Acquisition of a 500 MHz NMR Spectrometer and Establishment of the Mississippi Resonance Facility

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This award from the Academic Research Infrastructure Program will help the Department of Chemistry at Mississippi State University acquire a 500 MHz spectrometer which will be used in research. The research activity to be supported includes NMR studies of the conformation of derivatives of vitamin B12 in solution, bound to a vitamin B12 binding protein, and bound to a coenzyme B12 requiring enzyme. Also to be studied are the solution conformation of catalytically active fragments (5-10 kDa) of the enzyme glutamine cyclotransferase in the presence and absence of enzyme inhibitors; the distribution of leaf chloroplast water and the effects of environmental parameters on leaf chloroplast osmoregulation; conformation and tautomeric equilibria in carboxylic acids, tin carbamates, N-alkyl formamides, alkyl thioformates, alkyl thionitriles, N-tert-butylnitramine and N-tert-butylformamide; chloroheptafluorodirhenium dianion; cis-and trans-cyclodecene by 1H, 13C, 17O, and 19F NMR spectroscopy; the geometry and dynamics of the reversible binding of anilinoacridines and the geometry of the covalent binding of photo affinity probes; and the solution structure of the 49 amino acid residue neuropeptide, corticotropin-releasing factor and the conformational changes thereof. %%% Nuclear Magnetic Resonance (NMR) spectroscopy is the most powerful tool available to chemists for the elucidation of the structure of molecules. It is used to identify unknown substances, characterize specific arrangements of atoms within molecules, and to study the dynamics of interactions between molecules in solution. Access to state-of-the-art NMR spectrometry is essential to chemists who are carrying out frontier research. The results from these NMR studies are useful in areas such as polymers and catalysis, and in biology.