Vetenskap & teknik
Pocket
Atomic-Resolution Structures of Amyloid Fibrils by Solid-State NMR
Wasmer Christian
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Uppskattad leveranstid 7-11 arbetsdagar
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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.
- Format: Pocket/Paperback
- ISBN: 9783838130262
- Språk: Engelska
- Antal sidor: 192
- Utgivningsdatum: 2011-12-12
- Förlag: Sudwestdeutscher Verlag Fur Hochschulschriften AG