With this award from the Major Research Instrumentation program (MRI), the Department of Chemistry and Biochemistry at Miami University at Oxford will acquire a pulsed EPR spectrometer. The pulsed EPR spectrometer will be utilized in several research projects including 1) structural characterization of membrane proteins, 2) structural determination of Metallo-â-lactamases, 3) structural determination and binding of ATP and/or DNA to the Cohesin Complex, 4) structural properties of various HMGA1/DNA/protein complexes, and 5) characterization of several unique nanostructured artificial enzymes/proteins. This would be the first pulsed EPR spectrometer placed at an academic institution in the state of Ohio and access would be expanded to include six other academic institutions in the state of Ohio.
An electron paramagnetic resonance (EPR) spectrometer yields information on the molecular and electronic structure of molecules. It may also be used to obtain information about the lifetimes of free radicals, short-lived species that are often essential for the initiation of tumor growth and/or a variety of chemical reactions. Pulsed electron paramagnetic resonance (EPR) methods such as pulsed ENDOR, have been successfully utilized to investigate the local structure and dynamics of paramagnetic centers in biological samples. Different pulsed EPR methods allow different contributions to the EPR spectra to be distinguished and can help unravel complicated EPR spectra consisting of overlapping resonance lines, often found in disordered protein samples.
