Solid-State NMR Studies of Amyloid Fibril Structure.
 

Solid-State NMR Studies of Amyloid Fibril Structure.

Solid-State NMR Studies of Amyloid Fibril Structure.

Annu Rev Phys Chem. 2010 Apr 2;

Authors: Tycko R

Current interest in amyloid fibrils stems from their involvement in neurodegenerative and other diseases and from their role as an alternative structural state for many peptides and proteins. Solid-state nuclear magnetic resonance (NMR) methods have the unique capability of providing detailed structural constraints for amyloid fibrils, sufficient for the development of full molecular models. In this article, recent progress in the application of solid-state NMR to fibrils associated with Alzheimer's disease, prion fibrils, and related systems is reviewed, along with relevant developments in solid-state NMR techniques and technology. Expected final online publication date for the Annual Review of Physical Chemistry Volume 62 is March 31, 2011. Please see http://www.annualreviews.org/catalog/pubdates.aspx for revised estimates.

PMID: 21219138 [PubMed - as supplied by publisher]



Source: PubMed