UNC Acqusition of an Auto-iTC200 Isothermal Titration Calorimeter System

Project: Research project


The Macromolecular Interactions Facility, also called the "Mac-In-Fac" (web address: http://hekto.med.unc.edu:8080/macinfac/) is a core biophysical laboratory of the University of North Carolina at Chapel Hill. In operation since 1996, it provides state-of-the art instrumentation and resources for biophysical characterization of interactions of biological macromolecules. The capabilities include measurement of affinity, stoichiometry, kinetics and thermodynamics of interactions among proteins, DNA and their cognate ligands. Resources exist for analyzing the biophysical characteristics of molecular weight, shape, and conformations of proteins and DNA; and for exploring bimolecular interactions in real-time. The facility is open to all researchers in the Triangle area on a first-come-first-serve basis.

The equipment includes a surface plasmon resonance-based biosensor (Biacore 2000), a Beckman Optima XL-I Analytical Ultracentrifuge (AUC) with scanning UV/VISIBLE, and interference optics, a Beckman Optima XL-F Analytical Ultracentrifuge fitted with AVIV fluorescence detection system, Microcal differential scanning and isothermal titration calorimeters, a SPEX Fluorolog research spectrofluorometer, Applied Photophysics and Aviv circular dichroism spectropolarimeters, and a Wyatt multi angle light scattering system connected to a size-exclusion column. There are no similar facilities on the UNC Chapel Hill Campus, or nearby institutions. Its current users come from many departments on the UNC Chapel Hill campus belonging to Schools of Arts and Sciences, Medicine and Pharmacy (Biochemistry & Biophysics, Biology, Cell Biology, Cell and Molecular Physiology, Chemistry, Medicinal Chemistry, Microbiology & Immunology, Pathology, and Pharmacology), other universities from North Carolina (North Carolina State University and Duke University) and several North Carolina based biotechnology companies (Biolex , Encelle, and BD Technologies). Users from Wake Forest University and the National Institutes of Environmental Health Sciences (NIEHS) in Research Triangle Park and other Triangle-based biotechnology companies have also used our facility in the past.

Isothermal titration calorimetry is a very elegant and powerful technique for exploring receptor-ligand interactions and enzyme kinetics in solution by measuring the amount of heat released or taken up during the reaction. Our existing instrument (a Microcal VP-ITC) is a very widely used instrument in our facility. However, it requires very large quantities of samples to carry out the experiments. This has prevented the full exploitation of this technique. Very recently Microcal Inc. has come up with a revolutionary version of this instrument (ITC200), which requires only one-tenth of the samples needed in the previous model to carry out an experiment, and has a higher sensitivity. Additionally, in the fully-automatic mode (not available in the previous model) it can run 50 samples per day and upto 384 samples unattended. Acquisition of this new-generation of ITC will greatly enhance the research of many investigators who already use or plan to use our facility.
Effective start/end date2/1/081/31/09


  • North Carolina Biotechnology Center (NCBC)


Enzyme kinetics
Surface plasmon resonance
Light scattering