By Dr. John J. Correia and Dr. H. William Detrich, III (Eds.)
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Additional info for Biophysical Tools for Biologists, Volume One: In Vitro Techniques
C. (1997). Optical absorbance and fluorescence techniques for measuring drug-DNA interactions. In ‘‘Drug-DNA Interaction Protocols’’ (K. R. ), Vol. 90, pp. 195–218. Humana Press, Totowa, NJ. Klotz, I. M. (1997). ’’ John Wiley & Sons, New York. Lee, J. , Latimer, L. , and Hampel, K. J. (1993). C (þ)-containing DNA triplexes. Biochemistry 32, 5591–5597. , Chaires, J. , and Waring, M. J. (2003). Energetics of echinomycin binding to DNA. Nucleic Acids Res. 31, 6191–6197. LePecq, J. , and Paoletti, C.
Curr. Opin. Chem. Biol. 3, 694–704. Weber, G. (1992). ’’ Chapman & Hall, New York. , Brandts, J. , and Lin, L. N. (1989). Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179, 131–137. , and Gill, S. J. (1990). ’’ University Science Books, Mill Valley, CA. , and Zhang, Z. Y. (1998). Low-aYnity binding determined by titration calorimetry using a high-aYnity coupling ligand: A thermodynamic study of ligand binding to protein tyrosine phosphatase 1B.
All that is required for a protein–ligand interaction to be amenable to ITC measurement is a heat signal, either absorption or release, upon binding. Moreover, if this signal is not observed under one set of conditions of temperature, pH, or buVering agent, a change of these conditions may yield a signal. As with any other binding method, the ligand is injected into a solution of the protein and the heat evolved or taken up is monitored as a function of ligand concentration until saturation is reached.
Biophysical Tools for Biologists, Volume One: In Vitro Techniques by Dr. John J. Correia and Dr. H. William Detrich, III (Eds.)