Significant increases in field strength have always led to new frontiers in the scientific arenas approachable by NMR spectroscopy. Often the challenges and what has been viewed as the drawbacks to high fields have proven to some of their greatest advantages. The Series Connected Hybrid (SCH) magnet, at a field of 36T, that will become operational in the summer of 2016 at the NHMFL will provide a view into the future for NMR spectroscopy; a future in which High Temperature Superconducting (HTS) magnets will have the potential for doubling the field strengths of current Low-Temperature superconducting (LTS) magnets. The SCH magnet is a hybrid magnet having an outer superconducting coil of 13T and inner stacks of Bitter plates that will be powered by 14MW and cooled by deionized water flowing through the stacks at 1700 gal/min. The SCH magnet will be the highest homogeneity and the highest stability resistive magnet that has been constructed, but the homogeneity and stability will not be the same as that for LTS magnets. The BTRR will develop a biomedical research focus on this magnet through the development of additional technology using a cross section of scientists committed to developing and pushing the scientific frontiers of NMR spectroscopy at a field strength that is more than 50% higher than any other NMR spectrometer in the world. More than a decade of effort has now gone into developing new technologies to enhance the stability and homogeneity of this magnet. Two approaches are being taken: first, an advanced lock unit has been developed by Bruker and tested at the NHMFL and secondly, Prof. Jeffrey Schiano from Penn State has developed a cascade field regulation technology that takes advantage of an inductive pickup coil as well as NMR measurements to provide a feedback field correction. A new 1H detection HXY 1.3 mm MAS probe will be developed for structural biology solid state NMR. 1H detection has the potential to revolutionize solid state NMR in much the same way 1H detection revolutionized solution NMR 30 years ago. This revolution will open will facilitate the structural characterization of membrane proteins in lipid bilayers and potentially in native cellular membrane. This technology will be coupled with oriented samples ssNMR that provides complementary structural restraints. The signal to noise per unit of spectrometer time for spin nuclei improves with approximately B03, but for quadrupolar nuclei the rate of enhancement can be even greater due to a wide variety of factors including relaxation effects. While there are many odd halves quadrupolar nuclei in biological systems the most common and important one is 17O. Oxygen atoms are the primary sites in biological macromolecules of catalytic and functional chemistry. A goal in this effort is to work toward developing 17O spectroscopy as a routine spectroscopic tool.
