We have successfully elucidated detailed structural features of a nine- amino acid peptide found in the amyloid protein of Alzheimer's disease. These features may play an critical role in the stability of the amyloid protein, and therefore in the pathology of Alzheimer's disease. More basic work has included development of what is essentially a CPMAS version of TOCSY. We call this experiment DICSY, for dipolar correlation spectroscopy. Other ongoing research includes the theory and demonstration of CPMAS experiments (i) to create rotational resonances at scaled chemical shift offsets (ii) to explore dipolar interactions involving three nuclei and (iii) to selectively invert one sideband manifold overlapping that of another nucleus.
