Tycko R
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA.
Annu Rev Phys Chem. 2001;52:575-606. doi: 10.1146/annurev.physchem.52.1.575.
Solid state nuclear magnetic resonance (NMR) methods can provide atomic-level structural constraints on peptides and proteins in forms that are not amenable to characterization by other high-resolution structural techniques, owing to insolubility, high molecular weight, noncrystallinity, or other characteristics. Important examples include peptide and protein fibrils and membrane-bound peptides and proteins. Recent advances in solid state NMR methodology aimed at structural problems in biological systems are reviewed. The power of these methods is illustrated by experimental results on amyloid fibrils and other protein fibrils.
固态核磁共振(NMR)方法能够以其他高分辨率结构技术无法表征的形式,为肽和蛋白质提供原子水平的结构限制,这是由于其不溶性、高分子量、非结晶性或其他特性所致。重要的例子包括肽和蛋白质原纤维以及膜结合肽和蛋白质。本文综述了针对生物系统结构问题的固态NMR方法的最新进展。淀粉样原纤维和其他蛋白质原纤维的实验结果说明了这些方法的强大之处。