Category

share

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

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

 

Marketed By :    Sold By :  Kamal Books International  
Delivery in :  10-12 Business Days

 
₹ 6,631

Availability: Out of stock

 

Delivery :

5% Cashback on all Orders paid using MobiKwik Wallet T&C

Free Krispy Kreme Voucher on all Orders paid using UltraCash Wallet T&C
Product Out of Stock Subscription

(Notify me when this product is back in stock)

  • Product Description
 

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.

Product Specifications
SKU :COC97523
Country of ManufactureIndia
Product BrandNot defined
Product Packaging InfoBox
In The Box1 Piece
Product First Available On ClickOnCare.com2015-08-18
0 Review(s)