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In numerous neurological diseases like AD, PD, Type 2 diabetes or prion diseases protein misfolding processes lead to protein aggregation and finally to the formation of amyloid- and amyloid-like fibrils that represent the pathological hallmark of these diseases. The exact nature of the actual cytotoxic species is still quite controversial and consequently detailed structural information for the different forms of protein aggregates and insights into the molecular mechanisms of the misfolding processes is of utmost importance for understanding the mechanisms underlying such diseases.
SDSL EPR has turned out to be one of the most powerful techniques for studying such protein aggregates and revealed valuable information especially for several filamentous aggregates being involved in neurological diseases