The structure of fibrils from 'misfolded' proteins.

Meier BH; Böckmann A

doi:10.1016/j.sbi.2014.12.001

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Journal article

The structure of fibrils from 'misfolded' proteins.

Meier BH Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, CH-8093 Zurich, Switzerland. Electronic address: beme@ethz.ch.
Böckmann A 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.

2014-12-30

Published in:

Current opinion in structural biology. - 2015

Nuclear Magnetic Resonance, Biomolecular

English 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.

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