Christian Wasmer

Atomic-Resolution Structures of Amyloid Fibrils by Solid-State NMR

• Broschiertes Buch

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.

Produktdetails

• Verlag: Südwestdeutscher Verlag für Hochschulschriften
• Aufl.
• Seitenzahl: 192
• Erscheinungstermin: 5. Juli 2015
• Englisch
• Abmessung: 220mm x 150mm x 13mm
• Gewicht: 304g
• ISBN-13: 9783838130262
• ISBN-10: 383813026X
• Artikelnr.: 34638377

Autorenporträt

After the Abitur in Germany, Christian Wasmer studied Physics at the ETH in Zürich. He did his diploma work with Prof. K. Wüthrich on structural biology and his Ph.D. studies with Prof. B. H. Meier at ETH Zürich (this work). He obtained his doctoral degree in 2011 and now works as a research fellow at the Harvard Medical School in Boston, MA, USA.