NIH Research Festival
Isothermal titration calorimetry experiments provide unique and detailed information of the thermodynamic properties of macromolecular interactions, which is particularly important for studying reversible multi-protein complex formation. The multi-valent binding and cooperativity in such complexes are the key driving forces of their physiological functions. However, such information usually cannot be directly obtained from a single experiment or even multiple ones due to limited number of signals contributed from multiple species. In order to understand these systems and resolve the multiple thermodynamic states, it is critical to exploit global analysis strategy, not only for ITC, but also for the combination of data from ITC and other biophysical techniques. The computational programs, ITCsy and SEDPHAT are designed for this purpose and allow for global analysis of multiple data sets from ITC and multiple methods respectively. In both programs, powerful simulation and statistical tools allow one to select a variety of binding schemes, generate multiple data sets for multiple biophysical methods and explore their information content, as well as the confidence in the thermodynamic parameter of interest. With these advantages of ITCsy and SEDPHAT, one can decompose the signal contributions from different species, examine their fractional population under different conditions and finally optimize the experimental design to obtain maximum information. Therefore, the complicated multi-component system can be much more approachable than before with better precision and resolution for the thermodynamic properties.
Scientific Focus Area: Biomedical Engineering and Biophysics
This page was last updated on Friday, March 26, 2021