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Biophys Chem. 2016 Mar;210:14-26. doi: 10.1016/j.bpc.2015.07.003. Epub 2015 Jul 16.

Solid-state NMR: An emerging technique in structural biology of self-assemblies.

Author information

1
Institute of Chemistry & Biology of Membranes & Nanoobjects (UMR5248 CBMN), CNRS, Universite Bordeaux, Institut Polytechnique Bordeaux, All. Geoffroy Saint-Hilaire, 33600 Pessac, France. Electronic address: b.habenstein@iecb.u-bordeaux.fr.
2
Institute of Chemistry & Biology of Membranes & Nanoobjects (UMR5248 CBMN), CNRS, Universite Bordeaux, Institut Polytechnique Bordeaux, All. Geoffroy Saint-Hilaire, 33600 Pessac, France. Electronic address: a.loquet@iecb.u-bordeaux.fr.

Abstract

Protein self-assemblies are ubiquitous biological systems involved in many cellular processes, ranging from bacterial and viral infection to the propagation of neurodegenerative disorders. Studying the atomic three-dimensional structures of protein self-assemblies is a particularly demanding task, as these systems are usually insoluble, non-crystalline and of large size. Solid-state NMR (ssNMR) is an emerging method that can provide atomic-level structural data on intact macromolecular assemblies. We here present recent progress in magic-angle spinning ssNMR to study protein assemblies and give an overview on its combination with complementary techniques such as cryo-EM, mass-per-length measurements, SAXS and X-ray diffraction. Applications of ssNMR on its own and in hybrid approaches have revealed precious atomic details and first high-resolution structures of complex biological assemblies, including amyloid fibrils, bacterial filaments, phages or virus capsids.

KEYWORDS:

Amyloid fibril; Bacterial filament; Hybrid structure determination; Protein supramolecular assembly; Solid-state NMR spectroscopy

PMID:
26234527
DOI:
10.1016/j.bpc.2015.07.003
[Indexed for MEDLINE]

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