Title
AtomicResolution Structures of Amyloid Fibrils by SolidState NMR,Used
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Prions are infectious proteins best known as the agent of BSE and new variant CreutzfeldtJakob disease. Their infectious form has been identified as a betasheetrich molecular aggregate termed amyloid fibril. Additionally, amyloid formation is eponymous for a group of diseases (Amyloidoses) that includes Alzheimer and Parkinsons. Yet amyloid fibrils remain structurally poorly characterized as they are neither accessible by Xray crystallography nor solution NMR. My PhD work comprises structural studies of amyloid fibrils of prions and the development of new tools for structure determination by solidstate NMR (ssNMR), currently the sole source for atomiclevel structural information about amyloids. The central piece of this work was the calculation of the structure of HETs(218289). This is the first known structure of an amyloid core of a prion in general. It enabled the following diverse studies on a range of subjects such as noninfectious fibrils of HETs, a study on a homologue of HETs and a structural study of bacterial inclusion bodies.
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This warranty strictly does not cover damages that arose from negligence, misuse, wear and tear, or not in accordance with product instructions (dropping the product, etc.).
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