Spin Labeling Analysis of Amyloids and Other Protein Aggregates

摘要: Abstract Because of the enormous size amyloid fibrils and their low tendency to form crystal lattices, it has been difficult obtain high‐resolution structural information on these aggregates. Magnetic resonance methods, such as solid‐state nuclear magnetic spectroscopy electron paramagnetic (EPR) spectroscopy, are promising new technologies by which molecular models. This chapter will focus application EPR amyloids other protein Site‐directed spin labeling (SDSL), in combination with successfully used study structure dynamics soluble well membrane proteins. Recent studies indicate that this strategy is also suited for studying fibrils. For example, an important outcome SDSL performed our laboratory β, islet polypeptide, α‐synuclein, tau have β‐strands aligned in‐register, parallel fashion. Future promise yield about fibril topography protofilament arrangement can be extended include oligomeric structures.