Duke University proposes to replace, update, and enhance ts 800 MHz NMR spectroscopy system with a new console and pumped magnet monitoring data logger. The 800 MHz spectrometer is housed in and managed by the Duke NMR Spectroscopy Center which serves as an NMR resource for all university research projects at Duke and for scientists at universities and government laboratories in the Research Triangle and the Southeastern region. It supports frontier research in basic biochemical and biomedical sciences. The requested new equipment components are needed to replace original equipment installed with the system over 10 years ago, that is now failing at an unacceptable rate. This has significantly impacted research activities of numerous investigators who depend on the Duke 800 instrument to pursue their funded projects and who were already using it in the range of 90-95% of a 24/7 schedule, year around within 4 years of installation. Currently, however, the available time has been more limited due to unanticipated maintenance and repairs associated with failure of critical components as they have aged. This limitation in the instrument time available for research is compounded by the fact that the Varian Inova console and magnet monitoring system are no longer manufactured, having been replaced by a new generation spectrometer and cryogen monitoring system. New parts for our system in some cases are no longer available, and refurbished, used parts are often not immediately available, either. The new equipment components requested for our 800 MHz NMR system provide a cost effective strategy to restore this heavily used and unique spectrometer in this region to its designed capability at a fraction of the cost of a new system. In addition, replacement of the magnet monitoring system protects the investment in our pumped 18.9 Tesla NMR magnet valued at greater than $1M. Current research activities in the following areas will be enhanced by this upgrade to the Duke 800: studies of protein assemblies;protein conformational dynamics and folding;membrane associated lipids and enzymes involved in their synthesis;enzyme structural characterization and redesign;in-cell NMR spectroscopy of proteins;antibody recognition of immunogenic peptides and phospholipids associated with HIV vaccine design;cellular signaling;and methods development for rapid acquisition of multidimensional NMR data.
