This proposal seeks funds to upgrade current electron paramagnetic resonance (EPR) equipment at the University of Florida (UF) for biomedical studies. We specifically wish to upgrade our Bruker ESP300e X-band continuous wave (CW) EPR spectrometer to a Bruker E500 X-band (9.5 GHz) and Q-band (35 GHz) CW EPR spectrometer with the variable temperature capabilities down to 1.8 K. The proposed upgrade will provide new capabilities above our current instrumentation to several research groups at UF and at the University of Central Florida (UCF). These include temperature capabilities to 1.8 K for metalloprotein EPR investigations and Q- band frequencies for enhanced spectral resolution and investigation of protein dynamics through a multi- frequency approach in natively unstructured proteins and membrane proteins. This instrument will also become part of the external users program at the National High Magnetic Field Laboratory (NHMFL) and be made available to requests world-wide through that program. In addition, this new spectrometer will relieve the burden of CW EPR experiments that are currently being performed on our single pulsed EPR spectrometer. Over ten Faculty at UF, along with outside collaborations, and two Faculty at UCF will benefit from the increased EPR time and capabilities offered by this upgrade. Several of the Faculty are within the Chemistry Department. Many are Users or collaborators from the College of Medicine;some are new faculty. The NIH funded research of biomedical systems requiring EPR experiments vary across our User base and include studies of nanoparticles, spin-trapping and dosimetry measurements with applications in radiation therapy and oxidative damage;characterization of metalloproteins and inorganic complexes involved in energy metabolism;site-directed spin- labeling (SDSL) studies of natively unstructured proteins that regulate cell cycle and are involved in oncology;SDSL studies of membrane proteins involved in lipid and nutrient transport, and SDSL studies of conformational sampling in natural polymorphisms and drug-resistant constructs of HIV-1 protease.
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