Atomic resolution structures of amyloid fibrils by solid state nmr

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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.

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Oorspronkelijke releasedatum: 12 december 2011

Aantal pagina's: 192

Hoofdauteur: Wasmer Christian

Tweede Auteur: Wasmer Christian

Hoofduitgeverij: Südwestdeutscher Verlag für Hochschulschriften AG Co. KG

Product breedte: 152 mm

Product hoogte: 11 mm

Product lengte: 229 mm

Verpakking breedte: 150 mm

Verpakking hoogte: 12 mm

Verpakking lengte: 220 mm

Verpakkingsgewicht: 302 g

EAN: 9783838130262

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