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Curr Opin Struct Biol. 2015 Feb;30:43-49. doi: 10.1016/j.sbi.2014.12.001. Epub 2014 Dec 24.

The structure of fibrils from 'misfolded' proteins.

Author information

1
Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, CH-8093 Zurich, Switzerland. Electronic address: beme@ethz.ch.
2
Institut de Biologie et Chimie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon, 7 passage du Vercors, 69367 Lyon, France. Electronic address: a.bockmann@ibcp.fr.

Abstract

Recent developments in solid-state NMR have opened the way to the structural analysis of protein fibrils, with the power of studying them at atomic resolution. Solid-state NMR is a relatively new player in the field of structural biology, and reliable approaches to successfully tackle 3D structures have been developed and applied recently. Here we discuss a number of applications to selected fibrils, including prions, α-synuclein and Amyloid-β (Aβ). The latter is, as for its small monomer size, accessible to full 3D structure determination by solid-state NMR. In addition, chemical-shift assignments, from which secondary structure can be directly be determined, is possible for much larger proteins, and has provided important insight in the structural organization of prions and other amyloids playing a central role in disease.

PMID:
25544255
DOI:
10.1016/j.sbi.2014.12.001
[Indexed for MEDLINE]

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