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Solid-State NMR Studies of Amyloid Fibril Structure.

Authors :
Tycko, Robert
Source :
Annual Review of Physical Chemistry; May2011, Vol. 62, p279-299, 16p, 5 Diagrams, 1 Graph
Publication Year :
2011

Abstract

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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
0066426X
Volume :
62
Database :
Complementary Index
Journal :
Annual Review of Physical Chemistry
Publication Type :
Academic Journal
Accession number :
59700533
Full Text :
https://doi.org/10.1146/annurev-physchem-032210-103539