engleski

Studying Proteomics with Microcalorimetry

Essentially all biological processes involve inter- and intramolecular interactions. The forces involved in these interactions are quantitated by thermodynamic parameters. Beyond thermodynamics, binding kinetics also provide a measure of the strength and nature of these interactions, which is critical to understanding the complete structure-function description of biomolecular interactions. Microcalorimetry is an ultrasensitive technique that provides direct observations of thermal changes in a sample during these interactions. Differential scanning calorimetry (DSC) is used to study intramolecular interactions, such as protein unfolding and stability. Isothermal Titration Calorimetry (ITC) measures the enthalpy change, binding affinity, and stoichiometry of an intermolecular binding reaction, such as a protein-ligand or antibody- antigen interaction. This presentation will outline how these techniques are used in basic research, and drug discovery and development. We will also discuss how the data from these techniques can be combined with other biophysical characterization tools to better understand the implications of these properties on your research.

microcalorimetry, proteomics, biomolecular interactions

Malvern Panalytical Inc.