{"product_id":"atomic-resolution-structures-of-amyloid-fibrils-by-solid-state-nmr-383813026x","title":"Atomic-Resolution Structures of Amyloid Fibrils by Solid-State NMR","description":"\u003cp\u003e\u003cstrong\u003eISBN:\u003c\/strong\u003e 383813026X\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAuthor:\u003c\/strong\u003e Wasmer, Christian\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eCondition:\u003c\/strong\u003e New\u003c\/p\u003e\u003cp\u003ePrions 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 Parkinsons. 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.\u003c\/p\u003e","brand":"Mia Karts","offers":[{"title":"Default Title","offer_id":68136097120544,"sku":"NEW383813026X","price":132.22,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0980\/7426\/3840\/files\/51Is8dHHclS.jpg?v=1793806246","url":"https:\/\/miakarts.com\/products\/atomic-resolution-structures-of-amyloid-fibrils-by-solid-state-nmr-383813026x","provider":"Miakarts Books","version":"1.0","type":"link"}