Book of Abstracts: Albany 2003
June 17-21 2003
Isothermal Titration Calorimetry and Differential Scanning Calorimetry: Tools to Investigate Biomolecular Interactions
Essentially all biological processes involve inter- and/or intramolecular interactions. The forces involved in these interactions are quantitated by thermodynamic parameters, and are part of the complete structure-function description of biomolecular interactions, and are used in the discovery and design of new drugs.
Isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC) are powerful techniques that directly measure the heat changes associated with biomolecular interactions. ITC measures the enthalpy change, binding constant, and stoichiometry of an intermolecular binding reaction. DSC measures the enthalpy change and thermal transition temperature of proteins, DNA, and other biopolymers. DSC is also useful in estimating binding constants of intermolecular interactions.
Overview of microcalorimetry, applications and results will be discussed. Applications include:
? Nucleic acid-nucleic acid interactions
? Protein-nucleic acid interactions
? Nucleic acid-small molecule interactions
? Target-drug interactions, QSAR
? DNA stability