MOLECULAR STUDIES BY SOLID-STATE NMR

我们已经成功地阐明了一个九- 在阿尔茨海默病的淀粉样蛋白中发现的氨基酸肽。 这些特征可能在淀粉样蛋白的稳定性中起关键作用 蛋白质，因此在阿尔茨海默病的病理学。 更 基本工作包括开发基本上是CPMAS版本的内容 关于TOCSY。 我们称这个实验为DICSY，表示偶极相关 谱 其他正在进行的研究包括理论和 演示CPMAS实验（i）在2000 - 2005年期间产生旋转共振， 定标化学位移补偿（ii）探索偶极相互作用 涉及三个核和（iii）选择性地反转一个边带 与另一个原子核重叠的流形

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.