynamic constants, association constant and stoichiometry of molecular interactions in aqueous solutions. The technique has become widely used by biochemists to study protein interaction with other proteins, small molecules, metal ions, lipids, nucleic acids and carbohydrates; and nucleic acid interaction with small molecules. The drug discovery industry has utilized this approach to measure protein (or nucleic acid) interaction with drug candidates. ITC has been used to screen candidates, guide the design of potential drugs and validate the modelling used in structure-based drug design. Emerging disciplines including nanotechnology and drug delivery could benefit greatly from ITC in enhancing their understanding and control of nano-particle assembly, and drug binding and controlled release. Copyright © 2010 John Wiley & Sons, Ltd.