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Qinghua Wang
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My current research is focused on investigating protein aggregation-prone conformations and the effect of cellular environment on protein conformations and dynamics. Protein misfolding and aggregation is involved in many genetically linked or inherited neurodegenerative diseases such as Huntington's and Alzheimer's disease. Although it is known that many amyloid fibrils adopt a cross-β structure, few conformations are available for aggregation-prone protofibrillar states, which may be more directly tied to pathogenesis. By use of a novel NMR technique named relaxation dispersion experiments, I am investigating the aggregation-prone conformation of a well-characterized model β-sheet protein, Cellular Retinoic Acid-Binding Protein I (CRABP I), as a test case to develop methods and understand aggregation mechanisms more fully. Furthermore, I am applying in-cell NMR techniques to characterize protein conformations inside living cells to study the effect of cellular environment on protein conformations and dynamics. The outcome of this research should shed light on molecular mechanism of protein misfolding diseases in structural details and provide new avenues for therapeutic strategies.
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