PROTEIN STRUCTURE DETERMINATION BY SOLID-STATE NUCLEAR MAGNETIC RESONANCE (NMR)
Many proteins relevant to human disease, including membrane proteins and fibrous aggregates, cannot be examined by the traditional methods of structure determination (X-ray crystallography and solution NMR). This study proposes to leverage newly acquired state-of-the-art magic-angle spinning experiment capabilities to solve the structure of proteins associated with Parkinson's disease. The long-term objective of our research is to develop a detailed atomic-resolution structural and mechanistic understanding of protein aggregation and fibril formation. If successful, these studies will have a major impact on our understanding of protein aggregation, improving both diagnostic and therapeutic tools for neurodegenerative diseases.