Atomic-Resolution Structures of Amyloid Fibrils by Solid-State NMR
| Preis: | 79.90 EUR* (inkl. MWST zzgl. Versand - Preis kann jetzt höher sein!) |
| Versand: | 0.00 EUR Versandkostenfrei innerhalb von Deutschland |
| Partner: | buecher.de |
| Hersteller: | Südwestdeutscher Verlag Für Hochschulschriften (Wasmer, Christian) |
| Stand: | 2015-08-04 03:50:33 |
Produktbeschreibung
Prions are infectious proteins best known as the agent of BSE and new variant Creutzfeldt-Jakob disease. Their infectious form has been identified as a beta-sheet-rich molecular aggregate termed amyloid fibril. Additionally, amyloid formation is eponymous for a group of diseases (Amyloidoses) that includes Alzheimer and Parkinson´s. Yet amyloid fibrils remain structurally poorly characterized as they are neither accessible by X-ray 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 solid-state NMR (ssNMR), currently the sole source for atomic-level structural information about amyloids. The central piece of this work was the calculation of the structure of HET-s(218-289). 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 non-infectious fibrils of HET-s, a study on a homologue of HET-s and a structural study of bacterial inclusion bodies.
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