This proposal requests continuation funding for our research on applications of pulse shaping in the nuclear magnetic resonance (NMR) spectroscopy of biological molecules. Our group has helped to pioneer a number of applications in this field, with emphasis in the last grant period on complex multilevel spin systems such as proteins in concentrated solvents. We have also found exciting experimental results which have upset much of the theoretical foundation of NMR- we have transferred coherence between concentrated solvent and dilute solute molecules in solution, including a 20 mM glycoprotein in water. The proposed work extends our current work with presaturation pulses and sequences for improving cross-peak intensities in multidimensional experiments. It also continues our experimental and theoretical investigations of the effects of coherence transfer from the intense water magnetization to biomolecules in water, with the goal of understanding and exploiting these effects for enhanced sensitivity. At a minimum, the work will improve solvent suppression sequences; but based on our current experiments and calculations, which accurately simulate these unexpected results using radiation damping and the dipolar demagnetizing field, we expect to dramatically enhance multidimensional NMR spectra of dilute solutions of proteins in water, with techniques such as cross-polarization between solute and solvent, or relayed coherence transfer between ends of a protein.
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