Solid-State NMR Studies of Amyloid Fibril Structure

被引:431
作者
Tycko, Robert [1 ]
机构
[1] NIDDKD, Chem Phys Lab, NIH, Bethesda, MD 20892 USA
来源
ANNUAL REVIEW OF PHYSICAL CHEMISTRY, VOL 62 | 2011年 / 62卷
关键词
Alzheimer's disease; protein structure; prion; nuclear magnetic resonance; NUCLEAR-MAGNETIC-RESONANCE; PARALLEL BETA-SHEET; PRION PROTEIN; HET-S; MOLECULAR-LEVEL; ELECTRON-MICROSCOPY; SECONDARY-STRUCTURE; CORE STRUCTURE; PEPTIDE; POLYMORPHISM;
D O I
10.1146/annurev-physchem-032210-103539
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
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.
引用
收藏
页码:279 / 299
页数:21
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